************************************************************************ ********** REPORT OF PROTEIN ANALYSIS by the WHAT IF program ********** ************************************************************************ Date : 2005-03-09 This report was created by WHAT IF version 20050215-1726 INTRODUCTION ------------ This document contains a report of findings by the WHAT IF program during the analysis of one or more proteins. It contains a separate section for each of the proteins that have been analysed. Each reported fact has an assigned severity, one of: * error: severe errors encountered during the analyses. Items marked as errors are considered severe problems requiring immediate attention. * warning: Either less severe problems or uncommon structural features. These still need special attention. * note: Statistical values, plots, or other verbose results of tests and analyses that have been performed. If alternate conformations are present, only the first is evaluated. Hydrogen atoms are only included if explicitly requested, and even then they are not used by all checks. Legend ------ Some notations need a little explanation: RESIDUE: Residues in tables are normally given in 3-5 parts: - A number. This is the internal sequence number of the residue used by WHAT IF. - The residue name. Normally this is a three letter amino acid name. - The sequence number, between brackets. This is the residue number as it was given in the input file. It can be followed by the insertion code. - The chain identifier. A single character. If no chain identifier was given in the input file, this will be invisible. - A model number (only for NMR structures). Z-VALUE: To indicate the normality of a score, the score may be expressed as a Z-value or Z-score. This is just the number of standard deviations that the score deviates from the expected value. A property of Z-values is that the root-mean-square of a group of Z-values (the RMS Z-value) is expected to be 1.0. Z-values above 4.0 and below -4.0 are very uncommon. If a Z-score is used in WHAT IF, the accompanying text will explain how the expected value and standard deviation were obtained. ======================================================================== ==== Compound code /home/whatif/httpd/htdocs/servers/tmp//@17873.1//====1.fil ======================================================================== # 1 # Note: No strange inter-chain connections detected No covalent bonds have been detected between molecules with non-identical chain identifiers # 2 # Note: No duplicate atom names All atom names seem adequately unique # 3 # Error: Non-triclinic spacegroup-symbol is missing The CRYST1 card present in the PDB file gives a valid non-triclinic cell, but the space group symbol is not given. The CRYST1 cell dimensions A =1000.000 B =1000.000 C =1000.000 Alpha= 90.000 Beta= 90.000 Gamma= 90.000 # 4 # Error: Missing unit cell information No SCALE matrix is given in the PDB file. # 5 # Error: Missing symmetry information Problem: No CRYST1 card is given in the PDB file. # 6 # Note: Proposal for corrected SCALE matrix A corrected SCALE matrix has been derived. Proposed scale matrix 0.001000 0.000000 0.000000 0.000000 0.001000 0.000000 0.000000 0.000000 0.001000 # 7 # Note: No rounded coordinates detected No significant rounding of atom coordinates has been detected. # 8 # Note: Valine nomenclature OK No errors were detected in valine nomenclature. # 9 # Note: Threonine nomenclature OK No errors were detected in threonine nomenclature. # 10 # Note: Isoleucine nomenclature OK No errors were detected in isoleucine nomenclature. # 11 # Note: Leucine nomenclature OK No errors were detected in leucine nomenclature. # 12 # Warning: Arginine nomenclature problem The arginine residues listed in the table below have their N-H-1 and N-H-2 swapped. 17 ARG ( 17 ) 1 23 ARG ( 23 ) 1 36 ARG ( 36 ) 1 43 ARG ( 43 ) 1 59 ARG ( 59 ) 1 84 ARG ( 17 ) 2 90 ARG ( 23 ) 2 103 ARG ( 36 ) 2 110 ARG ( 43 ) 2 126 ARG ( 59 ) 2 151 ARG ( 17 ) 3 157 ARG ( 23 ) 3 170 ARG ( 36 ) 3 177 ARG ( 43 ) 3 193 ARG ( 59 ) 3 218 ARG ( 17 ) 4 224 ARG ( 23 ) 4 237 ARG ( 36 ) 4 244 ARG ( 43 ) 4 260 ARG ( 59 ) 4 285 ARG ( 17 ) 5 291 ARG ( 23 ) 5 304 ARG ( 36 ) 5 311 ARG ( 43 ) 5 327 ARG ( 59 ) 5 352 ARG ( 17 ) 6 358 ARG ( 23 ) 6 371 ARG ( 36 ) 6 378 ARG ( 43 ) 6 394 ARG ( 59 ) 6 419 ARG ( 17 ) 7 425 ARG ( 23 ) 7 438 ARG ( 36 ) 7 445 ARG ( 43 ) 7 461 ARG ( 59 ) 7 486 ARG ( 17 ) 8 492 ARG ( 23 ) 8 505 ARG ( 36 ) 8 512 ARG ( 43 ) 8 528 ARG ( 59 ) 8 553 ARG ( 17 ) 9 559 ARG ( 23 ) 9 572 ARG ( 36 ) 9 579 ARG ( 43 ) 9 595 ARG ( 59 ) 9 620 ARG ( 17 ) 10 626 ARG ( 23 ) 10 639 ARG ( 36 ) 10 646 ARG ( 43 ) 10 662 ARG ( 59 ) 10 687 ARG ( 17 ) 11 693 ARG ( 23 ) 11 706 ARG ( 36 ) 11 713 ARG ( 43 ) 11 729 ARG ( 59 ) 11 754 ARG ( 17 ) 12 760 ARG ( 23 ) 12 773 ARG ( 36 ) 12 780 ARG ( 43 ) 12 796 ARG ( 59 ) 12 821 ARG ( 17 ) 13 827 ARG ( 23 ) 13 840 ARG ( 36 ) 13 847 ARG ( 43 ) 13 863 ARG ( 59 ) 13 888 ARG ( 17 ) 14 894 ARG ( 23 ) 14 907 ARG ( 36 ) 14 914 ARG ( 43 ) 14 930 ARG ( 59 ) 14 955 ARG ( 17 ) 15 961 ARG ( 23 ) 15 974 ARG ( 36 ) 15 981 ARG ( 43 ) 15 997 ARG ( 59 ) 15 1022 ARG ( 17 ) 16 1028 ARG ( 23 ) 16 1041 ARG ( 36 ) 16 1048 ARG ( 43 ) 16 1064 ARG ( 59 ) 16 1089 ARG ( 17 ) 17 1095 ARG ( 23 ) 17 1108 ARG ( 36 ) 17 1115 ARG ( 43 ) 17 1131 ARG ( 59 ) 17 1156 ARG ( 17 ) 18 1162 ARG ( 23 ) 18 1175 ARG ( 36 ) 18 1182 ARG ( 43 ) 18 1198 ARG ( 59 ) 18 1223 ARG ( 17 ) 19 1229 ARG ( 23 ) 19 1242 ARG ( 36 ) 19 1249 ARG ( 43 ) 19 1265 ARG ( 59 ) 19 1290 ARG ( 17 ) 20 1296 ARG ( 23 ) 20 1309 ARG ( 36 ) 20 1316 ARG ( 43 ) 20 1332 ARG ( 59 ) 20 # 13 # Warning: Tyrosine convention problem The tyrosine residues listed in the table below have their chi-2 not between -90.0 and 90.0 52 TYR ( 52 ) 1 66 TYR ( 66 ) 1 133 TYR ( 66 ) 2 200 TYR ( 66 ) 3 225 TYR ( 24 ) 4 253 TYR ( 52 ) 4 334 TYR ( 66 ) 5 401 TYR ( 66 ) 6 426 TYR ( 24 ) 7 493 TYR ( 24 ) 8 521 TYR ( 52 ) 8 535 TYR ( 66 ) 8 588 TYR ( 52 ) 9 602 TYR ( 66 ) 9 627 TYR ( 24 ) 10 669 TYR ( 66 ) 10 694 TYR ( 24 ) 11 722 TYR ( 52 ) 11 789 TYR ( 52 ) 12 870 TYR ( 66 ) 13 923 TYR ( 52 ) 14 990 TYR ( 52 ) 15 1004 TYR ( 66 ) 15 1029 TYR ( 24 ) 16 1057 TYR ( 52 ) 16 1096 TYR ( 24 ) 17 1138 TYR ( 66 ) 17 1163 TYR ( 24 ) 18 1230 TYR ( 24 ) 19 1272 TYR ( 66 ) 19 # 14 # Warning: Phenylalanine convention problem The phenylalanine residues listed in the table below have their chi-2 not between -90.0 and 90.0. 25 PHE ( 25 ) 1 73 PHE ( 6 ) 2 92 PHE ( 25 ) 2 102 PHE ( 35 ) 2 140 PHE ( 6 ) 3 226 PHE ( 25 ) 4 274 PHE ( 6 ) 5 293 PHE ( 25 ) 5 341 PHE ( 6 ) 6 360 PHE ( 25 ) 6 370 PHE ( 35 ) 6 427 PHE ( 25 ) 7 475 PHE ( 6 ) 8 494 PHE ( 25 ) 8 504 PHE ( 35 ) 8 542 PHE ( 6 ) 9 561 PHE ( 25 ) 9 571 PHE ( 35 ) 9 628 PHE ( 25 ) 10 705 PHE ( 35 ) 11 762 PHE ( 25 ) 12 829 PHE ( 25 ) 13 839 PHE ( 35 ) 13 906 PHE ( 35 ) 14 973 PHE ( 35 ) 15 1040 PHE ( 35 ) 16 1107 PHE ( 35 ) 17 1145 PHE ( 6 ) 18 1308 PHE ( 35 ) 20 # 15 # Warning: Aspartic acid convention problem The aspartic acid residues listed in the table below have their chi-2 not between -90.0 and 90.0, or their proton on OD1 instead of OD2. 27 ASP ( 27 ) 1 39 ASP ( 39 ) 1 76 ASP ( 9 ) 2 106 ASP ( 39 ) 2 135 ASP ( 1 ) 3 141 ASP ( 7 ) 3 161 ASP ( 27 ) 3 202 ASP ( 1 ) 4 208 ASP ( 7 ) 4 240 ASP ( 39 ) 4 277 ASP ( 9 ) 5 295 ASP ( 27 ) 5 307 ASP ( 39 ) 5 336 ASP ( 1 ) 6 344 ASP ( 9 ) 6 403 ASP ( 1 ) 7 441 ASP ( 39 ) 7 478 ASP ( 9 ) 8 496 ASP ( 27 ) 8 543 ASP ( 7 ) 9 610 ASP ( 7 ) 10 612 ASP ( 9 ) 10 630 ASP ( 27 ) 10 642 ASP ( 39 ) 10 671 ASP ( 1 ) 11 677 ASP ( 7 ) 11 738 ASP ( 1 ) 12 744 ASP ( 7 ) 12 764 ASP ( 27 ) 12 776 ASP ( 39 ) 12 811 ASP ( 7 ) 13 831 ASP ( 27 ) 13 880 ASP ( 9 ) 14 898 ASP ( 27 ) 14 939 ASP ( 1 ) 15 965 ASP ( 27 ) 15 1006 ASP ( 1 ) 16 1012 ASP ( 7 ) 16 1044 ASP ( 39 ) 16 1073 ASP ( 1 ) 17 1079 ASP ( 7 ) 17 1146 ASP ( 7 ) 18 1148 ASP ( 9 ) 18 1207 ASP ( 1 ) 19 1213 ASP ( 7 ) 19 1215 ASP ( 9 ) 19 1233 ASP ( 27 ) 19 1245 ASP ( 39 ) 19 # 16 # Warning: Glutamic acid convention problem The glutamic acid residues listed in the table below have their chi-3 outside the -90.0 to 90.0 range, or their proton on OE1 instead of OE2. 55 GLU ( 55 ) 1 58 GLU ( 58 ) 1 122 GLU ( 55 ) 2 125 GLU ( 58 ) 2 139 GLU ( 5 ) 3 189 GLU ( 55 ) 3 190 GLU ( 56 ) 3 192 GLU ( 58 ) 3 206 GLU ( 5 ) 4 273 GLU ( 5 ) 5 318 GLU ( 50 ) 5 340 GLU ( 5 ) 6 390 GLU ( 55 ) 6 393 GLU ( 58 ) 6 457 GLU ( 55 ) 7 460 GLU ( 58 ) 7 586 GLU ( 50 ) 9 591 GLU ( 55 ) 9 592 GLU ( 56 ) 9 653 GLU ( 50 ) 10 659 GLU ( 56 ) 10 675 GLU ( 5 ) 11 720 GLU ( 50 ) 11 725 GLU ( 55 ) 11 726 GLU ( 56 ) 11 728 GLU ( 58 ) 11 742 GLU ( 5 ) 12 792 GLU ( 55 ) 12 793 GLU ( 56 ) 12 859 GLU ( 55 ) 13 926 GLU ( 55 ) 14 927 GLU ( 56 ) 14 929 GLU ( 58 ) 14 996 GLU ( 58 ) 15 1010 GLU ( 5 ) 16 1055 GLU ( 50 ) 16 1061 GLU ( 56 ) 16 1063 GLU ( 58 ) 16 1077 GLU ( 5 ) 17 1130 GLU ( 58 ) 17 1144 GLU ( 5 ) 18 1194 GLU ( 55 ) 18 1197 GLU ( 58 ) 18 1211 GLU ( 5 ) 19 1256 GLU ( 50 ) 19 1261 GLU ( 55 ) 19 1328 GLU ( 55 ) 20 1331 GLU ( 58 ) 20 # 17 # Warning: Heavy atom naming problem The atoms listed in the table below have nonstandard names in the input file. (Be aware that we sometomes consider an asterix and an apostrophe identical, and thus do not warn for the use of asterixes. Swapped OP1 and OP2 on nucleic acid phosphors also are reported elsewhere). 67 VAL ( 67 ) 1 O <--> OT1 134 VAL ( 67 ) 2 O <--> OT1 201 VAL ( 67 ) 3 O <--> O2 268 VAL ( 67 ) 4 O <--> O2 335 VAL ( 67 ) 5 O <--> O2 402 VAL ( 67 ) 6 O <--> OT1 469 VAL ( 67 ) 7 O <--> OT1 536 VAL ( 67 ) 8 O <--> OT1 603 VAL ( 67 ) 9 O <--> OT1 670 VAL ( 67 ) 10 O <--> OT1 737 VAL ( 67 ) 11 O <--> O2 804 VAL ( 67 ) 12 O <--> O2 871 VAL ( 67 ) 13 O <--> O2 938 VAL ( 67 ) 14 O <--> OT1 1005 VAL ( 67 ) 15 O <--> OT1 1072 VAL ( 67 ) 16 O <--> OT1 1139 VAL ( 67 ) 17 O <--> OT1 1206 VAL ( 67 ) 18 O <--> OT1 1273 VAL ( 67 ) 19 O <--> OT1 1340 VAL ( 67 ) 20 O <--> O2 1346 VAL ( OXT ) 3 O2 <--> OT1 1348 VAL ( OXT ) 4 O2 <--> OT1 1350 VAL ( OXT ) 5 O2 <--> OT1 1362 VAL ( OXT ) 11 O2 <--> OT1 1364 VAL ( OXT ) 12 O2 <--> OT1 1366 VAL ( OXT ) 13 O2 <--> OT1 1380 VAL ( OXT ) 20 O2 <--> OT1 # 18 # Note: Chirality OK All protein atoms have proper chirality. # 19 # Note: Improper dihedral angle distribution OK The RMS Z-score for all improper dihedrals in the structure is within normal ranges. Improper dihedral RMS Z-score : 0.879 # 20 # Note: Per-model averages for chirality check The table below gives the per-model improper dihedral RMS Z-scores. Model 1 : 0.879 Model 2 : 0.880 Model 3 : 0.881 Model 4 : 0.876 Model 5 : 0.875 Model 6 : 0.883 Model 7 : 0.880 Model 8 : 0.882 Model 9 : 0.880 Model 10 : 0.875 Model 11 : 0.872 Model 12 : 0.881 Model 13 : 0.883 Model 14 : 0.879 Model 15 : 0.880 Model 16 : 0.880 Model 17 : 0.877 Model 18 : 0.877 Model 19 : 0.878 Model 20 : 0.874 # 21 # Note: No missing atoms detected All expected atoms are present. # 22 # Note: OXT check OK All required C-terminal oxygen atoms are present. # 23 # Note: No extra C-terminal groups found No C-terminal groups are present for non C-terminal residues # 24 # Note: All bond lengths OK All bond lengths are in agreement with standard bond lengths using a tolerance of 4 sigma (both standard values and sigma for amino acid residues have been taken from Engh and Huber [REF], for DNA/RNA from Parkinson et al [REF]) # 25 # Warning: Low bond length variability Bond lengths were found to deviate less than normal from the mean Engh and Huber [REF] and/or Parkinson et al [REF] standard bond lengths. The RMS Z-score given below is expected to be around 1.0 for a normally restrained data set. The fact that it is lower than 0.667 in this structure might indicate that too-strong constraints have been used in the refinement. This can only be a problem for high resolution X-ray structures. RMS Z-score for bond lengths: 0.517 RMS-deviation in bond distances: 0.012 # 26 # Note: Per-model averages for bond-length check The table below gives the per-model bond-length RMS Z-scores. Model 1 : 0.518 Model 2 : 0.516 Model 3 : 0.516 Model 4 : 0.516 Model 5 : 0.517 Model 6 : 0.517 Model 7 : 0.519 Model 8 : 0.517 Model 9 : 0.518 Model 10 : 0.518 Model 11 : 0.518 Model 12 : 0.518 Model 13 : 0.518 Model 14 : 0.516 Model 15 : 0.516 Model 16 : 0.517 Model 17 : 0.518 Model 18 : 0.517 Model 19 : 0.519 Model 20 : 0.519 # 27 # Note: All bond angles OK All bond angles are in agreement with standard bond angles using a tolerance of 4 sigma (both standard values and sigma for protein residues have been taken from Engh and Huber [REF], for DNA/RNA from Parkinson et al. [REF]). Please note that disulphide bridges are neglected. # 28 # Note: Normal bond angle variability Bond angles were found to deviate normally from the mean standard bond angles (normal values for protein residues were taken from Engh and Huber [REF], for DNA/RNA from Parkinson et al [REF]). The RMS Z-score given below is expected to be around 1.0 for a normally restrained data set, and this is indeed observed for very high resolution X-ray structures. More common values are around 1.55. RMS Z-score for bond angles: 0.902 RMS-deviation in bond angles: 1.588 # 29 # Note: Per-model averages for bond-angle check The table below gives the per-model bond-angle RMS Z-scores. Model 1 : 0.903 Model 2 : 0.903 Model 3 : 0.903 Model 4 : 0.902 Model 5 : 0.903 Model 6 : 0.902 Model 7 : 0.903 Model 8 : 0.902 Model 9 : 0.903 Model 10 : 0.903 Model 11 : 0.901 Model 12 : 0.902 Model 13 : 0.904 Model 14 : 0.903 Model 15 : 0.901 Model 16 : 0.903 Model 17 : 0.903 Model 18 : 0.901 Model 19 : 0.903 Model 20 : 0.901 # 30 # Note: Side chain planarity OK All of the side chains of residues that have a planar group are planar within expected RMS deviations. # 31 # Note: Atoms connected to aromatic rings OK All of the atoms that are connected to planar aromatic rings in side chains of amino-acid residues are in the plane within expected RMS deviations. # 32 # Warning: Unusual PRO puckering amplitudes The proline residues listed in the table below have a puckering amplitude that is outside of normal ranges. Puckering parameters were calculated by the method of Cremer and Pople [REF]. Normal PRO rings have a puckering amplitude Q between 0.20 and 0.45 Angstrom. If Q is lower than 0.20 Angstrom for a PRO residue, this could indicate disorder between the two different normal ring forms (with C-gamma below and above the ring, respectively). If Q is higher than 0.45 Angstrom something could have gone wrong during the refinement. 2 PRO ( 2 ) 1 0.18 LOW 8 PRO ( 8 ) 1 0.18 LOW 11 PRO ( 11 ) 1 0.18 LOW 51 PRO ( 51 ) 1 0.18 LOW 69 PRO ( 2 ) 2 0.18 LOW 75 PRO ( 8 ) 2 0.18 LOW 78 PRO ( 11 ) 2 0.18 LOW 118 PRO ( 51 ) 2 0.18 LOW 136 PRO ( 2 ) 3 0.18 LOW 142 PRO ( 8 ) 3 0.18 LOW 145 PRO ( 11 ) 3 0.18 LOW 185 PRO ( 51 ) 3 0.18 LOW 203 PRO ( 2 ) 4 0.18 LOW 209 PRO ( 8 ) 4 0.18 LOW 212 PRO ( 11 ) 4 0.18 LOW 252 PRO ( 51 ) 4 0.18 LOW 270 PRO ( 2 ) 5 0.18 LOW 276 PRO ( 8 ) 5 0.18 LOW 279 PRO ( 11 ) 5 0.18 LOW 319 PRO ( 51 ) 5 0.18 LOW 337 PRO ( 2 ) 6 0.18 LOW 343 PRO ( 8 ) 6 0.18 LOW 346 PRO ( 11 ) 6 0.18 LOW 386 PRO ( 51 ) 6 0.18 LOW 404 PRO ( 2 ) 7 0.18 LOW 410 PRO ( 8 ) 7 0.18 LOW 413 PRO ( 11 ) 7 0.18 LOW 453 PRO ( 51 ) 7 0.18 LOW 471 PRO ( 2 ) 8 0.18 LOW 477 PRO ( 8 ) 8 0.18 LOW 480 PRO ( 11 ) 8 0.18 LOW 520 PRO ( 51 ) 8 0.18 LOW 538 PRO ( 2 ) 9 0.18 LOW 544 PRO ( 8 ) 9 0.18 LOW 547 PRO ( 11 ) 9 0.18 LOW 587 PRO ( 51 ) 9 0.18 LOW 605 PRO ( 2 ) 10 0.18 LOW 611 PRO ( 8 ) 10 0.18 LOW 614 PRO ( 11 ) 10 0.18 LOW 654 PRO ( 51 ) 10 0.18 LOW 672 PRO ( 2 ) 11 0.18 LOW 678 PRO ( 8 ) 11 0.18 LOW 681 PRO ( 11 ) 11 0.18 LOW 721 PRO ( 51 ) 11 0.18 LOW 739 PRO ( 2 ) 12 0.18 LOW 745 PRO ( 8 ) 12 0.18 LOW 748 PRO ( 11 ) 12 0.18 LOW 788 PRO ( 51 ) 12 0.18 LOW 806 PRO ( 2 ) 13 0.18 LOW 812 PRO ( 8 ) 13 0.18 LOW 815 PRO ( 11 ) 13 0.18 LOW 855 PRO ( 51 ) 13 0.18 LOW 873 PRO ( 2 ) 14 0.18 LOW 879 PRO ( 8 ) 14 0.18 LOW 882 PRO ( 11 ) 14 0.18 LOW 922 PRO ( 51 ) 14 0.18 LOW 940 PRO ( 2 ) 15 0.18 LOW 946 PRO ( 8 ) 15 0.18 LOW 949 PRO ( 11 ) 15 0.18 LOW 989 PRO ( 51 ) 15 0.18 LOW 1007 PRO ( 2 ) 16 0.18 LOW 1013 PRO ( 8 ) 16 0.18 LOW 1016 PRO ( 11 ) 16 0.18 LOW 1056 PRO ( 51 ) 16 0.18 LOW 1074 PRO ( 2 ) 17 0.18 LOW 1080 PRO ( 8 ) 17 0.18 LOW 1083 PRO ( 11 ) 17 0.18 LOW 1123 PRO ( 51 ) 17 0.18 LOW 1141 PRO ( 2 ) 18 0.18 LOW 1147 PRO ( 8 ) 18 0.18 LOW 1150 PRO ( 11 ) 18 0.18 LOW 1190 PRO ( 51 ) 18 0.18 LOW 1208 PRO ( 2 ) 19 0.18 LOW 1214 PRO ( 8 ) 19 0.18 LOW 1217 PRO ( 11 ) 19 0.18 LOW 1257 PRO ( 51 ) 19 0.18 LOW 1275 PRO ( 2 ) 20 0.18 LOW 1281 PRO ( 8 ) 20 0.18 LOW 1284 PRO ( 11 ) 20 0.18 LOW 1324 PRO ( 51 ) 20 0.18 LOW # 33 # Note: PRO puckering phases OK Puckering phases for all PRO residues are normal # 34 # Warning: Torsion angle evaluation shows unusual residues The residues listed in the table below contain bad or abnormal torsion angles. These scores give an impression of how ``normal'' the torsion angles in protein residues are. All torsion angles except omega are used for calculating a `normality' score. Average values and standard deviations were obtained from the residues in the WHAT IF database. These are used to calculate Z-scores. A residue with a Z-score of below -2.0 is poor, and a score of less than -3.0 is worrying. For such residues more than one torsion angle is in a highly unlikely position. 1057 TYR ( 52 ) 16 -3.0428 810 PHE ( 6 ) 13 -2.8262 535 TYR ( 66 ) 8 -2.8197 383 SER ( 48 ) 6 -2.7105 1156 ARG ( 17 ) 18 -2.7043 655 TYR ( 52 ) 10 -2.6985 316 SER ( 48 ) 5 -2.6811 1326 SER ( 53 ) 20 -2.6802 652 VAL ( 49 ) 10 -2.6631 853 VAL ( 49 ) 13 -2.6409 125 GLU ( 58 ) 2 -2.6346 986 SER ( 48 ) 15 -2.6285 653 GLU ( 50 ) 10 -2.6215 193 ARG ( 59 ) 3 -2.6162 1022 ARG ( 17 ) 16 -2.5961 1063 GLU ( 58 ) 16 -2.5848 317 VAL ( 49 ) 5 -2.5811 457 GLU ( 55 ) 7 -2.5601 1127 GLU ( 55 ) 17 -2.5403 994 GLU ( 56 ) 15 -2.5388 1261 GLU ( 55 ) 19 -2.5372 419 ARG ( 17 ) 7 -2.5322 527 GLU ( 58 ) 8 -2.5179 1060 GLU ( 55 ) 16 -2.5169 588 TYR ( 52 ) 9 -2.4966 921 GLU ( 50 ) 14 -2.4927 541 GLU ( 5 ) 9 -2.4844 1053 SER ( 48 ) 16 -2.4775 927 GLU ( 56 ) 14 -2.4657 323 GLU ( 55 ) 5 -2.4647 594 GLU ( 58 ) 9 -2.4627 792 GLU ( 55 ) 12 -2.4619 661 GLU ( 58 ) 10 -2.4590 1209 ASN ( 3 ) 19 -2.4553 405 ASN ( 3 ) 7 -2.4461 1142 ASN ( 3 ) 18 -2.4442 1124 TYR ( 52 ) 17 -2.4402 722 TYR ( 52 ) 11 -2.4327 807 ASN ( 3 ) 13 -2.4320 1075 ASN ( 3 ) 17 -2.4320 3 ASN ( 3 ) 1 -2.4320 723 SER ( 53 ) 11 -2.4292 598 GLY ( 62 ) 9 -2.4292 991 SER ( 53 ) 15 -2.4189 157 ARG ( 23 ) 3 -2.4147 1201 GLY ( 62 ) 18 -2.4144 673 ASN ( 3 ) 11 -2.4125 993 GLU ( 55 ) 15 -2.4097 996 GLU ( 58 ) 15 -2.4087 626 ARG ( 23 ) 10 -2.4046 1259 SER ( 53 ) 19 -2.4036 941 ASN ( 3 ) 15 -2.3967 790 SER ( 53 ) 12 -2.3946 1109 SER ( 37 ) 17 -2.3934 1187 SER ( 48 ) 18 -2.3881 1077 GLU ( 5 ) 17 -2.3862 260 ARG ( 59 ) 4 -2.3858 693 ARG ( 23 ) 11 -2.3839 1121 VAL ( 49 ) 17 -2.3787 123 GLU ( 56 ) 2 -2.3731 728 GLU ( 58 ) 11 -2.3699 259 GLU ( 58 ) 4 -2.3666 1329 GLU ( 56 ) 20 -2.3643 206 GLU ( 5 ) 4 -2.3605 926 GLU ( 55 ) 14 -2.3582 1198 ARG ( 59 ) 18 -2.3497 785 SER ( 48 ) 12 -2.3425 1262 GLU ( 56 ) 19 -2.3402 390 GLU ( 55 ) 6 -2.3361 452 GLU ( 50 ) 7 -2.3352 331 MET ( 63 ) 5 -2.3242 456 GLN ( 54 ) 7 -2.3231 1271 SER ( 65 ) 19 -2.3226 1339 TYR ( 66 ) 20 -2.3222 63 MET ( 63 ) 1 -2.3217 454 TYR ( 52 ) 7 -2.3189 192 GLU ( 58 ) 3 -2.3175 465 MET ( 63 ) 7 -2.3112 760 ARG ( 23 ) 12 -2.3062 961 ARG ( 23 ) 15 -2.3042 988 GLU ( 50 ) 15 -2.3030 796 ARG ( 59 ) 12 -2.2979 888 ARG ( 17 ) 14 -2.2973 563 ASP ( 27 ) 9 -2.2962 589 SER ( 53 ) 9 -2.2949 84 ARG ( 17 ) 2 -2.2944 398 MET ( 63 ) 6 -2.2856 857 SER ( 53 ) 13 -2.2809 190 GLU ( 56 ) 3 -2.2805 791 GLN ( 54 ) 12 -2.2800 1260 GLN ( 54 ) 19 -2.2768 362 ASP ( 27 ) 6 -2.2748 1296 ARG ( 23 ) 20 -2.2732 1058 SER ( 53 ) 16 -2.2698 874 ASN ( 3 ) 14 -2.2647 204 ASN ( 3 ) 4 -2.2647 371 ARG ( 36 ) 6 -2.2602 1278 GLU ( 5 ) 20 -2.2556 742 GLU ( 5 ) 12 -2.2519 1008 ASN ( 3 ) 16 -2.2518 59 ARG ( 59 ) 1 -2.2512 189 GLU ( 55 ) 3 -2.2503 929 GLU ( 58 ) 14 -2.2321 827 ARG ( 23 ) 13 -2.2294 228 ASP ( 27 ) 4 -2.2259 486 ARG ( 17 ) 8 -2.2236 720 GLU ( 50 ) 11 -2.2148 522 SER ( 53 ) 8 -2.2004 199 SER ( 65 ) 3 -2.1963 925 GLN ( 54 ) 14 -2.1876 802 SER ( 65 ) 12 -2.1870 120 SER ( 53 ) 2 -2.1815 466 GLY ( 64 ) 7 -2.1805 793 GLU ( 56 ) 12 -2.1800 868 GLY ( 64 ) 13 -2.1793 1028 ARG ( 23 ) 16 -2.1777 1137 SER ( 65 ) 17 -2.1735 1135 MET ( 63 ) 17 -2.1728 257 GLU ( 56 ) 4 -2.1720 1194 GLU ( 55 ) 18 -2.1698 1110 LYS ( 38 ) 17 -2.1669 591 GLU ( 55 ) 9 -2.1669 1069 GLY ( 64 ) 16 -2.1654 908 SER ( 37 ) 14 -2.1650 669 TYR ( 66 ) 10 -2.1640 667 GLY ( 64 ) 10 -2.1583 256 GLU ( 55 ) 4 -2.1570 1337 GLY ( 64 ) 20 -2.1521 935 GLY ( 64 ) 14 -2.1509 117 GLU ( 50 ) 2 -2.1501 397 GLY ( 62 ) 6 -2.1456 200 TYR ( 66 ) 3 -2.1436 533 GLY ( 64 ) 8 -2.1414 734 GLY ( 64 ) 11 -2.1406 1270 GLY ( 64 ) 19 -2.1378 675 GLU ( 5 ) 11 -2.1371 1061 GLU ( 56 ) 16 -2.1361 332 GLY ( 64 ) 5 -2.1331 121 GLN ( 54 ) 2 -2.1327 666 MET ( 63 ) 10 -2.1312 186 TYR ( 52 ) 3 -2.1224 1193 GLN ( 54 ) 18 -2.1223 658 GLU ( 55 ) 10 -2.1207 161 ASP ( 27 ) 3 -2.1146 930 ARG ( 59 ) 14 -2.1122 831 ASP ( 27 ) 13 -2.1094 909 LYS ( 38 ) 14 -2.1092 341 PHE ( 6 ) 6 -2.1081 1279 PHE ( 6 ) 20 -2.1054 1189 GLU ( 50 ) 18 -2.1048 867 MET ( 63 ) 13 -2.1007 729 ARG ( 59 ) 11 -2.0991 1004 TYR ( 66 ) 15 -2.0943 295 ASP ( 27 ) 5 -2.0929 1300 ASP ( 27 ) 20 -2.0918 732 GLY ( 62 ) 11 -2.0871 1309 ARG ( 36 ) 20 -2.0865 1256 GLU ( 50 ) 19 -2.0863 553 ARG ( 17 ) 9 -2.0860 1136 GLY ( 64 ) 17 -2.0823 852 SER ( 48 ) 13 -2.0807 531 GLY ( 62 ) 8 -2.0781 1211 GLU ( 5 ) 19 -2.0778 546 LEU ( 10 ) 9 -2.0758 630 ASP ( 27 ) 10 -2.0757 72 GLU ( 5 ) 2 -2.0748 1070 SER ( 65 ) 16 -2.0747 725 GLU ( 55 ) 11 -2.0734 458 GLU ( 56 ) 7 -2.0716 1126 GLN ( 54 ) 17 -2.0701 131 GLY ( 64 ) 2 -2.0680 1088 HIS ( 16 ) 17 -2.0623 182 SER ( 48 ) 3 -2.0613 64 GLY ( 64 ) 1 -2.0596 965 ASP ( 27 ) 15 -2.0462 184 GLU ( 50 ) 3 -2.0445 196 GLY ( 62 ) 3 -2.0398 1311 LYS ( 38 ) 20 -2.0398 787 GLU ( 50 ) 12 -2.0360 264 MET ( 63 ) 4 -2.0348 525 GLU ( 56 ) 8 -2.0338 399 GLY ( 64 ) 6 -2.0317 1191 TYR ( 52 ) 18 -2.0280 197 MET ( 63 ) 3 -2.0246 409 ASP ( 7 ) 7 -2.0206 599 MET ( 63 ) 9 -2.0124 85 CYS ( 18 ) 2 -2.0099 54 GLN ( 54 ) 1 -2.0080 284 HIS ( 16 ) 5 -2.0060 1001 MET ( 63 ) 15 -2.0055 1012 ASP ( 7 ) 16 -2.0046 358 ARG ( 23 ) 6 -2.0037 1291 CYS ( 18 ) 20 -2.0035 82 LEU ( 15 ) 2 -2.0027 1068 MET ( 63 ) 16 -2.0003 # 35 # Warning: Backbone torsion angle evaluation shows unusual conformations The residues listed in the table below have abnormal backbone torsion angles. Residues with ``forbidden'' phi-psi combinations are listed, as well as residues with unusual omega angles (deviating by more than 3 sigma from the normal value). Please note that it is normal if about 5 percent of the residues is listed here as having unusual phi-psi combinations. 22 ALA ( 22 ) 1 Poor phi/psi 50 GLU ( 50 ) 1 Poor phi/psi 53 SER ( 53 ) 1 Poor phi/psi 57 ALA ( 57 ) 1 Poor phi/psi 58 GLU ( 58 ) 1 Poor phi/psi 59 ARG ( 59 ) 1 Poor phi/psi 72 GLU ( 5 ) 2 Poor phi/psi 83 HIS ( 16 ) 2 Poor phi/psi 84 ARG ( 17 ) 2 Poor phi/psi 89 ALA ( 22 ) 2 Poor phi/psi 125 GLU ( 58 ) 2 Poor phi/psi 130 MET ( 63 ) 2 Poor phi/psi 150 HIS ( 16 ) 3 Poor phi/psi 151 ARG ( 17 ) 3 Poor phi/psi 156 ALA ( 22 ) 3 Poor phi/psi 182 SER ( 48 ) 3 Poor phi/psi 186 TYR ( 52 ) 3 Poor phi/psi 187 SER ( 53 ) 3 Poor phi/psi 191 ALA ( 57 ) 3 Poor phi/psi 192 GLU ( 58 ) 3 Poor phi/psi 197 MET ( 63 ) 3 Poor phi/psi 199 SER ( 65 ) 3 Poor phi/psi 217 HIS ( 16 ) 4 Poor phi/psi 218 ARG ( 17 ) 4 Poor phi/psi 223 ALA ( 22 ) 4 Poor phi/psi 228 ASP ( 27 ) 4 Poor phi/psi 262 ALA ( 61 ) 4 Poor phi/psi 266 SER ( 65 ) 4 Poor phi/psi 317 VAL ( 49 ) 5 Poor phi/psi 319 PRO ( 51 ) 5 Poor phi/psi 324 GLU ( 56 ) 5 Poor phi/psi 325 ALA ( 57 ) 5 Poor phi/psi 326 GLU ( 58 ) 5 Poor phi/psi 327 ARG ( 59 ) 5 Poor phi/psi 329 ALA ( 61 ) 5 Poor phi/psi 331 MET ( 63 ) 5 Poor phi/psi 333 SER ( 65 ) 5 Poor phi/psi 334 TYR ( 66 ) 5 Poor phi/psi 351 HIS ( 16 ) 6 Poor phi/psi 352 ARG ( 17 ) 6 Poor phi/psi 362 ASP ( 27 ) 6 Poor phi/psi 383 SER ( 48 ) 6 Poor phi/psi 385 GLU ( 50 ) 6 Poor phi/psi 388 SER ( 53 ) 6 Poor phi/psi 394 ARG ( 59 ) 6 Poor phi/psi 396 ALA ( 61 ) 6 Poor phi/psi 398 MET ( 63 ) 6 Poor phi/psi 400 SER ( 65 ) 6 Poor phi/psi 406 ALA ( 4 ) 7 Poor phi/psi 418 HIS ( 16 ) 7 Poor phi/psi 419 ARG ( 17 ) 7 Poor phi/psi 424 ALA ( 22 ) 7 Poor phi/psi 454 TYR ( 52 ) 7 Poor phi/psi 456 GLN ( 54 ) 7 Poor phi/psi 462 ALA ( 60 ) 7 Poor phi/psi 463 ALA ( 61 ) 7 Poor phi/psi 467 SER ( 65 ) 7 Poor phi/psi 482 GLY ( 13 ) 8 Poor phi/psi 485 HIS ( 16 ) 8 Poor phi/psi 491 ALA ( 22 ) 8 Poor phi/psi 517 SER ( 48 ) 8 Poor phi/psi 519 GLU ( 50 ) 8 Poor phi/psi 523 GLN ( 54 ) 8 Poor phi/psi 527 GLU ( 58 ) 8 Poor phi/psi 530 ALA ( 61 ) 8 Poor phi/psi 541 GLU ( 5 ) 9 Poor phi/psi 547 PRO ( 11 ) 9 Poor phi/psi 550 GLY ( 14 ) 9 Poor phi/psi 552 HIS ( 16 ) 9 Poor phi/psi 553 ARG ( 17 ) 9 Poor phi/psi 558 ALA ( 22 ) 9 Poor phi/psi 563 ASP ( 27 ) 9 Poor phi/psi 588 TYR ( 52 ) 9 Poor phi/psi 589 SER ( 53 ) 9 Poor phi/psi 591 GLU ( 55 ) 9 Poor phi/psi 594 GLU ( 58 ) 9 Poor phi/psi 598 GLY ( 62 ) 9 Poor phi/psi 599 MET ( 63 ) 9 Poor phi/psi 606 ASN ( 3 ) 10 Poor phi/psi 619 HIS ( 16 ) 10 Poor phi/psi 620 ARG ( 17 ) 10 Poor phi/psi 625 ALA ( 22 ) 10 Poor phi/psi 652 VAL ( 49 ) 10 Poor phi/psi 653 GLU ( 50 ) 10 Poor phi/psi 654 PRO ( 51 ) 10 Poor phi/psi 655 TYR ( 52 ) 10 Poor phi/psi 662 ARG ( 59 ) 10 Poor phi/psi 663 ALA ( 60 ) 10 Poor phi/psi 664 ALA ( 61 ) 10 Poor phi/psi 665 GLY ( 62 ) 10 Poor phi/psi 666 MET ( 63 ) 10 Poor phi/psi 674 ALA ( 4 ) 11 Poor phi/psi 686 HIS ( 16 ) 11 Poor phi/psi 687 ARG ( 17 ) 11 Poor phi/psi 692 ALA ( 22 ) 11 Poor phi/psi 722 TYR ( 52 ) 11 Poor phi/psi 723 SER ( 53 ) 11 Poor phi/psi 731 ALA ( 61 ) 11 Poor phi/psi 741 ALA ( 4 ) 12 Poor phi/psi 785 SER ( 48 ) 12 Poor phi/psi 790 SER ( 53 ) 12 Poor phi/psi 791 GLN ( 54 ) 12 Poor phi/psi 792 GLU ( 55 ) 12 Poor phi/psi 793 GLU ( 56 ) 12 Poor phi/psi 796 ARG ( 59 ) 12 Poor phi/psi 797 ALA ( 60 ) 12 Poor phi/psi 802 SER ( 65 ) 12 Poor phi/psi 820 HIS ( 16 ) 13 Poor phi/psi 821 ARG ( 17 ) 13 Poor phi/psi 826 ALA ( 22 ) 13 Poor phi/psi 857 SER ( 53 ) 13 Poor phi/psi 862 GLU ( 58 ) 13 Poor phi/psi 863 ARG ( 59 ) 13 Poor phi/psi 865 ALA ( 61 ) 13 Poor phi/psi 867 MET ( 63 ) 13 Poor phi/psi 869 SER ( 65 ) 13 Poor phi/psi 875 ALA ( 4 ) 14 Poor phi/psi 893 ALA ( 22 ) 14 Poor phi/psi 924 SER ( 53 ) 14 Poor phi/psi 926 GLU ( 55 ) 14 Poor phi/psi 927 GLU ( 56 ) 14 Poor phi/psi 931 ALA ( 60 ) 14 Poor phi/psi 934 MET ( 63 ) 14 Poor phi/psi 937 TYR ( 66 ) 14 Poor phi/psi 942 ALA ( 4 ) 15 Poor phi/psi 960 ALA ( 22 ) 15 Poor phi/psi 986 SER ( 48 ) 15 Poor phi/psi 987 VAL ( 49 ) 15 Poor phi/psi 990 TYR ( 52 ) 15 Poor phi/psi 991 SER ( 53 ) 15 Poor phi/psi 994 GLU ( 56 ) 15 Poor phi/psi 995 ALA ( 57 ) 15 Poor phi/psi 996 GLU ( 58 ) 15 Poor phi/psi 997 ARG ( 59 ) 15 Poor phi/psi 999 ALA ( 61 ) 15 Poor phi/psi 1016 PRO ( 11 ) 16 Poor phi/psi 1021 HIS ( 16 ) 16 Poor phi/psi 1022 ARG ( 17 ) 16 Poor phi/psi 1027 ALA ( 22 ) 16 Poor phi/psi 1032 ASP ( 27 ) 16 Poor phi/psi 1053 SER ( 48 ) 16 Poor phi/psi 1056 PRO ( 51 ) 16 Poor phi/psi 1057 TYR ( 52 ) 16 Poor phi/psi 1059 GLN ( 54 ) 16 Poor phi/psi 1063 GLU ( 58 ) 16 Poor phi/psi 1065 ALA ( 60 ) 16 Poor phi/psi 1066 ALA ( 61 ) 16 Poor phi/psi 1070 SER ( 65 ) 16 Poor phi/psi 1071 TYR ( 66 ) 16 Poor phi/psi 1077 GLU ( 5 ) 17 Poor phi/psi 1094 ALA ( 22 ) 17 Poor phi/psi 1121 VAL ( 49 ) 17 Poor phi/psi 1125 SER ( 53 ) 17 Poor phi/psi 1126 GLN ( 54 ) 17 Poor phi/psi 1137 SER ( 65 ) 17 Poor phi/psi 1155 HIS ( 16 ) 18 Poor phi/psi 1156 ARG ( 17 ) 18 Poor phi/psi 1161 ALA ( 22 ) 18 Poor phi/psi 1188 VAL ( 49 ) 18 Poor phi/psi 1189 GLU ( 50 ) 18 Poor phi/psi 1192 SER ( 53 ) 18 Poor phi/psi 1194 GLU ( 55 ) 18 Poor phi/psi 1196 ALA ( 57 ) 18 Poor phi/psi 1200 ALA ( 61 ) 18 Poor phi/psi 1201 GLY ( 62 ) 18 Poor phi/psi 1202 MET ( 63 ) 18 Poor phi/psi 1222 HIS ( 16 ) 19 Poor phi/psi 1223 ARG ( 17 ) 19 Poor phi/psi 1255 VAL ( 49 ) 19 Poor phi/psi 1257 PRO ( 51 ) 19 Poor phi/psi 1259 SER ( 53 ) 19 Poor phi/psi 1260 GLN ( 54 ) 19 Poor phi/psi 1262 GLU ( 56 ) 19 Poor phi/psi 1267 ALA ( 61 ) 19 Poor phi/psi 1271 SER ( 65 ) 19 Poor phi/psi 1289 HIS ( 16 ) 20 Poor phi/psi 1290 ARG ( 17 ) 20 Poor phi/psi 1295 ALA ( 22 ) 20 Poor phi/psi 1323 GLU ( 50 ) 20 Poor phi/psi 1325 TYR ( 52 ) 20 Poor phi/psi 1326 SER ( 53 ) 20 Poor phi/psi 1330 ALA ( 57 ) 20 Poor phi/psi 1332 ARG ( 59 ) 20 Poor phi/psi 1334 ALA ( 61 ) 20 Poor phi/psi # 36 # Error: Ramachandran Z-score very low The score expressing how well the backbone conformations of all residues are corresponding to the known allowed areas in the Ramachandran plot is very low. Ramachandran Z-score : -6.551 # 37 # Note: Per-model averages for Ramachandran check The table below gives the per-model Ramachandran Z-scores. Model 1 : -6.618 Model 2 : -6.170 Model 3 : -6.521 Model 4 : -5.671 Model 5 : -6.221 Model 6 : -7.353 Model 7 : -6.785 Model 8 : -6.851 Model 9 : -6.924 Model 10 : -5.670 Model 11 : -6.402 Model 12 : -5.654 Model 13 : -6.774 Model 14 : -7.312 Model 15 : -6.249 Model 16 : -7.325 Model 17 : -6.942 Model 18 : -5.822 Model 19 : -6.369 Model 20 : -7.394 # 38 # Warning: Omega angles too tightly restrained The omega angles for trans-peptide bonds in a structure are expected to give a gaussian distribution with the average around +178 degrees and a standard deviation around 5.5 degrees. These expected values were obtained from very accurately determined structures. Many protein structures are too tightly constrained. This seems to be the case with the current structure, as the observed standard deviation is below 4.0 degrees. Standard deviation of omega values : 0.000 # 39 # Note: Per-model averages for omega angle check The table below gives the per-model omega angle standard deviations. Model 1 : 0.066 Model 2 : 0.144 Model 3 : 0.063 Model 4 : 0.062 Model 5 : 0.069 Model 6 : 0.103 Model 7 : 0.087 Model 8 : 0.090 Model 9 : 0.097 Model 10 : 0.000 Model 11 : 0.068 Model 12 : 0.000 Model 13 : 0.086 Model 14 : 0.106 Model 15 : 0.083 Model 16 : 0.060 Model 17 : 0.075 Model 18 : 0.076 Model 19 : 0.088 Model 20 : 0.000 # 40 # Error: chi-1/chi-2 angle correlation Z-score very low The score expressing how well the chi-1/chi-2 angles of all residues are corresponding to the populated areas in the database is very low. chi-1/chi-2 correlation Z-score : -5.676 # 41 # Note: Per-model averages for chi-1/chi-2 angle check The table below gives the per-model chi-1/chi-2 correlation Z-scores. Model 1 : -5.189 Model 2 : -5.697 Model 3 : -5.899 Model 4 : -5.320 Model 5 : -5.643 Model 6 : -5.202 Model 7 : -5.751 Model 8 : -5.706 Model 9 : -5.909 Model 10 : -5.889 Model 11 : -6.013 Model 12 : -5.803 Model 13 : -6.004 Model 14 : -6.137 Model 15 : -5.705 Model 16 : -5.680 Model 17 : -5.520 Model 18 : -5.864 Model 19 : -5.847 Model 20 : -4.750 # 42 # Note: Ramachandran plot In this Ramachandran plot X-signs represent glycines, squares represent prolines and small plus-signs represent the other residues. If too many plus-signs fall outside the contoured areas then the molecule is poorly refined (or worse). In a colour picture, the residues that are part of a helix are shown in blue, strand residues in red. "Allowed" regions for helical residues are drawn in blue, for strand residues in red, and for all other residues in green. In the TeX file, a plot has been inserted here Model number 1 # 43 # Note: Ramachandran plot In the TeX file, a plot has been inserted here Model number 2 # 44 # Note: Ramachandran plot In the TeX file, a plot has been inserted here Model number 3 # 45 # Note: Ramachandran plot In the TeX file, a plot has been inserted here Model number 4 # 46 # Note: Ramachandran plot In the TeX file, a plot has been inserted here Model number 5 # 47 # Note: Ramachandran plot In the TeX file, a plot has been inserted here Model number 6 # 48 # Note: Ramachandran plot In the TeX file, a plot has been inserted here Model number 7 # 49 # Note: Ramachandran plot In the TeX file, a plot has been inserted here Model number 8 # 50 # Note: Ramachandran plot In the TeX file, a plot has been inserted here Model number 9 # 51 # Note: Ramachandran plot In the TeX file, a plot has been inserted here Model number 10 # 52 # Note: Ramachandran plot In the TeX file, a plot has been inserted here Model number 11 # 53 # Note: Ramachandran plot In the TeX file, a plot has been inserted here Model number 12 # 54 # Note: Ramachandran plot In the TeX file, a plot has been inserted here Model number 13 # 55 # Note: Ramachandran plot In the TeX file, a plot has been inserted here Model number 14 # 56 # Note: Ramachandran plot In the TeX file, a plot has been inserted here Model number 15 # 57 # Note: Ramachandran plot In the TeX file, a plot has been inserted here Model number 16 # 58 # Note: Ramachandran plot In the TeX file, a plot has been inserted here Model number 17 # 59 # Note: Ramachandran plot In the TeX file, a plot has been inserted here Model number 18 # 60 # Note: Ramachandran plot In the TeX file, a plot has been inserted here Model number 19 # 61 # Note: Ramachandran plot In the TeX file, a plot has been inserted here Model number 20 # 62 # Note: Inside/Outside residue distribution normal The distribution of residue types over the inside and the outside of the protein is normal. inside/outside RMS Z-score : 1.117 # 63 # Note: Per-model averages for inside/outside residue distribution check The table below gives the per-model inside/outside residue distribution RMS Z-scores. Model 1 : 1.131 Model 2 : 1.066 Model 3 : 1.080 Model 4 : 1.080 Model 5 : 1.069 Model 6 : 1.106 Model 7 : 1.196 Model 8 : 1.115 Model 9 : 1.171 Model 10 : 1.120 Model 11 : 1.182 Model 12 : 1.135 Model 13 : 1.072 Model 14 : 1.092 Model 15 : 1.043 Model 16 : 1.158 Model 17 : 1.052 Model 18 : 1.077 Model 19 : 1.149 Model 20 : 1.229 # 64 # Note: Inside/Outside RMS Z-score plot The Inside/Outside distribution normality RMS Z-score over a 15 residue window is plotted as function of the residue number. High areas in the plot (above 1.5) indicate unusual inside/outside patterns. In the TeX file, a plot has been inserted here Model number 1 # 65 # Note: Inside/Outside RMS Z-score plot In the TeX file, a plot has been inserted here Model number 2 # 66 # Note: Inside/Outside RMS Z-score plot In the TeX file, a plot has been inserted here Model number 3 # 67 # Note: Inside/Outside RMS Z-score plot In the TeX file, a plot has been inserted here Model number 4 # 68 # Note: Inside/Outside RMS Z-score plot In the TeX file, a plot has been inserted here Model number 5 # 69 # Note: Inside/Outside RMS Z-score plot In the TeX file, a plot has been inserted here Model number 6 # 70 # Note: Inside/Outside RMS Z-score plot In the TeX file, a plot has been inserted here Model number 7 # 71 # Note: Inside/Outside RMS Z-score plot In the TeX file, a plot has been inserted here Model number 8 # 72 # Note: Inside/Outside RMS Z-score plot In the TeX file, a plot has been inserted here Model number 9 # 73 # Note: Inside/Outside RMS Z-score plot In the TeX file, a plot has been inserted here Model number 10 # 74 # Note: Inside/Outside RMS Z-score plot In the TeX file, a plot has been inserted here Model number 11 # 75 # Note: Inside/Outside RMS Z-score plot In the TeX file, a plot has been inserted here Model number 12 # 76 # Note: Inside/Outside RMS Z-score plot In the TeX file, a plot has been inserted here Model number 13 # 77 # Note: Inside/Outside RMS Z-score plot In the TeX file, a plot has been inserted here Model number 14 # 78 # Note: Inside/Outside RMS Z-score plot In the TeX file, a plot has been inserted here Model number 15 # 79 # Note: Inside/Outside RMS Z-score plot In the TeX file, a plot has been inserted here Model number 16 # 80 # Note: Inside/Outside RMS Z-score plot In the TeX file, a plot has been inserted here Model number 17 # 81 # Note: Inside/Outside RMS Z-score plot In the TeX file, a plot has been inserted here Model number 18 # 82 # Note: Inside/Outside RMS Z-score plot In the TeX file, a plot has been inserted here Model number 19 # 83 # Note: Inside/Outside RMS Z-score plot In the TeX file, a plot has been inserted here Model number 20 # 84 # Note: Secondary structure This is the secondary structure according to DSSP. Only helix (H), strand (S), turn (T) and coil (blank) are shown. [REF] Secondary structure assignment 10 20 30 40 50 60 | | | | | | 1 - 60 DPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERA 1 - 60 T TTTTTTTTT TTT T HHHHHHHTT HHHHHHHHHHT TTT 61 - 67 AGMGSYV 61 - 67 70 80 90 100 110 120 | | | | | | 68 - 127 DPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERA 68 - 127 TTT333TTT TTTT T HHHHHHHTT HHHHHHHHHH TT TTTT 130 | 128 - 134 AGMGSYV 128 - 134 140 150 160 170 180 190 | | | | | | 135 - 194 DPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERA 135 - 194 TT TTTTT TTTT TTT T HHHHHHHTT HHHHHHHHHH TT TTT 200 | 195 - 201 AGMGSYV 195 - 201 210 220 230 240 250 260 | | | | | | 202 - 261 DPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERA 202 - 261 T TT TTT3333TTT TTTT T HHHHHHHTT HHHHHHHHHH T TTTT 262 - 268 AGMGSYV 262 - 268 270 280 290 300 310 320 | | | | | | 269 - 328 DPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERA 269 - 328 TTT3333TTSSTTTTSS T HHHHHHHTT HHHHHHHHHHT T TTT 330 | 329 - 335 AGMGSYV 329 - 335 340 350 360 370 380 390 | | | | | | 336 - 395 DPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERA 336 - 395 333 T TTT333TTTT TTTT T HHHHHHHTT HHHHHHHHHH T TTTT 400 | 396 - 402 AGMGSYV 396 - 402 410 420 430 440 450 460 | | | | | | 403 - 462 DPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERA 403 - 462 T TTT333TTTT TTTT T HHHHHHHTT HHHHHHHHHHTTT TTTT 463 - 469 AGMGSYV 463 - 469 470 480 490 500 510 520 | | | | | | 470 - 529 DPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERA 470 - 529 TTTTTTT T TTT TTHHHHHHHTT HHHHHHHHHH TTTTT 530 | 530 - 536 AGMGSYV 530 - 536 540 550 560 570 580 590 | | | | | | 537 - 596 DPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERA 537 - 596 T TTTTTTTTTT TTT TTHHHHHHHTT HHHHHHHHHHHHTTT TTTTT T 600 | 597 - 603 AGMGSYV 597 - 603 T 610 620 630 640 650 660 | | | | | | 604 - 663 DPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERA 604 - 663 T TTTTT TTTT TTT TTHHHHHHHTT HHHHHHHHHHT T333 670 | 664 - 670 AGMGSYV 664 - 670 680 690 700 710 720 730 | | | | | | 671 - 730 DPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERA 671 - 730 T TT TTTTT TTTT TTTT T HHHHHHHHT HHHHHHHHHHTT TTTT 731 - 737 AGMGSYV 731 - 737 740 750 760 770 780 790 | | | | | | 738 - 797 DPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERA 738 - 797 T TTTTTTTTTSSTTTTSS T HHHHHHHTT HHHHHHHHHH T TTT 800 | 798 - 804 AGMGSYV 798 - 804 810 820 830 840 850 860 | | | | | | 805 - 864 DPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERA 805 - 864 T TTT333TTTT TTTT T HHHHHHHTT HHHHHHHHHH TT TTTTT T 870 | 865 - 871 AGMGSYV 865 - 871 880 890 900 910 920 930 | | | | | | 872 - 931 DPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERA 872 - 931 T T TTT3333TT TTT T HHHHHHHHT HHHHHHHHHHHHT TTTT T 932 - 938 AGMGSYV 932 - 938 940 950 960 970 980 990 | | | | | | 939 - 998 DPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERA 939 - 998 TT TTT333TTTSSTTTTSS T HHHHHHHTT HHHHHHHHHH TT TTT 1000 | 999 -1005 AGMGSYV 999 -1005 1010 1020 1030 1040 1050 1060 | | | | | | 1006 -1065 DPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERA 1006 -1065 T TT TTTTTTTTTT TTT T HHHHHHHTT HHHHHHHHHHTT TTTTT 1070 | 1066 -1072 AGMGSYV 1066 -1072 1080 1090 1100 1110 1120 1130 | | | | | | 1073 -1132 DPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERA 1073 -1132 T T TTT3333TTSSTTTTSS T HHHHHHHTT HHHHHHHHHH TT TTTT T 1133 -1139 AGMGSYV 1133 -1139 1140 1150 1160 1170 1180 1190 | | | | | | 1140 -1199 DPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERA 1140 -1199 T T TTTTT TTTT TTTT T HHHHHHHTT HHHHHHHHHHHT TTTTT T 1200 | 1200 -1206 AGMGSYV 1200 -1206 1210 1220 1230 1240 1250 1260 | | | | | | 1207 -1266 DPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERA 1207 -1266 T T TTT3333TTT TTT T HHHHHHHHT HHHHHHHHHHTT TTTTT T 1270 | 1267 -1273 AGMGSYV 1267 -1273 1280 1290 1300 1310 1320 1330 | | | | | | 1274 -1333 DPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERA 1274 -1333 T TTT3333TTT TTTT T HHHHHHHHT HHHHHHHHHHT TTTTTT 1340 | 1334 -1340 AGMGSYV 1334 -1340 # 85 # Error: Abnormally short interatomic distances The pairs of atoms listed in the table below have an unusually short distance. The contact distances of all atom pairs have been checked. Two atoms are said to `bump' if they are closer than the sum of their Van der Waals radii minus 0.40 Angstrom. For hydrogen bonded pairs a tolerance of 0.55 Angstrom is used. The first number in the table tells you how much shorter that specific contact is than the acceptable limit. The second distance is the distance between the centers of the two atoms. The last text-item on each line represents the status of the atom pair. The text `INTRA' means that the bump is between atoms that are explicitly listed in the PDB file. `INTER' means it is an inter-symmetry bump. If the final column contains the text 'HB', the bump criterium was relaxed because there could be a hydrogen bond. Similarly relaxed criteria are used for 1--3 and 1--4 interactions (listed as 'B2' and 'B3', respectively). If the last column is 'BF', the sum of the B-factors of the atoms is higher than 80, which makes the appearance of the bump somewhat less severe because the atoms probably aren't there anyway. Bumps between atoms for which the sum of their occupancies is lower than one are not reported. In any case, each bump is listed in only one direction. 691 CYS ( 21 ) 11 SG -- 710 HIS ( 40 ) 11 CE1 0.514 2.886 INTRA 1227 CYS ( 21 ) 19 SG -- 1246 HIS ( 40 ) 19 CE1 0.512 2.888 INTRA 490 CYS ( 21 ) 8 SG -- 509 HIS ( 40 ) 8 CE1 0.491 2.909 INTRA 892 CYS ( 21 ) 14 SG -- 911 HIS ( 40 ) 14 CE1 0.488 2.912 INTRA 1160 CYS ( 21 ) 18 SG -- 1179 HIS ( 40 ) 18 CE1 0.484 2.916 INTRA 423 CYS ( 21 ) 7 SG -- 442 HIS ( 40 ) 7 CE1 0.476 2.924 INTRA 825 CYS ( 21 ) 13 SG -- 844 HIS ( 40 ) 13 CE1 0.474 2.926 INTRA 289 CYS ( 21 ) 5 SG -- 308 HIS ( 40 ) 5 CE1 0.467 2.933 INTRA 557 CYS ( 21 ) 9 SG -- 576 HIS ( 40 ) 9 CE1 0.466 2.934 INTRA 1294 CYS ( 21 ) 20 SG -- 1313 HIS ( 40 ) 20 CE1 0.466 2.934 INTRA 356 CYS ( 21 ) 6 SG -- 375 HIS ( 40 ) 6 CE1 0.466 2.934 INTRA 222 CYS ( 21 ) 4 SG -- 241 HIS ( 40 ) 4 CE1 0.465 2.935 INTRA 624 CYS ( 21 ) 10 SG -- 643 HIS ( 40 ) 10 CE1 0.463 2.937 INTRA 88 CYS ( 21 ) 2 SG -- 107 HIS ( 40 ) 2 CE1 0.463 2.937 INTRA 155 CYS ( 21 ) 3 SG -- 174 HIS ( 40 ) 3 CE1 0.457 2.943 INTRA 21 CYS ( 21 ) 1 SG -- 40 HIS ( 40 ) 1 CE1 0.456 2.944 INTRA 959 CYS ( 21 ) 15 SG -- 978 HIS ( 40 ) 15 CE1 0.455 2.945 INTRA 1026 CYS ( 21 ) 16 SG -- 1045 HIS ( 40 ) 16 CE1 0.452 2.948 INTRA 1093 CYS ( 21 ) 17 SG -- 1112 HIS ( 40 ) 17 CE1 0.451 2.949 INTRA 758 CYS ( 21 ) 12 SG -- 777 HIS ( 40 ) 12 CE1 0.451 2.949 INTRA 413 PRO ( 11 ) 7 CD -- 426 TYR ( 24 ) 7 CD1 0.437 2.763 INTRA 634 LEU ( 31 ) 10 CD1 -- 638 PHE ( 35 ) 10 CZ 0.435 2.765 INTRA 419 ARG ( 17 ) 7 CG -- 420 CYS ( 18 ) 7 N 0.434 2.666 INTRA 624 CYS ( 21 ) 10 SG -- 643 HIS ( 40 ) 10 ND1 0.428 2.872 INTRA 1156 ARG ( 17 ) 18 CG -- 1157 CYS ( 18 ) 18 N 0.428 2.672 INTRA 621 CYS ( 18 ) 10 SG -- 643 HIS ( 40 ) 10 CE1 0.427 2.973 INTRA 484 LEU ( 15 ) 8 CD1 -- 485 HIS ( 16 ) 8 CE1 0.426 2.774 INTRA 911 HIS ( 40 ) 14 CG -- 1367 ZIN ( 68 ) 14 ZN1 0.424 2.776 INTRA 1170 LEU ( 31 ) 18 CD2 -- 1174 PHE ( 35 ) 18 CZ 0.418 2.782 INTRA 1294 CYS ( 21 ) 20 SG -- 1313 HIS ( 40 ) 20 ND1 0.417 2.883 INTRA 642 ASP ( 39 ) 10 CG -- 643 HIS ( 40 ) 10 N 0.416 2.684 INTRA 85 CYS ( 18 ) 2 SG -- 107 HIS ( 40 ) 2 CE1 0.413 2.987 INTRA 18 CYS ( 18 ) 1 SG -- 40 HIS ( 40 ) 1 CE1 0.412 2.988 INTRA 423 CYS ( 21 ) 7 SG -- 442 HIS ( 40 ) 7 ND1 0.409 2.891 INTRA 1160 CYS ( 21 ) 18 SG -- 1179 HIS ( 40 ) 18 ND1 0.407 2.893 INTRA 490 CYS ( 21 ) 8 SG -- 509 HIS ( 40 ) 8 ND1 0.406 2.894 INTRA 1227 CYS ( 21 ) 19 SG -- 1246 HIS ( 40 ) 19 ND1 0.403 2.897 INTRA 88 CYS ( 21 ) 2 SG -- 107 HIS ( 40 ) 2 ND1 0.402 2.898 INTRA 413 PRO ( 11 ) 7 CG -- 426 TYR ( 24 ) 7 CD1 0.400 2.800 INTRA 1179 HIS ( 40 ) 18 CG -- 1375 ZIN ( 68 ) 18 ZN1 0.398 2.802 INTRA 956 CYS ( 18 ) 15 SG -- 978 HIS ( 40 ) 15 CE1 0.396 3.004 INTRA 353 CYS ( 18 ) 6 SG -- 375 HIS ( 40 ) 6 CE1 0.392 3.008 INTRA 1121 VAL ( 49 ) 17 CG2 -- 1122 GLU ( 50 ) 17 N 0.392 2.708 INTRA 232 LEU ( 31 ) 4 CD2 -- 236 PHE ( 35 ) 4 CZ 0.389 2.811 INTRA 609 PHE ( 6 ) 10 CE2 -- 616 GLY ( 13 ) 10 N 0.384 2.716 INTRA 219 CYS ( 18 ) 4 SG -- 241 HIS ( 40 ) 4 NE2 0.382 2.768 INTRA HB 356 CYS ( 21 ) 6 SG -- 375 HIS ( 40 ) 6 ND1 0.382 2.918 INTRA 755 CYS ( 18 ) 12 SG -- 777 HIS ( 40 ) 12 NE2 0.377 2.773 INTRA HB 710 HIS ( 40 ) 11 CG -- 1361 ZIN ( 68 ) 11 ZN1 0.377 2.823 INTRA 1090 CYS ( 18 ) 17 SG -- 1112 HIS ( 40 ) 17 NE2 0.376 2.774 INTRA HB 1023 CYS ( 18 ) 16 SG -- 1045 HIS ( 40 ) 16 NE2 0.375 2.775 INTRA HB 956 CYS ( 18 ) 15 SG -- 978 HIS ( 40 ) 15 NE2 0.375 2.775 INTRA HB 1304 LEU ( 31 ) 20 CD2 -- 1308 PHE ( 35 ) 20 CZ 0.374 2.826 INTRA 85 CYS ( 18 ) 2 SG -- 107 HIS ( 40 ) 2 NE2 0.374 2.776 INTRA HB 835 LEU ( 31 ) 13 CD1 -- 836 LYS ( 32 ) 13 N 0.373 2.727 INTRA 18 CYS ( 18 ) 1 SG -- 40 HIS ( 40 ) 1 NE2 0.372 2.778 INTRA HB 152 CYS ( 18 ) 3 SG -- 174 HIS ( 40 ) 3 NE2 0.371 2.779 INTRA HB 1023 CYS ( 18 ) 16 SG -- 1045 HIS ( 40 ) 16 CE1 0.369 3.031 INTRA 353 CYS ( 18 ) 6 SG -- 375 HIS ( 40 ) 6 NE2 0.369 2.781 INTRA HB 755 CYS ( 18 ) 12 SG -- 777 HIS ( 40 ) 12 CE1 0.369 3.031 INTRA 286 CYS ( 18 ) 5 SG -- 308 HIS ( 40 ) 5 NE2 0.369 2.781 INTRA HB 554 CYS ( 18 ) 9 SG -- 576 HIS ( 40 ) 9 NE2 0.368 2.782 INTRA HB 889 CYS ( 18 ) 14 SG -- 911 HIS ( 40 ) 14 NE2 0.366 2.784 INTRA HB 1163 TYR ( 24 ) 18 C -- 1164 PHE ( 25 ) 18 CD1 0.366 2.834 INTRA 609 PHE ( 6 ) 10 CD2 -- 616 GLY ( 13 ) 10 CA 0.366 2.834 INTRA 165 LEU ( 31 ) 3 CD2 -- 169 PHE ( 35 ) 3 CZ 0.365 2.835 INTRA 1237 LEU ( 31 ) 19 CD1 -- 1241 PHE ( 35 ) 19 CE2 0.363 2.837 INTRA 560 TYR ( 24 ) 9 C -- 561 PHE ( 25 ) 9 CD1 0.363 2.837 INTRA 286 CYS ( 18 ) 5 SG -- 308 HIS ( 40 ) 5 CE1 0.360 3.040 INTRA 1291 CYS ( 18 ) 20 SG -- 1313 HIS ( 40 ) 20 CE1 0.359 3.041 INTRA 688 CYS ( 18 ) 11 SG -- 710 HIS ( 40 ) 11 NE2 0.359 2.791 INTRA HB 1291 CYS ( 18 ) 20 SG -- 1313 HIS ( 40 ) 20 NE2 0.359 2.791 INTRA HB 822 CYS ( 18 ) 13 SG -- 844 HIS ( 40 ) 13 NE2 0.358 2.792 INTRA HB 420 CYS ( 18 ) 7 SG -- 442 HIS ( 40 ) 7 NE2 0.355 2.795 INTRA HB 413 PRO ( 11 ) 7 CD -- 426 TYR ( 24 ) 7 CE1 0.354 2.846 INTRA 484 LEU ( 15 ) 8 CD1 -- 485 HIS ( 16 ) 8 ND1 0.354 2.746 INTRA 500 LEU ( 31 ) 8 CD2 -- 504 PHE ( 35 ) 8 CZ 0.352 2.848 INTRA 317 VAL ( 49 ) 5 CG2 -- 318 GLU ( 50 ) 5 N 0.352 2.748 INTRA 691 CYS ( 21 ) 11 SG -- 710 HIS ( 40 ) 11 ND1 0.351 2.949 INTRA 652 VAL ( 49 ) 10 CG2 -- 653 GLU ( 50 ) 10 N 0.350 2.750 INTRA 1246 HIS ( 40 ) 19 CG -- 1377 ZIN ( 68 ) 19 ZN1 0.350 2.850 INTRA 1289 HIS ( 16 ) 20 CE1 -- 1301 SER ( 28 ) 20 CB 0.349 2.851 INTRA 21 CYS ( 21 ) 1 SG -- 40 HIS ( 40 ) 1 ND1 0.347 2.953 INTRA 487 CYS ( 18 ) 8 SG -- 509 HIS ( 40 ) 8 CE1 0.347 3.053 INTRA 420 CYS ( 18 ) 7 SG -- 442 HIS ( 40 ) 7 CE1 0.345 3.055 INTRA 825 CYS ( 21 ) 13 SG -- 844 HIS ( 40 ) 13 ND1 0.344 2.956 INTRA 621 CYS ( 18 ) 10 SG -- 643 HIS ( 40 ) 10 NE2 0.343 2.807 INTRA HB 487 CYS ( 18 ) 8 SG -- 509 HIS ( 40 ) 8 NE2 0.343 2.807 INTRA HB 1103 LEU ( 31 ) 17 CD2 -- 1107 PHE ( 35 ) 17 CZ 0.342 2.858 INTRA 892 CYS ( 21 ) 14 SG -- 911 HIS ( 40 ) 14 ND1 0.339 2.961 INTRA 557 CYS ( 21 ) 9 SG -- 576 HIS ( 40 ) 9 ND1 0.338 2.962 INTRA 346 PRO ( 11 ) 6 CG -- 359 TYR ( 24 ) 6 CD1 0.337 2.863 INTRA 219 CYS ( 18 ) 4 SG -- 241 HIS ( 40 ) 4 CE1 0.335 3.065 INTRA 1157 CYS ( 18 ) 18 SG -- 1179 HIS ( 40 ) 18 NE2 0.334 2.816 INTRA HB 937 TYR ( 66 ) 14 CG -- 938 VAL ( 67 ) 14 N 0.332 2.768 INTRA 567 LEU ( 31 ) 9 CD2 -- 571 PHE ( 35 ) 9 CZ 0.331 2.869 INTRA 83 HIS ( 16 ) 2 CE1 -- 95 SER ( 28 ) 2 CB 0.330 2.870 INTRA 1224 CYS ( 18 ) 19 SG -- 1246 HIS ( 40 ) 19 NE2 0.327 2.823 INTRA HB 150 HIS ( 16 ) 3 CE1 -- 162 SER ( 28 ) 3 CB 0.326 2.874 INTRA 627 TYR ( 24 ) 10 C -- 628 PHE ( 25 ) 10 CD1 0.326 2.874 INTRA 1090 CYS ( 18 ) 17 SG -- 1112 HIS ( 40 ) 17 CE1 0.325 3.075 INTRA 334 TYR ( 66 ) 5 CG -- 335 VAL ( 67 ) 5 N 0.324 2.776 INTRA 152 CYS ( 18 ) 3 SG -- 174 HIS ( 40 ) 3 CE1 0.322 3.078 INTRA 480 PRO ( 11 ) 8 CD -- 493 TYR ( 24 ) 8 CD1 0.320 2.880 INTRA 1230 TYR ( 24 ) 19 C -- 1231 PHE ( 25 ) 19 CD1 0.319 2.881 INTRA 844 HIS ( 40 ) 13 CG -- 1365 ZIN ( 68 ) 13 ZN1 0.318 2.882 INTRA 1071 TYR ( 66 ) 16 CG -- 1072 VAL ( 67 ) 16 N 0.317 2.783 INTRA 1313 HIS ( 40 ) 20 CG -- 1379 ZIN ( 68 ) 20 ZN1 0.308 2.892 INTRA 554 CYS ( 18 ) 9 SG -- 576 HIS ( 40 ) 9 CE1 0.308 3.092 INTRA 902 LEU ( 31 ) 14 CD2 -- 906 PHE ( 35 ) 14 CZ 0.308 2.892 INTRA 442 HIS ( 40 ) 7 CG -- 1353 ZIN ( 68 ) 7 ZN1 0.308 2.892 INTRA 1170 LEU ( 31 ) 18 CD1 -- 1174 PHE ( 35 ) 18 CE2 0.305 2.895 INTRA 155 CYS ( 21 ) 3 SG -- 174 HIS ( 40 ) 3 ND1 0.305 2.995 INTRA 1255 VAL ( 49 ) 19 CG1 -- 1256 GLU ( 50 ) 19 N 0.303 2.797 INTRA 1093 CYS ( 21 ) 17 SG -- 1112 HIS ( 40 ) 17 ND1 0.301 2.999 INTRA 500 LEU ( 31 ) 8 CD1 -- 504 PHE ( 35 ) 8 CE2 0.300 2.900 INTRA 485 HIS ( 16 ) 8 CE1 -- 497 SER ( 28 ) 8 CB 0.298 2.902 INTRA 232 LEU ( 31 ) 4 CD1 -- 236 PHE ( 35 ) 4 CE2 0.297 2.903 INTRA 1304 LEU ( 31 ) 20 CD1 -- 1305 LYS ( 32 ) 20 N 0.292 2.808 INTRA 585 VAL ( 49 ) 9 CG1 -- 586 GLU ( 50 ) 9 N 0.290 2.810 INTRA 222 CYS ( 21 ) 4 SG -- 241 HIS ( 40 ) 4 ND1 0.290 3.010 INTRA 547 PRO ( 11 ) 9 CG -- 560 TYR ( 24 ) 9 CD1 0.289 2.911 INTRA 98 LEU ( 31 ) 2 CD1 -- 102 PHE ( 35 ) 2 CZ 0.289 2.911 INTRA 351 HIS ( 16 ) 6 CE1 -- 363 SER ( 28 ) 6 CB 0.288 2.912 INTRA 959 CYS ( 21 ) 15 SG -- 978 HIS ( 40 ) 15 ND1 0.284 3.016 INTRA 701 LEU ( 31 ) 11 CD1 -- 705 PHE ( 35 ) 11 CE2 0.283 2.917 INTRA 681 PRO ( 11 ) 11 CG -- 694 TYR ( 24 ) 11 CD1 0.283 2.917 INTRA 628 PHE ( 25 ) 10 CD1 -- 634 LEU ( 31 ) 10 CD2 0.280 2.920 INTRA 671 ASP ( 1 ) 11 N -- 672 PRO ( 2 ) 11 CD 0.278 2.722 INTRA 1224 CYS ( 18 ) 19 SG -- 1246 HIS ( 40 ) 19 CE1 0.275 3.125 INTRA 990 TYR ( 52 ) 15 CD1 -- 991 SER ( 53 ) 15 N 0.274 2.826 INTRA 1237 LEU ( 31 ) 19 CD2 -- 1241 PHE ( 35 ) 19 CZ 0.274 2.926 INTRA 289 CYS ( 21 ) 5 SG -- 308 HIS ( 40 ) 5 ND1 0.273 3.027 INTRA 758 CYS ( 21 ) 12 SG -- 777 HIS ( 40 ) 12 ND1 0.273 3.027 INTRA 433 LEU ( 31 ) 7 CD1 -- 437 PHE ( 35 ) 7 CZ 0.272 2.928 INTRA 509 HIS ( 40 ) 8 CG -- 1355 ZIN ( 68 ) 8 ZN1 0.270 2.930 INTRA 1274 ASP ( 1 ) 20 N -- 1275 PRO ( 2 ) 20 CD 0.270 2.730 INTRA 552 HIS ( 16 ) 9 O -- 553 ARG ( 17 ) 9 C 0.270 2.530 INTRA 828 TYR ( 24 ) 13 C -- 829 PHE ( 25 ) 13 CD1 0.270 2.930 INTRA 455 SER ( 53 ) 7 O -- 456 GLN ( 54 ) 7 C 0.269 2.531 INTRA 990 TYR ( 52 ) 15 CG -- 991 SER ( 53 ) 15 N 0.269 2.831 INTRA 299 LEU ( 31 ) 5 CD1 -- 303 PHE ( 35 ) 5 CZ 0.267 2.933 INTRA 638 PHE ( 35 ) 10 O -- 639 ARG ( 36 ) 10 C 0.265 2.535 INTRA 217 HIS ( 16 ) 4 CE1 -- 229 SER ( 28 ) 4 CB 0.262 2.938 INTRA 576 HIS ( 40 ) 9 CG -- 1357 ZIN ( 68 ) 9 ZN1 0.262 2.938 INTRA 337 PRO ( 2 ) 6 O -- 338 ASN ( 3 ) 6 C 0.262 2.538 INTRA 885 GLY ( 14 ) 14 CA -- 888 ARG ( 17 ) 14 NH1 0.260 2.840 INTRA 1026 CYS ( 21 ) 16 SG -- 1045 HIS ( 40 ) 16 ND1 0.257 3.043 INTRA 1036 LEU ( 31 ) 16 CD1 -- 1040 PHE ( 35 ) 16 CZ 0.257 2.943 INTRA 1030 PHE ( 25 ) 16 CE1 -- 1039 HIS ( 34 ) 16 CG 0.256 2.944 INTRA 604 ASP ( 1 ) 10 N -- 605 PRO ( 2 ) 10 CD 0.256 2.744 INTRA 628 PHE ( 25 ) 10 CE1 -- 634 LEU ( 31 ) 10 CD2 0.254 2.946 INTRA 748 PRO ( 11 ) 12 CG -- 761 TYR ( 24 ) 12 CD1 0.252 2.948 INTRA 165 LEU ( 31 ) 3 CD1 -- 166 LYS ( 32 ) 3 N 0.251 2.849 INTRA 548 GLY ( 12 ) 9 O -- 552 HIS ( 16 ) 9 CD2 0.251 2.549 INTRA 822 CYS ( 18 ) 13 SG -- 844 HIS ( 40 ) 13 CE1 0.250 3.150 INTRA 426 TYR ( 24 ) 7 C -- 427 PHE ( 25 ) 7 CD1 0.250 2.950 INTRA 950 GLY ( 12 ) 15 O -- 954 HIS ( 16 ) 15 CD2 0.250 2.550 INTRA 854 GLU ( 50 ) 13 CB -- 855 PRO ( 51 ) 13 CD 0.249 2.951 INTRA 1157 CYS ( 18 ) 18 SG -- 1179 HIS ( 40 ) 18 CE1 0.249 3.151 INTRA 11 PRO ( 11 ) 1 CG -- 24 TYR ( 24 ) 1 CD1 0.247 2.953 INTRA 815 PRO ( 11 ) 13 CG -- 828 TYR ( 24 ) 13 CD1 0.246 2.954 INTRA 107 HIS ( 40 ) 2 CG -- 1343 ZIN ( 68 ) 2 ZN1 0.246 2.954 INTRA 680 LEU ( 10 ) 11 CD2 -- 687 ARG ( 17 ) 11 NH1 0.244 2.856 INTRA 78 PRO ( 11 ) 2 CG -- 91 TYR ( 24 ) 2 CD1 0.242 2.958 INTRA 643 HIS ( 40 ) 10 CG -- 1359 ZIN ( 68 ) 10 ZN1 0.242 2.958 INTRA 1308 PHE ( 35 ) 20 O -- 1309 ARG ( 36 ) 20 C 0.242 2.558 INTRA 437 PHE ( 35 ) 7 O -- 438 ARG ( 36 ) 7 C 0.242 2.558 INTRA 366 LEU ( 31 ) 6 CD2 -- 370 PHE ( 35 ) 6 CZ 0.241 2.959 INTRA 267 TYR ( 66 ) 4 CG -- 268 VAL ( 67 ) 4 N 0.240 2.860 INTRA 969 LEU ( 31 ) 15 CD2 -- 973 PHE ( 35 ) 15 CZ 0.239 2.961 INTRA 705 PHE ( 35 ) 11 O -- 706 ARG ( 36 ) 11 C 0.239 2.561 INTRA 280 GLY ( 12 ) 5 O -- 284 HIS ( 16 ) 5 CD2 0.237 2.563 INTRA 701 LEU ( 31 ) 11 CD1 -- 705 PHE ( 35 ) 11 CZ 0.233 2.967 INTRA 255 GLN ( 54 ) 4 O -- 256 GLU ( 55 ) 4 C 0.233 2.567 INTRA 835 LEU ( 31 ) 13 CD2 -- 839 PHE ( 35 ) 13 CZ 0.233 2.967 INTRA 418 HIS ( 16 ) 7 O -- 419 ARG ( 17 ) 7 C 0.231 2.569 INTRA 375 HIS ( 40 ) 6 CG -- 1351 ZIN ( 68 ) 6 ZN1 0.230 2.970 INTRA 151 ARG ( 17 ) 3 NE -- 158 TYR ( 24 ) 3 CE1 0.230 2.870 INTRA 940 PRO ( 2 ) 15 O -- 941 ASN ( 3 ) 15 C 0.228 2.572 INTRA 433 LEU ( 31 ) 7 CD1 -- 437 PHE ( 35 ) 7 CE2 0.228 2.972 INTRA 676 PHE ( 6 ) 11 CD2 -- 683 GLY ( 13 ) 11 CA 0.227 2.973 INTRA 92 PHE ( 25 ) 2 CE2 -- 101 HIS ( 34 ) 2 CG 0.225 2.975 INTRA 671 ASP ( 1 ) 11 CG -- 672 PRO ( 2 ) 11 N 0.225 2.875 INTRA 663 ALA ( 60 ) 10 O -- 664 ALA ( 61 ) 10 CB 0.225 2.575 INTRA 571 PHE ( 35 ) 9 O -- 572 ARG ( 36 ) 9 C 0.223 2.577 INTRA 861 ALA ( 57 ) 13 O -- 862 GLU ( 58 ) 13 CB 0.222 2.578 INTRA 1304 LEU ( 31 ) 20 CD2 -- 1308 PHE ( 35 ) 20 CE1 0.221 2.979 INTRA 169 PHE ( 35 ) 3 O -- 170 ARG ( 36 ) 3 C 0.221 2.579 INTRA 102 PHE ( 35 ) 2 O -- 103 ARG ( 36 ) 2 C 0.221 2.579 INTRA 366 LEU ( 31 ) 6 CD1 -- 370 PHE ( 35 ) 6 CZ 0.220 2.980 INTRA 553 ARG ( 17 ) 9 CG -- 554 CYS ( 18 ) 9 N 0.220 2.880 INTRA 370 PHE ( 35 ) 6 O -- 371 ARG ( 36 ) 6 C 0.219 2.581 INTRA 1239 THR ( 33 ) 19 O -- 1242 ARG ( 36 ) 19 CG 0.219 2.581 INTRA 1205 TYR ( 66 ) 18 CZ -- 1206 VAL ( 67 ) 18 CG1 0.219 2.981 INTRA 839 PHE ( 35 ) 13 O -- 840 ARG ( 36 ) 13 C 0.218 2.582 INTRA 614 PRO ( 11 ) 10 CG -- 627 TYR ( 24 ) 10 CD1 0.218 2.982 INTRA 747 LEU ( 10 ) 12 CD1 -- 750 GLY ( 13 ) 12 C 0.218 2.982 INTRA 338 ASN ( 3 ) 6 O -- 339 ALA ( 4 ) 6 C 0.217 2.583 INTRA 672 PRO ( 2 ) 11 O -- 673 ASN ( 3 ) 11 C 0.216 2.584 INTRA 1112 HIS ( 40 ) 17 CG -- 1373 ZIN ( 68 ) 17 ZN1 0.216 2.984 INTRA 1193 GLN ( 54 ) 18 O -- 1194 GLU ( 55 ) 18 CB 0.216 2.584 INTRA 1021 HIS ( 16 ) 16 O -- 1022 ARG ( 17 ) 16 C 0.215 2.585 INTRA 806 PRO ( 2 ) 13 O -- 807 ASN ( 3 ) 13 C 0.215 2.585 INTRA 1275 PRO ( 2 ) 20 O -- 1276 ASN ( 3 ) 20 C 0.214 2.586 INTRA 719 VAL ( 49 ) 11 O -- 720 GLU ( 50 ) 11 C 0.214 2.586 INTRA 1208 PRO ( 2 ) 19 O -- 1209 ASN ( 3 ) 19 C 0.214 2.586 INTRA 404 PRO ( 2 ) 7 O -- 405 ASN ( 3 ) 7 C 0.214 2.586 INTRA 2 PRO ( 2 ) 1 O -- 3 ASN ( 3 ) 1 C 0.214 2.586 INTRA 346 PRO ( 11 ) 6 CD -- 359 TYR ( 24 ) 6 CE1 0.213 2.987 INTRA 772 PHE ( 35 ) 12 O -- 773 ARG ( 36 ) 12 C 0.213 2.587 INTRA 873 PRO ( 2 ) 14 O -- 874 ASN ( 3 ) 14 C 0.213 2.587 INTRA 1040 PHE ( 35 ) 16 O -- 1041 ARG ( 36 ) 16 C 0.213 2.587 INTRA 1074 PRO ( 2 ) 17 O -- 1075 ASN ( 3 ) 17 C 0.213 2.587 INTRA 877 PHE ( 6 ) 14 CE1 -- 879 PRO ( 8 ) 14 N 0.212 2.888 INTRA 451 VAL ( 49 ) 7 O -- 452 GLU ( 50 ) 7 C 0.212 2.588 INTRA 1141 PRO ( 2 ) 18 O -- 1142 ASN ( 3 ) 18 C 0.212 2.588 INTRA 203 PRO ( 2 ) 4 O -- 204 ASN ( 3 ) 4 C 0.212 2.588 INTRA 303 PHE ( 35 ) 5 O -- 304 ARG ( 36 ) 5 C 0.211 2.589 INTRA 1007 PRO ( 2 ) 16 O -- 1008 ASN ( 3 ) 16 C 0.211 2.589 INTRA 634 LEU ( 31 ) 10 CD1 -- 638 PHE ( 35 ) 10 CE1 0.211 2.989 INTRA 120 SER ( 53 ) 2 O -- 121 GLN ( 54 ) 2 C 0.211 2.589 INTRA 1107 PHE ( 35 ) 17 O -- 1108 ARG ( 36 ) 17 C 0.211 2.589 INTRA 882 PRO ( 11 ) 14 O -- 888 ARG ( 17 ) 14 NH2 0.210 2.490 INTRA 455 SER ( 53 ) 7 C -- 456 GLN ( 54 ) 7 OE1 0.210 2.590 INTRA 174 HIS ( 40 ) 3 CG -- 1345 ZIN ( 68 ) 3 ZN1 0.210 2.990 INTRA 346 PRO ( 11 ) 6 CD -- 359 TYR ( 24 ) 6 CD1 0.209 2.991 INTRA 877 PHE ( 6 ) 14 CG -- 878 ASP ( 7 ) 14 N 0.209 2.891 INTRA 1298 PHE ( 25 ) 20 CE2 -- 1307 HIS ( 34 ) 20 CG 0.209 2.991 INTRA 1276 ASN ( 3 ) 20 O -- 1277 ALA ( 4 ) 20 C 0.209 2.591 INTRA 366 LEU ( 31 ) 6 CD2 -- 370 PHE ( 35 ) 6 CE1 0.209 2.991 INTRA 457 GLU ( 55 ) 7 O -- 458 GLU ( 56 ) 7 C 0.208 2.592 INTRA 906 PHE ( 35 ) 14 O -- 907 ARG ( 36 ) 14 C 0.208 2.592 INTRA 753 HIS ( 16 ) 12 ND1 -- 765 SER ( 28 ) 12 CB 0.208 2.892 INTRA 973 PHE ( 35 ) 15 O -- 974 ARG ( 36 ) 15 C 0.207 2.593 INTRA 31 LEU ( 31 ) 1 CD1 -- 35 PHE ( 35 ) 1 CZ 0.206 2.994 INTRA 236 PHE ( 35 ) 4 O -- 237 ARG ( 36 ) 4 C 0.205 2.595 INTRA 768 LEU ( 31 ) 12 CD2 -- 772 PHE ( 35 ) 12 CZ 0.205 2.995 INTRA 688 CYS ( 18 ) 11 SG -- 710 HIS ( 40 ) 11 CE1 0.205 3.195 INTRA 691 CYS ( 21 ) 11 O -- 692 ALA ( 22 ) 11 CB 0.204 2.596 INTRA 138 ALA ( 4 ) 3 O -- 139 GLU ( 5 ) 3 C 0.204 2.596 INTRA 507 LYS ( 38 ) 8 O -- 511 LYS ( 42 ) 8 CB 0.203 2.597 INTRA 694 TYR ( 24 ) 11 C -- 695 PHE ( 25 ) 11 CD1 0.203 2.997 INTRA 151 ARG ( 17 ) 3 CZ -- 158 TYR ( 24 ) 3 CE1 0.202 2.998 INTRA 1108 ARG ( 36 ) 17 O -- 1110 LYS ( 38 ) 17 N 0.201 2.499 INTRA 544 PRO ( 8 ) 9 O -- 545 ASP ( 9 ) 9 C 0.201 2.599 INTRA 1061 GLU ( 56 ) 16 O -- 1062 ALA ( 57 ) 16 C 0.201 2.599 INTRA 772 PHE ( 35 ) 12 O -- 774 SER ( 37 ) 12 N 0.201 2.499 INTRA 674 ALA ( 4 ) 11 O -- 675 GLU ( 5 ) 11 C 0.201 2.599 INTRA 1060 GLU ( 55 ) 16 O -- 1061 GLU ( 56 ) 16 C 0.201 2.599 INTRA 1210 ALA ( 4 ) 19 O -- 1211 GLU ( 5 ) 19 C 0.200 2.600 INTRA 474 GLU ( 5 ) 8 O -- 475 PHE ( 6 ) 8 C 0.200 2.600 INTRA 72 GLU ( 5 ) 2 O -- 73 PHE ( 6 ) 2 C 0.200 2.600 INTRA 739 PRO ( 2 ) 12 O -- 740 ASN ( 3 ) 12 C 0.200 2.600 INTRA 651 SER ( 48 ) 10 O -- 652 VAL ( 49 ) 10 C 0.199 2.601 INTRA 598 GLY ( 62 ) 9 C -- 599 MET ( 63 ) 9 CG 0.199 3.001 INTRA 136 PRO ( 2 ) 3 O -- 137 ASN ( 3 ) 3 C 0.199 2.601 INTRA 351 HIS ( 16 ) 6 O -- 352 ARG ( 17 ) 6 C 0.199 2.601 INTRA 942 ALA ( 4 ) 15 O -- 943 GLU ( 5 ) 15 C 0.199 2.601 INTRA 1321 SER ( 48 ) 20 O -- 1322 VAL ( 49 ) 20 C 0.199 2.601 INTRA 49 VAL ( 49 ) 1 CG2 -- 50 GLU ( 50 ) 1 N 0.197 2.903 INTRA 852 SER ( 48 ) 13 O -- 853 VAL ( 49 ) 13 C 0.197 2.603 INTRA 597 ALA ( 61 ) 9 O -- 598 GLY ( 62 ) 9 C 0.196 2.604 INTRA 870 TYR ( 66 ) 13 O -- 871 VAL ( 67 ) 13 C 0.196 2.604 INTRA 1200 ALA ( 61 ) 18 O -- 1201 GLY ( 62 ) 18 C 0.195 2.605 INTRA 541 GLU ( 5 ) 9 O -- 542 PHE ( 6 ) 9 C 0.194 2.606 INTRA 658 GLU ( 55 ) 10 O -- 659 GLU ( 56 ) 10 C 0.194 2.606 INTRA 991 SER ( 53 ) 15 O -- 993 GLU ( 55 ) 15 N 0.194 2.506 INTRA 1284 PRO ( 11 ) 20 CG -- 1297 TYR ( 24 ) 20 CD1 0.193 3.007 INTRA 217 HIS ( 16 ) 4 O -- 218 ARG ( 17 ) 4 C 0.193 2.607 INTRA 768 LEU ( 31 ) 12 CD1 -- 772 PHE ( 35 ) 12 CZ 0.193 3.007 INTRA 539 ASN ( 3 ) 9 O -- 540 ALA ( 4 ) 9 C 0.193 2.607 INTRA 1217 PRO ( 11 ) 19 CG -- 1230 TYR ( 24 ) 19 CD1 0.192 3.008 INTRA 35 PHE ( 35 ) 1 O -- 36 ARG ( 36 ) 1 C 0.192 2.608 INTRA 809 GLU ( 5 ) 13 O -- 810 PHE ( 6 ) 13 C 0.192 2.608 INTRA 929 GLU ( 58 ) 14 O -- 930 ARG ( 59 ) 14 C 0.192 2.608 INTRA 142 PRO ( 8 ) 3 O -- 143 ASP ( 9 ) 3 C 0.191 2.609 INTRA 598 GLY ( 62 ) 9 O -- 599 MET ( 63 ) 9 CG 0.191 2.609 INTRA 1308 PHE ( 35 ) 20 O -- 1310 SER ( 37 ) 20 N 0.191 2.509 INTRA 550 GLY ( 14 ) 9 C -- 552 HIS ( 16 ) 9 N 0.190 2.710 INTRA 732 GLY ( 62 ) 11 O -- 733 MET ( 63 ) 11 C 0.190 2.610 INTRA 486 ARG ( 17 ) 8 NH2 -- 488 LEU ( 19 ) 8 CD1 0.189 2.911 INTRA 158 TYR ( 24 ) 3 C -- 159 PHE ( 25 ) 3 CD1 0.189 3.011 INTRA 1155 HIS ( 16 ) 18 O -- 1156 ARG ( 17 ) 18 C 0.188 2.612 INTRA 772 PHE ( 35 ) 12 C -- 774 SER ( 37 ) 12 N 0.188 2.712 INTRA 315 LEU ( 47 ) 5 O -- 316 SER ( 48 ) 5 C 0.187 2.613 INTRA 1241 PHE ( 35 ) 19 C -- 1243 SER ( 37 ) 19 N 0.186 2.714 INTRA 741 ALA ( 4 ) 12 O -- 742 GLU ( 5 ) 12 C 0.185 2.615 INTRA 155 CYS ( 21 ) 3 O -- 156 ALA ( 22 ) 3 CB 0.185 2.615 INTRA 1127 GLU ( 55 ) 17 C -- 1128 GLU ( 56 ) 17 CG 0.184 3.016 INTRA 1144 GLU ( 5 ) 18 O -- 1145 PHE ( 6 ) 18 C 0.183 2.617 INTRA 69 PRO ( 2 ) 2 O -- 70 ASN ( 3 ) 2 C 0.183 2.617 INTRA 430 SER ( 28 ) 7 O -- 434 LYS ( 32 ) 7 CB 0.182 2.618 INTRA 889 CYS ( 18 ) 14 SG -- 911 HIS ( 40 ) 14 CE1 0.182 3.218 INTRA 1009 ALA ( 4 ) 16 O -- 1010 GLU ( 5 ) 16 C 0.180 2.620 INTRA 1122 GLU ( 50 ) 17 CB -- 1123 PRO ( 51 ) 17 CD 0.179 3.021 INTRA 1167 SER ( 28 ) 18 O -- 1171 LYS ( 32 ) 18 CB 0.179 2.621 INTRA 146 GLY ( 12 ) 3 O -- 150 HIS ( 16 ) 3 CD2 0.179 2.621 INTRA 272 ALA ( 4 ) 5 O -- 273 GLU ( 5 ) 5 C 0.178 2.622 INTRA 40 HIS ( 40 ) 1 CG -- 1341 ZIN ( 68 ) 1 ZN1 0.177 3.023 INTRA 115 SER ( 48 ) 2 O -- 116 VAL ( 49 ) 2 C 0.177 2.623 INTRA 433 LEU ( 31 ) 7 CD1 -- 434 LYS ( 32 ) 7 N 0.177 2.923 INTRA 241 HIS ( 40 ) 4 NE2 -- 245 LEU ( 44 ) 4 CD1 0.177 2.923 INTRA 241 HIS ( 40 ) 4 CG -- 1347 ZIN ( 68 ) 4 ZN1 0.176 3.024 INTRA 538 PRO ( 2 ) 9 O -- 539 ASN ( 3 ) 9 C 0.176 2.624 INTRA 1320 LEU ( 47 ) 20 O -- 1321 SER ( 48 ) 20 C 0.176 2.624 INTRA 1150 PRO ( 11 ) 18 CG -- 1163 TYR ( 24 ) 18 CD1 0.176 3.024 INTRA 954 HIS ( 16 ) 15 ND1 -- 966 SER ( 28 ) 15 CB 0.175 2.925 INTRA 1138 TYR ( 66 ) 17 CG -- 1139 VAL ( 67 ) 17 N 0.174 2.926 INTRA 624 CYS ( 21 ) 10 O -- 625 ALA ( 22 ) 10 CB 0.174 2.626 INTRA 482 GLY ( 13 ) 8 C -- 484 LEU ( 15 ) 8 N 0.174 2.726 INTRA 1021 HIS ( 16 ) 16 NE2 -- 1033 SER ( 28 ) 16 CB 0.174 2.926 INTRA 31 LEU ( 31 ) 1 CD2 -- 35 PHE ( 35 ) 1 CZ 0.173 3.027 INTRA 133 TYR ( 66 ) 2 O -- 134 VAL ( 67 ) 2 C 0.173 2.627 INTRA 139 GLU ( 5 ) 3 O -- 140 PHE ( 6 ) 3 C 0.172 2.628 INTRA 66 TYR ( 66 ) 1 O -- 67 VAL ( 67 ) 1 C 0.172 2.628 INTRA 1147 PRO ( 8 ) 18 O -- 1148 ASP ( 9 ) 18 C 0.172 2.628 INTRA 547 PRO ( 11 ) 9 CD -- 560 TYR ( 24 ) 9 CD1 0.172 3.028 INTRA 818 GLY ( 14 ) 13 O -- 821 ARG ( 17 ) 13 NE 0.171 2.529 INTRA 1021 HIS ( 16 ) 16 CE1 -- 1033 SER ( 28 ) 16 CB 0.171 3.029 INTRA 1244 LYS ( 38 ) 19 O -- 1248 LYS ( 42 ) 19 CB 0.170 2.630 INTRA 167 THR ( 33 ) 3 O -- 170 ARG ( 36 ) 3 CG 0.170 2.630 INTRA 120 SER ( 53 ) 2 C -- 121 GLN ( 54 ) 2 CD 0.170 3.030 INTRA 611 PRO ( 8 ) 10 O -- 612 ASP ( 9 ) 10 C 0.170 2.630 INTRA 425 ARG ( 23 ) 7 CG -- 426 TYR ( 24 ) 7 N 0.170 2.930 INTRA 480 PRO ( 11 ) 8 CG -- 493 TYR ( 24 ) 8 CD1 0.169 3.031 INTRA 232 LEU ( 31 ) 4 CD2 -- 236 PHE ( 35 ) 4 CE1 0.169 3.031 INTRA 601 SER ( 65 ) 9 O -- 602 TYR ( 66 ) 9 C 0.168 2.632 INTRA 919 SER ( 48 ) 14 O -- 920 VAL ( 49 ) 14 C 0.168 2.632 INTRA 370 PHE ( 35 ) 6 O -- 372 SER ( 37 ) 6 N 0.168 2.532 INTRA 122 GLU ( 55 ) 2 O -- 123 GLU ( 56 ) 2 C 0.168 2.632 INTRA 678 PRO ( 8 ) 11 O -- 679 ASP ( 9 ) 11 C 0.167 2.633 INTRA 205 ALA ( 4 ) 4 O -- 206 GLU ( 5 ) 4 C 0.167 2.633 INTRA 687 ARG ( 17 ) 11 NE -- 694 TYR ( 24 ) 11 CE1 0.166 2.934 INTRA 1155 HIS ( 16 ) 18 C -- 1156 ARG ( 17 ) 18 O 0.166 2.634 INTRA 140 PHE ( 6 ) 3 CD2 -- 147 GLY ( 13 ) 3 CA 0.166 3.034 INTRA 550 GLY ( 14 ) 9 O -- 551 LEU ( 15 ) 9 C 0.165 2.635 INTRA 366 LEU ( 31 ) 6 CD1 -- 370 PHE ( 35 ) 6 CE2 0.165 3.035 INTRA 604 ASP ( 1 ) 10 CB -- 605 PRO ( 2 ) 10 CD 0.164 3.036 INTRA 657 GLN ( 54 ) 10 O -- 658 GLU ( 55 ) 10 C 0.164 2.636 INTRA 876 GLU ( 5 ) 14 CG -- 877 PHE ( 6 ) 14 N 0.164 2.936 INTRA 477 PRO ( 8 ) 8 O -- 478 ASP ( 9 ) 8 C 0.164 2.636 INTRA 422 ALA ( 20 ) 7 CB -- 446 LEU ( 44 ) 7 CD2 0.163 3.037 INTRA 450 SER ( 48 ) 7 O -- 451 VAL ( 49 ) 7 C 0.163 2.637 INTRA 546 LEU ( 10 ) 9 CB -- 550 GLY ( 14 ) 9 CA 0.163 3.037 INTRA 1308 PHE ( 35 ) 20 C -- 1310 SER ( 37 ) 20 N 0.163 2.737 INTRA 130 MET ( 63 ) 2 SD -- 131 GLY ( 64 ) 2 N 0.163 3.137 INTRA 818 GLY ( 14 ) 13 O -- 821 ARG ( 17 ) 13 CZ 0.161 2.639 INTRA 1205 TYR ( 66 ) 18 CG -- 1206 VAL ( 67 ) 18 N 0.161 2.939 INTRA 719 VAL ( 49 ) 11 O -- 721 PRO ( 51 ) 11 N 0.161 2.539 INTRA 557 CYS ( 21 ) 9 O -- 558 ALA ( 22 ) 9 CB 0.160 2.640 INTRA 451 VAL ( 49 ) 7 O -- 453 PRO ( 51 ) 7 N 0.160 2.540 INTRA 370 PHE ( 35 ) 6 C -- 372 SER ( 37 ) 6 N 0.159 2.741 INTRA 1294 CYS ( 21 ) 20 O -- 1295 ALA ( 22 ) 20 CB 0.159 2.641 INTRA 949 PRO ( 11 ) 15 CG -- 962 TYR ( 24 ) 15 CD1 0.158 3.042 INTRA 276 PRO ( 8 ) 5 O -- 277 ASP ( 9 ) 5 C 0.157 2.643 INTRA 682 GLY ( 12 ) 11 O -- 686 HIS ( 16 ) 11 CD2 0.157 2.643 INTRA 194 ALA ( 60 ) 3 O -- 195 ALA ( 61 ) 3 C 0.157 2.643 INTRA 418 HIS ( 16 ) 7 C -- 419 ARG ( 17 ) 7 O 0.156 2.644 INTRA 1126 GLN ( 54 ) 17 O -- 1127 GLU ( 55 ) 17 C 0.156 2.644 INTRA 359 TYR ( 24 ) 6 C -- 360 PHE ( 25 ) 6 CD1 0.155 3.045 INTRA 1172 THR ( 33 ) 18 O -- 1175 ARG ( 36 ) 18 CG 0.155 2.645 INTRA 1160 CYS ( 21 ) 18 O -- 1161 ALA ( 22 ) 18 CB 0.155 2.645 INTRA 299 LEU ( 31 ) 5 CD1 -- 300 LYS ( 32 ) 5 N 0.154 2.946 INTRA 67 VAL ( 67 ) 1 CG1 -- 1342 VAL ( OXT ) 1 O2 0.153 2.647 INTRA 585 VAL ( 49 ) 9 O -- 586 GLU ( 50 ) 9 C 0.153 2.647 INTRA 502 THR ( 33 ) 8 O -- 505 ARG ( 36 ) 8 CG 0.152 2.648 INTRA 1036 LEU ( 31 ) 16 CD2 -- 1040 PHE ( 35 ) 16 CE1 0.151 3.049 INTRA 742 GLU ( 5 ) 12 O -- 743 PHE ( 6 ) 12 C 0.151 2.649 INTRA 1274 ASP ( 1 ) 20 CB -- 1275 PRO ( 2 ) 20 CD 0.149 3.051 INTRA 870 TYR ( 66 ) 13 CG -- 871 VAL ( 67 ) 13 N 0.149 2.951 INTRA 812 PRO ( 8 ) 13 O -- 813 ASP ( 9 ) 13 C 0.149 2.651 INTRA 637 HIS ( 34 ) 10 C -- 639 ARG ( 36 ) 10 N 0.148 2.752 INTRA 991 SER ( 53 ) 15 O -- 992 GLN ( 54 ) 15 C 0.148 2.652 INTRA 1177 LYS ( 38 ) 18 O -- 1181 LYS ( 42 ) 18 CB 0.148 2.652 INTRA 1016 PRO ( 11 ) 16 CB -- 1030 PHE ( 25 ) 16 O 0.147 2.653 INTRA 969 LEU ( 31 ) 15 CD2 -- 973 PHE ( 35 ) 15 CE1 0.147 3.053 INTRA 241 HIS ( 40 ) 4 CD2 -- 245 LEU ( 44 ) 4 CD1 0.147 3.053 INTRA 570 HIS ( 34 ) 9 CD2 -- 571 PHE ( 35 ) 9 N 0.147 2.953 INTRA 570 HIS ( 34 ) 9 C -- 572 ARG ( 36 ) 9 N 0.146 2.754 INTRA 1127 GLU ( 55 ) 17 O -- 1128 GLU ( 56 ) 17 CG 0.146 2.654 INTRA 768 LEU ( 31 ) 12 CD2 -- 772 PHE ( 35 ) 12 CE1 0.145 3.055 INTRA 803 TYR ( 66 ) 12 CD1 -- 804 VAL ( 67 ) 12 N 0.145 2.955 INTRA 255 GLN ( 54 ) 4 C -- 256 GLU ( 55 ) 4 CD 0.145 3.055 INTRA 1122 GLU ( 50 ) 17 N -- 1123 PRO ( 51 ) 17 CD 0.145 2.855 INTRA 820 HIS ( 16 ) 13 C -- 821 ARG ( 17 ) 13 O 0.144 2.656 INTRA 1192 SER ( 53 ) 18 C -- 1193 GLN ( 54 ) 18 O 0.143 2.657 INTRA 1241 PHE ( 35 ) 19 O -- 1243 SER ( 37 ) 19 N 0.143 2.557 INTRA 768 LEU ( 31 ) 12 CD1 -- 772 PHE ( 35 ) 12 CE2 0.143 3.057 INTRA 687 ARG ( 17 ) 11 CZ -- 694 TYR ( 24 ) 11 CE1 0.142 3.058 INTRA 619 HIS ( 16 ) 10 C -- 620 ARG ( 17 ) 10 O 0.142 2.658 INTRA 150 HIS ( 16 ) 3 C -- 151 ARG ( 17 ) 3 O 0.141 2.659 INTRA 1036 LEU ( 31 ) 16 CD1 -- 1037 LYS ( 32 ) 16 N 0.141 2.959 INTRA 838 HIS ( 34 ) 13 C -- 840 ARG ( 36 ) 13 N 0.141 2.759 INTRA 894 ARG ( 23 ) 14 CG -- 895 TYR ( 24 ) 14 N 0.141 2.959 INTRA 671 ASP ( 1 ) 11 CB -- 672 PRO ( 2 ) 11 CD 0.140 3.060 INTRA 1188 VAL ( 49 ) 18 CG1 -- 1189 GLU ( 50 ) 18 N 0.140 2.960 INTRA 924 SER ( 53 ) 14 C -- 925 GLN ( 54 ) 14 O 0.139 2.661 INTRA 88 CYS ( 21 ) 2 O -- 89 ALA ( 22 ) 2 CB 0.139 2.661 INTRA 352 ARG ( 17 ) 6 CG -- 353 CYS ( 18 ) 6 N 0.138 2.962 INTRA 98 LEU ( 31 ) 2 CD1 -- 99 LYS ( 32 ) 2 N 0.138 2.962 INTRA 790 SER ( 53 ) 12 C -- 791 GLN ( 54 ) 12 O 0.138 2.662 INTRA 98 LEU ( 31 ) 2 CD1 -- 102 PHE ( 35 ) 2 CE2 0.137 3.063 INTRA 1289 HIS ( 16 ) 20 C -- 1290 ARG ( 17 ) 20 O 0.137 2.663 INTRA 704 HIS ( 34 ) 11 CD2 -- 705 PHE ( 35 ) 11 N 0.137 2.963 INTRA 226 PHE ( 25 ) 4 CE2 -- 235 HIS ( 34 ) 4 CG 0.137 3.063 INTRA 1227 CYS ( 21 ) 19 O -- 1228 ALA ( 22 ) 19 C 0.137 2.663 INTRA 1083 PRO ( 11 ) 17 CG -- 1096 TYR ( 24 ) 17 CD1 0.136 3.064 INTRA 11 PRO ( 11 ) 1 CD -- 24 TYR ( 24 ) 1 CD1 0.135 3.065 INTRA 1067 GLY ( 62 ) 16 O -- 1068 MET ( 63 ) 16 C 0.135 2.665 INTRA 550 GLY ( 14 ) 9 O -- 552 HIS ( 16 ) 9 N 0.135 2.565 INTRA 165 LEU ( 31 ) 3 CD1 -- 169 PHE ( 35 ) 3 CE2 0.135 3.065 INTRA 1259 SER ( 53 ) 19 C -- 1260 GLN ( 54 ) 19 O 0.135 2.665 INTRA 1241 PHE ( 35 ) 19 O -- 1242 ARG ( 36 ) 19 C 0.134 2.666 INTRA 969 LEU ( 31 ) 15 CD1 -- 973 PHE ( 35 ) 15 CZ 0.134 3.066 INTRA 83 HIS ( 16 ) 2 C -- 84 ARG ( 17 ) 2 O 0.133 2.667 INTRA 892 CYS ( 21 ) 14 O -- 893 ALA ( 22 ) 14 CB 0.133 2.667 INTRA 1222 HIS ( 16 ) 19 C -- 1223 ARG ( 17 ) 19 O 0.132 2.668 INTRA 78 PRO ( 11 ) 2 CD -- 91 TYR ( 24 ) 2 CD1 0.132 3.068 INTRA 1176 SER ( 37 ) 18 C -- 1178 ASP ( 39 ) 18 N 0.132 2.768 INTRA 137 ASN ( 3 ) 3 O -- 138 ALA ( 4 ) 3 C 0.131 2.669 INTRA 1237 LEU ( 31 ) 19 CD2 -- 1241 PHE ( 35 ) 19 CE1 0.131 3.069 INTRA 1170 LEU ( 31 ) 18 CD2 -- 1174 PHE ( 35 ) 18 CE1 0.130 3.070 INTRA 484 LEU ( 15 ) 8 CD1 -- 485 HIS ( 16 ) 8 CG 0.130 3.070 INTRA 234 THR ( 33 ) 4 O -- 237 ARG ( 36 ) 4 CG 0.130 2.670 INTRA 21 CYS ( 21 ) 1 O -- 22 ALA ( 22 ) 1 CB 0.130 2.670 INTRA 590 GLN ( 54 ) 9 O -- 591 GLU ( 55 ) 9 CB 0.130 2.670 INTRA 1013 PRO ( 8 ) 16 O -- 1014 ASP ( 9 ) 16 C 0.130 2.670 INTRA 506 SER ( 37 ) 8 C -- 508 ASP ( 39 ) 8 N 0.129 2.771 INTRA 1056 PRO ( 51 ) 16 O -- 1057 TYR ( 52 ) 16 C 0.129 2.671 INTRA 908 SER ( 37 ) 14 C -- 910 ASP ( 39 ) 14 N 0.129 2.771 INTRA 351 HIS ( 16 ) 6 C -- 352 ARG ( 17 ) 6 O 0.128 2.672 INTRA 686 HIS ( 16 ) 11 C -- 687 ARG ( 17 ) 11 O 0.128 2.672 INTRA 436 HIS ( 34 ) 7 C -- 438 ARG ( 36 ) 7 N 0.128 2.772 INTRA 777 HIS ( 40 ) 12 CG -- 1363 ZIN ( 68 ) 12 ZN1 0.128 3.072 INTRA 492 ARG ( 23 ) 8 CG -- 493 TYR ( 24 ) 8 N 0.128 2.972 INTRA 482 GLY ( 13 ) 8 O -- 484 LEU ( 15 ) 8 N 0.127 2.573 INTRA 1205 TYR ( 66 ) 18 O -- 1206 VAL ( 67 ) 18 C 0.126 2.674 INTRA 354 LEU ( 19 ) 6 C -- 356 CYS ( 21 ) 6 N 0.126 2.774 INTRA 308 HIS ( 40 ) 5 CG -- 1349 ZIN ( 68 ) 5 ZN1 0.126 3.074 INTRA 494 PHE ( 25 ) 8 CE2 -- 503 HIS ( 34 ) 8 CG 0.126 3.074 INTRA 316 SER ( 48 ) 5 O -- 317 VAL ( 49 ) 5 C 0.126 2.674 INTRA 225 TYR ( 24 ) 4 C -- 226 PHE ( 25 ) 4 CD1 0.126 3.074 INTRA 696 ILE ( 26 ) 11 C -- 697 ASP ( 27 ) 11 CG 0.125 3.075 INTRA 104 SER ( 37 ) 2 C -- 106 ASP ( 39 ) 2 N 0.125 2.775 INTRA 904 THR ( 33 ) 14 O -- 907 ARG ( 36 ) 14 CG 0.125 2.675 INTRA 1036 LEU ( 31 ) 16 CD2 -- 1040 PHE ( 35 ) 16 CZ 0.125 3.075 INTRA 598 GLY ( 62 ) 9 O -- 599 MET ( 63 ) 9 C 0.125 2.675 INTRA 439 SER ( 37 ) 7 C -- 441 ASP ( 39 ) 7 N 0.125 2.775 INTRA 552 HIS ( 16 ) 9 C -- 553 ARG ( 17 ) 9 O 0.124 2.676 INTRA 490 CYS ( 21 ) 8 O -- 491 ALA ( 22 ) 8 CB 0.124 2.676 INTRA 756 LEU ( 19 ) 12 C -- 758 CYS ( 21 ) 12 N 0.124 2.776 INTRA 1311 LYS ( 38 ) 20 O -- 1315 LYS ( 42 ) 20 CB 0.124 2.676 INTRA 8 PRO ( 8 ) 1 O -- 9 ASP ( 9 ) 1 C 0.123 2.677 INTRA 587 PRO ( 51 ) 9 C -- 588 TYR ( 52 ) 9 O 0.123 2.677 INTRA 303 PHE ( 35 ) 5 C -- 305 SER ( 37 ) 5 N 0.123 2.777 INTRA 664 ALA ( 61 ) 10 C -- 665 GLY ( 62 ) 10 O 0.123 2.677 INTRA 535 TYR ( 66 ) 8 CG -- 536 VAL ( 67 ) 8 N 0.123 2.977 INTRA 707 SER ( 37 ) 11 C -- 709 ASP ( 39 ) 11 N 0.123 2.777 INTRA 51 PRO ( 51 ) 1 C -- 52 TYR ( 52 ) 1 O 0.123 2.677 INTRA 1165 ILE ( 26 ) 18 O -- 1166 ASP ( 27 ) 18 CG 0.123 2.677 INTRA 504 PHE ( 35 ) 8 C -- 506 SER ( 37 ) 8 N 0.123 2.777 INTRA 619 HIS ( 16 ) 10 CE1 -- 631 SER ( 28 ) 10 CB 0.121 3.079 INTRA 567 LEU ( 31 ) 9 CD2 -- 571 PHE ( 35 ) 9 CE1 0.121 3.079 INTRA 543 ASP ( 7 ) 9 CB -- 546 LEU ( 10 ) 9 CD1 0.121 3.079 INTRA 996 GLU ( 58 ) 15 C -- 997 ARG ( 59 ) 15 O 0.121 2.679 INTRA 168 HIS ( 34 ) 3 C -- 170 ARG ( 36 ) 3 N 0.120 2.780 INTRA 986 SER ( 48 ) 15 O -- 988 GLU ( 50 ) 15 N 0.120 2.430 INTRA HB 1108 ARG ( 36 ) 17 O -- 1109 SER ( 37 ) 17 C 0.119 2.681 INTRA 1127 GLU ( 55 ) 17 O -- 1128 GLU ( 56 ) 17 C 0.119 2.681 INTRA 1320 LEU ( 47 ) 20 C -- 1321 SER ( 48 ) 20 O 0.119 2.681 INTRA 936 SER ( 65 ) 14 C -- 937 TYR ( 66 ) 14 O 0.119 2.681 INTRA 1310 SER ( 37 ) 20 C -- 1312 ASP ( 39 ) 20 N 0.118 2.782 INTRA 1278 GLU ( 5 ) 20 O -- 1279 PHE ( 6 ) 20 C 0.118 2.682 INTRA 654 PRO ( 51 ) 10 O -- 655 TYR ( 52 ) 10 C 0.118 2.682 INTRA 66 TYR ( 66 ) 1 C -- 67 VAL ( 67 ) 1 CG1 0.117 3.083 INTRA 217 HIS ( 16 ) 4 C -- 218 ARG ( 17 ) 4 O 0.117 2.683 INTRA 841 SER ( 37 ) 13 C -- 843 ASP ( 39 ) 13 N 0.117 2.783 INTRA 567 LEU ( 31 ) 9 CD1 -- 568 LYS ( 32 ) 9 N 0.116 2.984 INTRA 1150 PRO ( 11 ) 18 CD -- 1163 TYR ( 24 ) 18 CD1 0.116 3.084 INTRA 1070 SER ( 65 ) 16 C -- 1071 TYR ( 66 ) 16 O 0.116 2.684 INTRA 820 HIS ( 16 ) 13 CE1 -- 832 SER ( 28 ) 13 CB 0.115 3.085 INTRA 1013 PRO ( 8 ) 16 C -- 1015 LEU ( 10 ) 16 N 0.115 2.785 INTRA 835 LEU ( 31 ) 13 CD2 -- 839 PHE ( 35 ) 13 CE1 0.115 3.085 INTRA 333 SER ( 65 ) 5 C -- 334 TYR ( 66 ) 5 O 0.115 2.685 INTRA 185 PRO ( 51 ) 3 C -- 186 TYR ( 52 ) 3 O 0.115 2.685 INTRA 654 PRO ( 51 ) 10 C -- 655 TYR ( 52 ) 10 O 0.115 2.685 INTRA 909 LYS ( 38 ) 14 O -- 913 LYS ( 42 ) 14 CB 0.115 2.685 INTRA 598 GLY ( 62 ) 9 C -- 599 MET ( 63 ) 9 O 0.115 2.685 INTRA 366 LEU ( 31 ) 6 CD1 -- 367 LYS ( 32 ) 6 N 0.114 2.986 INTRA 1326 SER ( 53 ) 20 O -- 1327 GLN ( 54 ) 20 C 0.113 2.687 INTRA 11 PRO ( 11 ) 1 CD -- 24 TYR ( 24 ) 1 CE1 0.113 3.087 INTRA 303 PHE ( 35 ) 5 O -- 305 SER ( 37 ) 5 N 0.113 2.587 INTRA 978 HIS ( 40 ) 15 CG -- 1369 ZIN ( 68 ) 15 ZN1 0.113 3.087 INTRA 969 LEU ( 31 ) 15 CD1 -- 973 PHE ( 35 ) 15 CE2 0.113 3.087 INTRA 238 SER ( 37 ) 4 C -- 240 ASP ( 39 ) 4 N 0.112 2.788 INTRA 308 HIS ( 40 ) 5 CE1 -- 312 LEU ( 44 ) 5 CD1 0.112 3.088 INTRA 437 PHE ( 35 ) 7 O -- 439 SER ( 37 ) 7 N 0.111 2.589 INTRA 31 LEU ( 31 ) 1 CD1 -- 35 PHE ( 35 ) 1 CE2 0.111 3.089 INTRA 460 GLU ( 58 ) 7 O -- 461 ARG ( 59 ) 7 C 0.111 2.689 INTRA And so on for a total of 1069 lines # 86 # Warning: Abnormal packing environment for some residues The residues listed in the table below have an unusual packing environment. The packing environment of the residues is compared with the average packing environment for all residues of the same type in good PDB files. A low packing score can indicate one of several things: Poor packing, misthreading of the sequence through the density, crystal contacts, contacts with a co-factor, or the residue is part of the active site. It is not uncommon to see a few of these, but in any case this requires further inspection of the residue. 1272 TYR ( 66 ) 19 -9.02 133 TYR ( 66 ) 2 -8.89 736 TYR ( 66 ) 11 -8.86 521 TYR ( 52 ) 8 -8.85 789 TYR ( 52 ) 12 -8.84 1004 TYR ( 66 ) 15 -8.81 66 TYR ( 66 ) 1 -8.73 803 TYR ( 66 ) 12 -8.69 588 TYR ( 52 ) 9 -8.67 602 TYR ( 66 ) 9 -8.66 923 TYR ( 52 ) 14 -8.61 1325 TYR ( 52 ) 20 -8.54 186 TYR ( 52 ) 3 -8.52 669 TYR ( 66 ) 10 -8.50 722 TYR ( 52 ) 11 -8.40 200 TYR ( 66 ) 3 -8.40 401 TYR ( 66 ) 6 -8.37 1339 TYR ( 66 ) 20 -8.37 870 TYR ( 66 ) 13 -8.36 468 TYR ( 66 ) 7 -8.22 1131 ARG ( 59 ) 17 -8.21 1138 TYR ( 66 ) 17 -8.20 535 TYR ( 66 ) 8 -8.15 856 TYR ( 52 ) 13 -8.13 465 MET ( 63 ) 7 -8.11 1205 TYR ( 66 ) 18 -8.09 267 TYR ( 66 ) 4 -8.09 334 TYR ( 66 ) 5 -8.08 867 MET ( 63 ) 13 -8.05 733 MET ( 63 ) 11 -8.05 937 TYR ( 66 ) 14 -8.05 1071 TYR ( 66 ) 16 -8.04 1336 MET ( 63 ) 20 -8.04 63 MET ( 63 ) 1 -8.03 662 ARG ( 59 ) 10 -8.02 595 ARG ( 59 ) 9 -8.02 260 ARG ( 59 ) 4 -7.93 264 MET ( 63 ) 4 -7.92 532 MET ( 63 ) 8 -7.91 1135 MET ( 63 ) 17 -7.88 1191 TYR ( 52 ) 18 -7.87 1265 ARG ( 59 ) 19 -7.84 997 ARG ( 59 ) 15 -7.80 1258 TYR ( 52 ) 19 -7.80 126 ARG ( 59 ) 2 -7.77 1269 MET ( 63 ) 19 -7.76 197 MET ( 63 ) 3 -7.69 800 MET ( 63 ) 12 -7.66 52 TYR ( 52 ) 1 -7.63 461 ARG ( 59 ) 7 -7.62 1068 MET ( 63 ) 16 -7.61 930 ARG ( 59 ) 14 -7.61 934 MET ( 63 ) 14 -7.61 130 MET ( 63 ) 2 -7.60 1202 MET ( 63 ) 18 -7.56 387 TYR ( 52 ) 6 -7.56 599 MET ( 63 ) 9 -7.43 331 MET ( 63 ) 5 -7.41 398 MET ( 63 ) 6 -7.29 560 TYR ( 24 ) 9 -7.27 1198 ARG ( 59 ) 18 -7.27 895 TYR ( 24 ) 14 -7.15 1163 TYR ( 24 ) 18 -7.14 1064 ARG ( 59 ) 16 -7.13 666 MET ( 63 ) 10 -7.09 292 TYR ( 24 ) 5 -7.07 6 PHE ( 6 ) 1 -7.06 1332 ARG ( 59 ) 20 -6.99 796 ARG ( 59 ) 12 -6.95 729 ARG ( 59 ) 11 -6.91 59 ARG ( 59 ) 1 -6.88 990 TYR ( 52 ) 15 -6.87 694 TYR ( 24 ) 11 -6.84 359 TYR ( 24 ) 6 -6.73 761 TYR ( 24 ) 12 -6.70 1078 PHE ( 6 ) 17 -6.63 1096 TYR ( 24 ) 17 -6.60 394 ARG ( 59 ) 6 -6.58 158 TYR ( 24 ) 3 -6.58 426 TYR ( 24 ) 7 -6.55 327 ARG ( 59 ) 5 -6.53 73 PHE ( 6 ) 2 -6.52 828 TYR ( 24 ) 13 -6.43 944 PHE ( 6 ) 15 -6.38 274 PHE ( 6 ) 5 -6.35 493 TYR ( 24 ) 8 -6.34 341 PHE ( 6 ) 6 -6.33 609 PHE ( 6 ) 10 -6.27 417 LEU ( 15 ) 7 -6.20 618 LEU ( 15 ) 10 -6.19 1124 TYR ( 52 ) 17 -6.17 1221 LEU ( 15 ) 19 -6.16 962 TYR ( 24 ) 15 -6.15 627 TYR ( 24 ) 10 -6.13 1230 TYR ( 24 ) 19 -6.12 743 PHE ( 6 ) 12 -6.11 225 TYR ( 24 ) 4 -6.04 1279 PHE ( 6 ) 20 -6.02 475 PHE ( 6 ) 8 -5.98 91 TYR ( 24 ) 2 -5.96 1011 PHE ( 6 ) 16 -5.91 24 TYR ( 24 ) 1 -5.91 925 GLN ( 54 ) 14 -5.88 676 PHE ( 6 ) 11 -5.85 791 GLN ( 54 ) 12 -5.84 685 LEU ( 15 ) 11 -5.84 1029 TYR ( 24 ) 16 -5.83 747 LEU ( 10 ) 12 -5.83 810 PHE ( 6 ) 13 -5.82 661 GLU ( 58 ) 10 -5.80 1297 TYR ( 24 ) 20 -5.79 58 GLU ( 58 ) 1 -5.78 278 LEU ( 10 ) 5 -5.77 140 PHE ( 6 ) 3 -5.77 193 ARG ( 59 ) 3 -5.77 1288 LEU ( 15 ) 20 -5.77 590 GLN ( 54 ) 9 -5.74 408 PHE ( 6 ) 7 -5.74 1145 PHE ( 6 ) 18 -5.71 149 LEU ( 15 ) 3 -5.70 819 LEU ( 15 ) 13 -5.68 881 LEU ( 10 ) 14 -5.67 1082 LEU ( 10 ) 17 -5.66 484 LEU ( 15 ) 8 -5.65 54 GLN ( 54 ) 1 -5.64 655 TYR ( 52 ) 10 -5.63 877 PHE ( 6 ) 14 -5.63 863 ARG ( 59 ) 13 -5.63 1193 GLN ( 54 ) 18 -5.57 428 ILE ( 26 ) 7 -5.55 188 GLN ( 54 ) 3 -5.52 1212 PHE ( 6 ) 19 -5.51 882 PRO ( 11 ) 14 -5.51 279 PRO ( 11 ) 5 -5.51 1083 PRO ( 11 ) 17 -5.50 948 LEU ( 10 ) 15 -5.50 1149 LEU ( 10 ) 18 -5.50 78 PRO ( 11 ) 2 -5.50 207 PHE ( 6 ) 4 -5.50 346 PRO ( 11 ) 6 -5.50 413 PRO ( 11 ) 7 -5.49 814 LEU ( 10 ) 13 -5.48 657 GLN ( 54 ) 10 -5.48 1098 ILE ( 26 ) 17 -5.48 212 PRO ( 11 ) 4 -5.48 1216 LEU ( 10 ) 19 -5.47 815 PRO ( 11 ) 13 -5.47 350 LEU ( 15 ) 6 -5.46 546 LEU ( 10 ) 9 -5.46 996 GLU ( 58 ) 15 -5.46 1217 PRO ( 11 ) 19 -5.46 1284 PRO ( 11 ) 20 -5.45 1075 ASN ( 3 ) 17 -5.45 326 GLU ( 58 ) 5 -5.45 1299 ILE ( 26 ) 20 -5.44 1015 LEU ( 10 ) 16 -5.43 518 VAL ( 49 ) 8 -5.42 1283 LEU ( 10 ) 20 -5.42 451 VAL ( 49 ) 7 -5.42 696 ILE ( 26 ) 11 -5.42 719 VAL ( 49 ) 11 -5.41 361 ILE ( 26 ) 6 -5.41 82 LEU ( 15 ) 2 -5.41 77 LEU ( 10 ) 2 -5.40 405 ASN ( 3 ) 7 -5.40 1057 TYR ( 52 ) 16 -5.40 160 ILE ( 26 ) 3 -5.39 858 GLN ( 54 ) 13 -5.38 673 ASN ( 3 ) 11 -5.38 949 PRO ( 11 ) 15 -5.38 211 LEU ( 10 ) 4 -5.37 144 LEU ( 10 ) 3 -5.36 613 LEU ( 10 ) 10 -5.35 338 ASN ( 3 ) 6 -5.34 523 GLN ( 54 ) 8 -5.34 1232 ILE ( 26 ) 19 -5.34 1322 VAL ( 49 ) 20 -5.33 652 VAL ( 49 ) 10 -5.33 763 ILE ( 26 ) 12 -5.33 551 LEU ( 15 ) 9 -5.32 629 ILE ( 26 ) 10 -5.32 253 TYR ( 52 ) 4 -5.32 562 ILE ( 26 ) 9 -5.31 964 ILE ( 26 ) 15 -5.30 412 LEU ( 10 ) 7 -5.30 680 LEU ( 10 ) 11 -5.29 250 VAL ( 49 ) 4 -5.28 830 ILE ( 26 ) 13 -5.28 495 ILE ( 26 ) 8 -5.28 183 VAL ( 49 ) 3 -5.26 1197 GLU ( 58 ) 18 -5.25 724 GLN ( 54 ) 11 -5.25 795 GLU ( 58 ) 12 -5.24 479 LEU ( 10 ) 8 -5.24 345 LEU ( 10 ) 6 -5.24 10 LEU ( 10 ) 1 -5.23 227 ILE ( 26 ) 4 -5.23 1031 ILE ( 26 ) 16 -5.22 1008 ASN ( 3 ) 16 -5.21 1329 GLU ( 56 ) 20 -5.20 1165 ILE ( 26 ) 18 -5.20 216 LEU ( 15 ) 4 -5.18 897 ILE ( 26 ) 14 -5.17 322 GLN ( 54 ) 5 -5.17 874 ASN ( 3 ) 14 -5.17 190 GLU ( 56 ) 3 -5.16 820 HIS ( 16 ) 13 -5.16 26 ILE ( 26 ) 1 -5.15 1154 LEU ( 15 ) 18 -5.14 389 GLN ( 54 ) 6 -5.13 926 GLU ( 55 ) 14 -5.13 1020 LEU ( 15 ) 16 -5.09 591 GLU ( 55 ) 9 -5.08 792 GLU ( 55 ) 12 -5.07 15 LEU ( 15 ) 1 -5.06 992 GLN ( 54 ) 15 -5.06 658 GLU ( 55 ) 10 -5.01 384 VAL ( 49 ) 6 -5.01 1188 VAL ( 49 ) 18 -5.00 116 VAL ( 49 ) 2 -5.00 # 87 # Warning: Abnormal packing environment for sequential residues A stretch of at least three sequential residues with a questionable packing environment was found. This could indicate that these residues are part of a strange loop, but might also be an indication of misthreading. The table below lists the first and last residue in each stretch found, as well as the average residue score of the series. 58 GLU ( 58 ) 1 --- 60 ALA ( 60 ) 1 -5.62 62 GLY ( 62 ) 1 --- 66 TYR ( 66 ) 1 -6.01 76 ASP ( 9 ) 2 --- 80 GLY ( 13 ) 2 -4.70 129 GLY ( 62 ) 2 --- 131 GLY ( 64 ) 2 -5.48 192 GLU ( 58 ) 3 --- 194 ALA ( 60 ) 3 -4.91 196 GLY ( 62 ) 3 --- 200 TYR ( 66 ) 3 -5.94 210 ASP ( 9 ) 4 --- 214 GLY ( 13 ) 4 -4.65 259 GLU ( 58 ) 4 --- 267 TYR ( 66 ) 4 -5.61 277 ASP ( 9 ) 5 --- 280 GLY ( 12 ) 5 -4.89 326 GLU ( 58 ) 5 --- 328 ALA ( 60 ) 5 -5.42 330 GLY ( 62 ) 5 --- 334 TYR ( 66 ) 5 -5.68 344 ASP ( 9 ) 6 --- 348 GLY ( 13 ) 6 -4.62 393 GLU ( 58 ) 6 --- 395 ALA ( 60 ) 6 -5.08 397 GLY ( 62 ) 6 --- 401 TYR ( 66 ) 6 -5.77 411 ASP ( 9 ) 7 --- 414 GLY ( 12 ) 7 -4.79 463 ALA ( 61 ) 7 --- 468 TYR ( 66 ) 7 -5.64 598 GLY ( 62 ) 9 --- 600 GLY ( 64 ) 9 -5.31 657 GLN ( 54 ) 10 --- 659 GLU ( 56 ) 10 -5.05 661 GLU ( 58 ) 10 --- 663 ALA ( 60 ) 10 -6.02 732 GLY ( 62 ) 11 --- 734 GLY ( 64 ) 11 -5.52 789 TYR ( 52 ) 12 --- 792 GLU ( 55 ) 12 -6.06 799 GLY ( 62 ) 12 --- 803 TYR ( 66 ) 12 -5.83 813 ASP ( 9 ) 13 --- 817 GLY ( 13 ) 13 -4.70 862 GLU ( 58 ) 13 --- 864 ALA ( 60 ) 13 -4.87 866 GLY ( 62 ) 13 --- 870 TYR ( 66 ) 13 -6.00 880 ASP ( 9 ) 14 --- 883 GLY ( 12 ) 14 -4.87 933 GLY ( 62 ) 14 --- 937 TYR ( 66 ) 14 -5.76 947 ASP ( 9 ) 15 --- 951 GLY ( 13 ) 15 -4.68 996 GLU ( 58 ) 15 --- 998 ALA ( 60 ) 15 -5.87 1067 GLY ( 62 ) 16 --- 1071 TYR ( 66 ) 16 -5.82 1081 ASP ( 9 ) 17 --- 1085 GLY ( 13 ) 17 -4.73 1130 GLU ( 58 ) 17 --- 1132 ALA ( 60 ) 17 -5.59 1134 GLY ( 62 ) 17 --- 1138 TYR ( 66 ) 17 -5.85 1197 GLU ( 58 ) 18 --- 1199 ALA ( 60 ) 18 -5.61 1201 GLY ( 62 ) 18 --- 1205 TYR ( 66 ) 18 -5.82 1215 ASP ( 9 ) 19 --- 1219 GLY ( 13 ) 19 -4.67 1258 TYR ( 52 ) 19 --- 1261 GLU ( 55 ) 19 -5.34 1265 ARG ( 59 ) 19 --- 1269 MET ( 63 ) 19 -5.67 1282 ASP ( 9 ) 20 --- 1286 GLY ( 13 ) 20 -4.68 1331 GLU ( 58 ) 20 --- 1333 ALA ( 60 ) 20 -5.05 1335 GLY ( 62 ) 20 --- 1339 TYR ( 66 ) 20 -5.97 # 88 # Error: Abnormal average packing environment The average quality control value for the structure is very low. A molecule is certain to be incorrect if the average quality score is below -3.0. Poorly refined molecules, very well energy minimized misthreaded molecules and low homology models give values between -2.0 and -3.0. The average quality of 200 highly refined Xray structures was -0.5+/-0.4 [REF]. Average for range 1 -1340 : -2.721 # 89 # Note: Quality value plot The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 1 # 90 # Note: Quality value plot The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 2 # 91 # Note: Quality value plot The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 3 # 92 # Note: Quality value plot The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 4 # 93 # Note: Quality value plot The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 5 # 94 # Note: Quality value plot The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 6 # 95 # Note: Quality value plot The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 7 # 96 # Note: Quality value plot The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 8 # 97 # Note: Quality value plot The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 9 # 98 # Note: Quality value plot The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 10 # 99 # Note: Quality value plot The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 11 # 100 # Note: Quality value plot The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 12 # 101 # Note: Quality value plot The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 13 # 102 # Note: Quality value plot The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 14 # 103 # Note: Quality value plot The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 15 # 104 # Note: Quality value plot The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 16 # 105 # Note: Quality value plot The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 17 # 106 # Note: Quality value plot The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 18 # 107 # Note: Quality value plot The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 19 # 108 # Note: Quality value plot The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 20 # 109 # Warning: Low packing Z-score for some residues The residues listed in the table below have an unusual packing environment according to the 2nd generation quality check. The score listed in the table is a packing normality Z-score: positive means better than average, negative means worse than average. Only residues scoring less than -2.50 are listed here. These are the "unusual" residues in the structure, so it will be interesting to take a special look at them. 63 MET ( 63 ) 1 -3.05 130 MET ( 63 ) 2 -3.05 197 MET ( 63 ) 3 -3.05 264 MET ( 63 ) 4 -3.05 331 MET ( 63 ) 5 -3.05 398 MET ( 63 ) 6 -3.05 465 MET ( 63 ) 7 -3.05 599 MET ( 63 ) 9 -3.05 666 MET ( 63 ) 10 -3.05 733 MET ( 63 ) 11 -3.05 800 MET ( 63 ) 12 -3.05 867 MET ( 63 ) 13 -3.05 934 MET ( 63 ) 14 -3.05 1001 MET ( 63 ) 15 -3.05 1068 MET ( 63 ) 16 -3.05 1135 MET ( 63 ) 17 -3.05 1202 MET ( 63 ) 18 -3.05 1269 MET ( 63 ) 19 -3.05 1336 MET ( 63 ) 20 -3.05 532 MET ( 63 ) 8 -3.00 870 TYR ( 66 ) 13 -2.95 133 TYR ( 66 ) 2 -2.95 1004 TYR ( 66 ) 15 -2.95 401 TYR ( 66 ) 6 -2.95 602 TYR ( 66 ) 9 -2.95 736 TYR ( 66 ) 11 -2.95 66 TYR ( 66 ) 1 -2.95 1272 TYR ( 66 ) 19 -2.95 1205 TYR ( 66 ) 18 -2.95 669 TYR ( 66 ) 10 -2.95 803 TYR ( 66 ) 12 -2.95 200 TYR ( 66 ) 3 -2.95 1339 TYR ( 66 ) 20 -2.95 1138 TYR ( 66 ) 17 -2.94 468 TYR ( 66 ) 7 -2.94 267 TYR ( 66 ) 4 -2.94 937 TYR ( 66 ) 14 -2.94 1071 TYR ( 66 ) 16 -2.94 334 TYR ( 66 ) 5 -2.94 1258 TYR ( 52 ) 19 -2.93 521 TYR ( 52 ) 8 -2.91 52 TYR ( 52 ) 1 -2.91 1328 GLU ( 55 ) 20 -2.87 1325 TYR ( 52 ) 20 -2.83 186 TYR ( 52 ) 3 -2.82 535 TYR ( 66 ) 8 -2.82 138 ALA ( 4 ) 3 -2.80 318 GLU ( 50 ) 5 -2.76 827 ARG ( 23 ) 13 -2.76 693 ARG ( 23 ) 11 -2.75 1095 ARG ( 23 ) 17 -2.74 856 TYR ( 52 ) 13 -2.71 588 TYR ( 52 ) 9 -2.71 789 TYR ( 52 ) 12 -2.71 760 ARG ( 23 ) 12 -2.70 1229 ARG ( 23 ) 19 -2.67 291 ARG ( 23 ) 5 -2.66 425 ARG ( 23 ) 7 -2.64 1256 GLU ( 50 ) 19 -2.64 1162 ARG ( 23 ) 18 -2.64 942 ALA ( 4 ) 15 -2.63 358 ARG ( 23 ) 6 -2.63 387 TYR ( 52 ) 6 -2.62 1191 TYR ( 52 ) 18 -2.60 1323 GLU ( 50 ) 20 -2.56 923 TYR ( 52 ) 14 -2.55 250 VAL ( 49 ) 4 -2.52 518 VAL ( 49 ) 8 -2.51 # 110 # Warning: Abnormal packing Z-score for sequential residues A stretch of at least four sequential residues with a 2nd generation packing Z-score below -1.75 was found. This could indicate that these residues are part of a strange loop or that the residues in this range are incomplete, but it might also be an indication of misthreading. The table below lists the first and last residue in each stretch found, as well as the average residue Z-score of the series. 58 GLU ( 58 ) 1 --- 61 ALA ( 61 ) 1 -1.90 125 GLU ( 58 ) 2 --- 128 ALA ( 61 ) 2 -1.77 192 GLU ( 58 ) 3 --- 195 ALA ( 61 ) 3 -1.90 259 GLU ( 58 ) 4 --- 262 ALA ( 61 ) 4 -2.02 326 GLU ( 58 ) 5 --- 329 ALA ( 61 ) 5 -1.91 330 GLY ( 62 ) 5 --- 335 VAL ( 67 ) 5 -2.25 393 GLU ( 58 ) 6 --- 396 ALA ( 61 ) 6 -2.12 527 GLU ( 58 ) 8 --- 530 ALA ( 61 ) 8 -1.91 591 GLU ( 55 ) 9 --- 594 GLU ( 58 ) 9 -1.59 661 GLU ( 58 ) 10 --- 666 MET ( 63 ) 10 -2.08 728 GLU ( 58 ) 11 --- 731 ALA ( 61 ) 11 -1.75 795 GLU ( 58 ) 12 --- 798 ALA ( 61 ) 12 -1.85 862 GLU ( 58 ) 13 --- 865 ALA ( 61 ) 13 -1.94 927 GLU ( 56 ) 14 --- 932 ALA ( 61 ) 14 -1.94 935 GLY ( 64 ) 14 --- 938 VAL ( 67 ) 14 -2.16 996 GLU ( 58 ) 15 --- 999 ALA ( 61 ) 15 -2.02 1002 GLY ( 64 ) 15 --- 1005 VAL ( 67 ) 15 -2.08 1062 ALA ( 57 ) 16 --- 1066 ALA ( 61 ) 16 -1.87 1130 GLU ( 58 ) 17 --- 1133 ALA ( 61 ) 17 -1.90 1262 GLU ( 56 ) 19 --- 1269 MET ( 63 ) 19 -2.04 1330 ALA ( 57 ) 20 --- 1334 ALA ( 61 ) 20 -1.95 # 111 # Error: Abnormal structural average packing Z-score The quality control Z-score for the structure is very low. A molecule is certain to be incorrect if the Z-score is below -5.0. Poorly refined molecules, very well energy minimized misthreaded molecules and low homology models give values between -2.0 and -5.0. The average quality of properly refined Xray structures is 0.0+/-1.0. All contacts : Average = -0.890 Z-score = -5.88 BB-BB contacts : Average = -0.114 Z-score = -0.87 BB-SC contacts : Average = -0.953 Z-score = -6.28 SC-BB contacts : Average = -0.399 Z-score = -2.50 SC-SC contacts : Average = -1.005 Z-score = -5.96 # 112 # Note: Per-model averages for NQA The table below gives the per-model NQA averages and Z-scores. These are the numbers for all contacts. Model 1 : -0.820; -5.423 Model 2 : -0.791; -5.235 Model 3 : -0.909; -6.006 Model 4 : -0.842; -5.566 Model 5 : -0.879; -5.812 Model 6 : -0.983; -6.492 Model 7 : -0.895; -5.918 Model 8 : -1.019; -6.732 Model 9 : -0.874; -5.777 Model 10 : -0.828; -5.474 Model 11 : -0.971; -6.414 Model 12 : -0.928; -6.130 Model 13 : -0.807; -5.336 Model 14 : -0.817; -5.402 Model 15 : -0.857; -5.664 Model 16 : -0.915; -6.048 Model 17 : -0.822; -5.434 Model 18 : -0.864; -5.709 Model 19 : -0.951; -6.280 Model 20 : -1.027; -6.781 # 113 # Note: Second generation quality Z-score plot The second generation quality Z-score smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -1.3) indicate "unusual" packing. In the TeX file, a plot has been inserted here Model number 1 # 114 # Note: Second generation quality Z-score plot In the TeX file, a plot has been inserted here Model number 2 # 115 # Note: Second generation quality Z-score plot In the TeX file, a plot has been inserted here Model number 3 # 116 # Note: Second generation quality Z-score plot In the TeX file, a plot has been inserted here Model number 4 # 117 # Note: Second generation quality Z-score plot In the TeX file, a plot has been inserted here Model number 5 # 118 # Note: Second generation quality Z-score plot In the TeX file, a plot has been inserted here Model number 6 # 119 # Note: Second generation quality Z-score plot In the TeX file, a plot has been inserted here Model number 7 # 120 # Note: Second generation quality Z-score plot In the TeX file, a plot has been inserted here Model number 8 # 121 # Note: Second generation quality Z-score plot In the TeX file, a plot has been inserted here Model number 9 # 122 # Note: Second generation quality Z-score plot In the TeX file, a plot has been inserted here Model number 10 # 123 # Note: Second generation quality Z-score plot In the TeX file, a plot has been inserted here Model number 11 # 124 # Note: Second generation quality Z-score plot In the TeX file, a plot has been inserted here Model number 12 # 125 # Note: Second generation quality Z-score plot In the TeX file, a plot has been inserted here Model number 13 # 126 # Note: Second generation quality Z-score plot In the TeX file, a plot has been inserted here Model number 14 # 127 # Note: Second generation quality Z-score plot In the TeX file, a plot has been inserted here Model number 15 # 128 # Note: Second generation quality Z-score plot In the TeX file, a plot has been inserted here Model number 16 # 129 # Note: Second generation quality Z-score plot In the TeX file, a plot has been inserted here Model number 17 # 130 # Note: Second generation quality Z-score plot In the TeX file, a plot has been inserted here Model number 18 # 131 # Note: Second generation quality Z-score plot In the TeX file, a plot has been inserted here Model number 19 # 132 # Note: Second generation quality Z-score plot In the TeX file, a plot has been inserted here Model number 20 # 133 # Warning: Backbone oxygen evaluation The residues listed in the table below have an unusual backbone oxygen position. For each of the residues in the structure, a search was performed to find 5-residue stretches in the WHAT IF database with superposable C-alpha coordinates, and some constraints on the neighboring backbone oxygens. In the following table the RMS distance between the backbone oxygen positions of these matching structures in the database and the position of the backbone oxygen atom in the current residue is given. If this number is larger than 1.5 a significant number of structures in the database show an alternative position for the backbone oxygen. If the number is larger than 2.0 most matching backbone fragments in the database have the peptide plane flipped. A manual check needs to be performed to assess whether the experimental data can support that alternative as well. The number in the last column is the number of database hits (maximum 80) used in the calculation. It is "normal" that some glycine residues show up in this list, but they are still worth checking! 466 GLY ( 64 ) 7 3.06 22 868 GLY ( 64 ) 13 2.97 15 866 GLY ( 62 ) 13 2.29 19 1069 GLY ( 64 ) 16 2.10 18 265 GLY ( 64 ) 4 1.75 33 1203 GLY ( 64 ) 18 1.67 23 64 GLY ( 64 ) 1 1.67 18 667 GLY ( 64 ) 10 1.64 61 198 GLY ( 64 ) 3 1.64 38 464 GLY ( 62 ) 7 1.62 49 1000 GLY ( 62 ) 15 1.54 10 # 134 # Warning: Unusual rotamers The residues listed in the table below have a rotamer that is not seen very often in the database of solved protein structures. This option determines for every residue the position specific chi-1 rotamer distribution. Thereafter it verified whether the actual residue in the molecule has the most preferred rotamer or not. If the actual rotamer is the preferred one, the score is 1.0. If the actual rotamer is unique, the score is 0.0. If there are two preferred rotamers, with a population distribution of 3:2 and your rotamer sits in the lesser populated rotamer, the score will be 0.667. No value will be given if insufficient hits are found in the database. It is not necessarily an error if a few residues have rotamer values below 0.3, but careful inspection of all residues with these low values could be worth it. 1106 HIS ( 34 ) 17 0.34 1003 SER ( 65 ) 15 0.36 235 HIS ( 34 ) 4 0.37 1173 HIS ( 34 ) 18 0.37 1043 LYS ( 38 ) 16 0.38 168 HIS ( 34 ) 3 0.38 704 HIS ( 34 ) 11 0.38 1307 HIS ( 34 ) 20 0.38 1311 LYS ( 38 ) 20 0.38 584 SER ( 48 ) 9 0.39 63 MET ( 63 ) 1 0.39 440 LYS ( 38 ) 7 0.39 # 135 # Warning: Unusual backbone conformations For the residues listed in the table below, the backbone formed by itself and two neighboring residues on either side is in a conformation that is not seen very often in the database of solved protein structures. The number given in the table is the number of similar backbone conformations in the database with the same amino acid in the center. For this check, backbone conformations are compared with database structures using C-alpha superpositions with some restraints on the backbone oxygen positions. A residue mentioned in the table can be part of a strange loop, or there might be something wrong with it or its directly surrounding residues. There are a few of these in every protein, but in any case it is worth looking at! 4 ALA ( 4 ) 1 0 36 ARG ( 36 ) 1 0 50 GLU ( 50 ) 1 0 54 GLN ( 54 ) 1 0 58 GLU ( 58 ) 1 0 59 ARG ( 59 ) 1 0 70 ASN ( 3 ) 2 0 71 ALA ( 4 ) 2 0 72 GLU ( 5 ) 2 0 83 HIS ( 16 ) 2 0 84 ARG ( 17 ) 2 0 85 CYS ( 18 ) 2 0 88 CYS ( 21 ) 2 0 120 SER ( 53 ) 2 0 121 GLN ( 54 ) 2 0 122 GLU ( 55 ) 2 0 123 GLU ( 56 ) 2 0 128 ALA ( 61 ) 2 0 137 ASN ( 3 ) 3 0 138 ALA ( 4 ) 3 0 150 HIS ( 16 ) 3 0 151 ARG ( 17 ) 3 0 152 CYS ( 18 ) 3 0 155 CYS ( 21 ) 3 0 182 SER ( 48 ) 3 0 186 TYR ( 52 ) 3 0 188 GLN ( 54 ) 3 0 190 GLU ( 56 ) 3 0 191 ALA ( 57 ) 3 0 192 GLU ( 58 ) 3 0 194 ALA ( 60 ) 3 0 197 MET ( 63 ) 3 0 205 ALA ( 4 ) 4 0 217 HIS ( 16 ) 4 0 218 ARG ( 17 ) 4 0 219 CYS ( 18 ) 4 0 222 CYS ( 21 ) 4 0 255 GLN ( 54 ) 4 0 256 GLU ( 55 ) 4 0 257 GLU ( 56 ) 4 0 261 ALA ( 60 ) 4 0 262 ALA ( 61 ) 4 0 271 ASN ( 3 ) 5 0 272 ALA ( 4 ) 5 0 304 ARG ( 36 ) 5 0 318 GLU ( 50 ) 5 0 323 GLU ( 55 ) 5 0 324 GLU ( 56 ) 5 0 325 ALA ( 57 ) 5 0 326 GLU ( 58 ) 5 0 328 ALA ( 60 ) 5 0 331 MET ( 63 ) 5 0 333 SER ( 65 ) 5 0 351 HIS ( 16 ) 6 0 352 ARG ( 17 ) 6 0 353 CYS ( 18 ) 6 0 356 CYS ( 21 ) 6 0 361 ILE ( 26 ) 6 0 371 ARG ( 36 ) 6 0 383 SER ( 48 ) 6 0 384 VAL ( 49 ) 6 0 385 GLU ( 50 ) 6 0 389 GLN ( 54 ) 6 0 390 GLU ( 55 ) 6 0 393 GLU ( 58 ) 6 0 394 ARG ( 59 ) 6 0 396 ALA ( 61 ) 6 0 398 MET ( 63 ) 6 0 400 SER ( 65 ) 6 0 406 ALA ( 4 ) 7 0 414 GLY ( 12 ) 7 0 418 HIS ( 16 ) 7 0 419 ARG ( 17 ) 7 0 420 CYS ( 18 ) 7 0 451 VAL ( 49 ) 7 0 455 SER ( 53 ) 7 0 456 GLN ( 54 ) 7 0 457 GLU ( 55 ) 7 0 458 GLU ( 56 ) 7 0 460 GLU ( 58 ) 7 0 461 ARG ( 59 ) 7 0 462 ALA ( 60 ) 7 0 463 ALA ( 61 ) 7 0 467 SER ( 65 ) 7 0 472 ASN ( 3 ) 8 0 474 GLU ( 5 ) 8 0 490 CYS ( 21 ) 8 0 517 SER ( 48 ) 8 0 519 GLU ( 50 ) 8 0 523 GLN ( 54 ) 8 0 527 GLU ( 58 ) 8 0 529 ALA ( 60 ) 8 0 530 ALA ( 61 ) 8 0 532 MET ( 63 ) 8 0 534 SER ( 65 ) 8 0 539 ASN ( 3 ) 9 0 541 GLU ( 5 ) 9 0 552 HIS ( 16 ) 9 0 553 ARG ( 17 ) 9 0 554 CYS ( 18 ) 9 0 588 TYR ( 52 ) 9 0 590 GLN ( 54 ) 9 0 591 GLU ( 55 ) 9 0 592 GLU ( 56 ) 9 0 593 ALA ( 57 ) 9 0 594 GLU ( 58 ) 9 0 599 MET ( 63 ) 9 0 606 ASN ( 3 ) 10 0 619 HIS ( 16 ) 10 0 620 ARG ( 17 ) 10 0 624 CYS ( 21 ) 10 0 625 ALA ( 22 ) 10 0 652 VAL ( 49 ) 10 0 653 GLU ( 50 ) 10 0 654 PRO ( 51 ) 10 0 655 TYR ( 52 ) 10 0 656 SER ( 53 ) 10 0 657 GLN ( 54 ) 10 0 658 GLU ( 55 ) 10 0 659 GLU ( 56 ) 10 0 661 GLU ( 58 ) 10 0 662 ARG ( 59 ) 10 0 663 ALA ( 60 ) 10 0 664 ALA ( 61 ) 10 0 666 MET ( 63 ) 10 0 686 HIS ( 16 ) 11 0 687 ARG ( 17 ) 11 0 719 VAL ( 49 ) 11 0 722 TYR ( 52 ) 11 0 724 GLN ( 54 ) 11 0 725 GLU ( 55 ) 11 0 726 GLU ( 56 ) 11 0 731 ALA ( 61 ) 11 0 733 MET ( 63 ) 11 0 740 ASN ( 3 ) 12 0 741 ALA ( 4 ) 12 0 758 CYS ( 21 ) 12 0 791 GLN ( 54 ) 12 0 792 GLU ( 55 ) 12 0 793 GLU ( 56 ) 12 0 795 GLU ( 58 ) 12 0 796 ARG ( 59 ) 12 0 798 ALA ( 61 ) 12 0 802 SER ( 65 ) 12 0 817 GLY ( 13 ) 13 0 820 HIS ( 16 ) 13 0 821 ARG ( 17 ) 13 0 853 VAL ( 49 ) 13 0 854 GLU ( 50 ) 13 0 862 GLU ( 58 ) 13 0 863 ARG ( 59 ) 13 0 865 ALA ( 61 ) 13 0 869 SER ( 65 ) 13 0 875 ALA ( 4 ) 14 0 876 GLU ( 5 ) 14 0 893 ALA ( 22 ) 14 0 925 GLN ( 54 ) 14 0 926 GLU ( 55 ) 14 0 927 GLU ( 56 ) 14 0 928 ALA ( 57 ) 14 0 930 ARG ( 59 ) 14 0 931 ALA ( 60 ) 14 0 934 MET ( 63 ) 14 0 936 SER ( 65 ) 14 0 941 ASN ( 3 ) 15 0 942 ALA ( 4 ) 15 0 959 CYS ( 21 ) 15 0 986 SER ( 48 ) 15 0 987 VAL ( 49 ) 15 0 989 PRO ( 51 ) 15 0 990 TYR ( 52 ) 15 0 991 SER ( 53 ) 15 0 992 GLN ( 54 ) 15 0 994 GLU ( 56 ) 15 0 995 ALA ( 57 ) 15 0 996 GLU ( 58 ) 15 0 997 ARG ( 59 ) 15 0 998 ALA ( 60 ) 15 0 1021 HIS ( 16 ) 16 0 1022 ARG ( 17 ) 16 0 1023 CYS ( 18 ) 16 0 1026 CYS ( 21 ) 16 0 1031 ILE ( 26 ) 16 0 1055 GLU ( 50 ) 16 0 1056 PRO ( 51 ) 16 0 1057 TYR ( 52 ) 16 0 1058 SER ( 53 ) 16 0 1059 GLN ( 54 ) 16 0 1060 GLU ( 55 ) 16 0 1061 GLU ( 56 ) 16 0 1062 ALA ( 57 ) 16 0 1065 ALA ( 60 ) 16 0 1066 ALA ( 61 ) 16 0 1068 MET ( 63 ) 16 0 1070 SER ( 65 ) 16 0 1076 ALA ( 4 ) 17 0 1077 GLU ( 5 ) 17 0 1121 VAL ( 49 ) 17 0 1122 GLU ( 50 ) 17 0 1123 PRO ( 51 ) 17 0 1124 TYR ( 52 ) 17 0 1125 SER ( 53 ) 17 0 1126 GLN ( 54 ) 17 0 1127 GLU ( 55 ) 17 0 1128 GLU ( 56 ) 17 0 1131 ARG ( 59 ) 17 0 1132 ALA ( 60 ) 17 0 1133 ALA ( 61 ) 17 0 1155 HIS ( 16 ) 18 0 1156 ARG ( 17 ) 18 0 1187 SER ( 48 ) 18 0 1188 VAL ( 49 ) 18 0 1189 GLU ( 50 ) 18 0 1193 GLN ( 54 ) 18 0 1194 GLU ( 55 ) 18 0 1196 ALA ( 57 ) 18 0 1197 GLU ( 58 ) 18 0 1199 ALA ( 60 ) 18 0 1200 ALA ( 61 ) 18 0 1222 HIS ( 16 ) 19 0 1223 ARG ( 17 ) 19 0 1254 SER ( 48 ) 19 0 1255 VAL ( 49 ) 19 0 1259 SER ( 53 ) 19 0 1260 GLN ( 54 ) 19 0 1261 GLU ( 55 ) 19 0 1262 GLU ( 56 ) 19 0 1263 ALA ( 57 ) 19 0 1266 ALA ( 60 ) 19 0 1267 ALA ( 61 ) 19 0 1271 SER ( 65 ) 19 0 1276 ASN ( 3 ) 20 0 1277 ALA ( 4 ) 20 0 1289 HIS ( 16 ) 20 0 1290 ARG ( 17 ) 20 0 1291 CYS ( 18 ) 20 0 1294 CYS ( 21 ) 20 0 1322 VAL ( 49 ) 20 0 1323 GLU ( 50 ) 20 0 1324 PRO ( 51 ) 20 0 1325 TYR ( 52 ) 20 0 1326 SER ( 53 ) 20 0 1327 GLN ( 54 ) 20 0 1330 ALA ( 57 ) 20 0 1331 GLU ( 58 ) 20 0 1332 ARG ( 59 ) 20 0 1334 ALA ( 61 ) 20 0 1336 MET ( 63 ) 20 0 5 GLU ( 5 ) 1 1 21 CYS ( 21 ) 1 1 22 ALA ( 22 ) 1 1 56 GLU ( 56 ) 1 1 57 ALA ( 57 ) 1 1 60 ALA ( 60 ) 1 1 61 ALA ( 61 ) 1 1 73 PHE ( 6 ) 2 1 89 ALA ( 22 ) 2 1 93 ILE ( 26 ) 2 1 103 ARG ( 36 ) 2 1 117 GLU ( 50 ) 2 1 139 GLU ( 5 ) 3 1 146 GLY ( 12 ) 3 1 147 GLY ( 13 ) 3 1 156 ALA ( 22 ) 3 1 170 ARG ( 36 ) 3 1 184 GLU ( 50 ) 3 1 195 ALA ( 61 ) 3 1 214 GLY ( 13 ) 4 1 223 ALA ( 22 ) 4 1 227 ILE ( 26 ) 4 1 237 ARG ( 36 ) 4 1 249 SER ( 48 ) 4 1 254 SER ( 53 ) 4 1 258 ALA ( 57 ) 4 1 289 CYS ( 21 ) 5 1 290 ALA ( 22 ) 5 1 316 SER ( 48 ) 5 1 329 ALA ( 61 ) 5 1 339 ALA ( 4 ) 6 1 340 GLU ( 5 ) 6 1 357 ALA ( 22 ) 6 1 391 GLU ( 56 ) 6 1 392 ALA ( 57 ) 6 1 395 ALA ( 60 ) 6 1 407 GLU ( 5 ) 7 1 423 CYS ( 21 ) 7 1 424 ALA ( 22 ) 7 1 428 ILE ( 26 ) 7 1 438 ARG ( 36 ) 7 1 450 SER ( 48 ) 7 1 473 ALA ( 4 ) 8 1 482 GLY ( 13 ) 8 1 491 ALA ( 22 ) 8 1 518 VAL ( 49 ) 8 1 526 ALA ( 57 ) 8 1 549 GLY ( 13 ) 9 1 550 GLY ( 14 ) 9 1 558 ALA ( 22 ) 9 1 562 ILE ( 26 ) 9 1 596 ALA ( 60 ) 9 1 607 ALA ( 4 ) 10 1 616 GLY ( 13 ) 10 1 639 ARG ( 36 ) 10 1 660 ALA ( 57 ) 10 1 674 ALA ( 4 ) 11 1 683 GLY ( 13 ) 11 1 688 CYS ( 18 ) 11 1 718 SER ( 48 ) 11 1 728 GLU ( 58 ) 11 1 732 GLY ( 62 ) 11 1 735 SER ( 65 ) 11 1 759 ALA ( 22 ) 12 1 763 ILE ( 26 ) 12 1 773 ARG ( 36 ) 12 1 785 SER ( 48 ) 12 1 790 SER ( 53 ) 12 1 797 ALA ( 60 ) 12 1 822 CYS ( 18 ) 13 1 825 CYS ( 21 ) 13 1 830 ILE ( 26 ) 13 1 855 PRO ( 51 ) 13 1 858 GLN ( 54 ) 13 1 861 ALA ( 57 ) 13 1 864 ALA ( 60 ) 13 1 892 CYS ( 21 ) 14 1 921 GLU ( 50 ) 14 1 929 GLU ( 58 ) 14 1 932 ALA ( 61 ) 14 1 951 GLY ( 13 ) 15 1 960 ALA ( 22 ) 15 1 974 ARG ( 36 ) 15 1 993 GLU ( 55 ) 15 1 999 ALA ( 61 ) 15 1 1009 ALA ( 4 ) 16 1 1016 PRO ( 11 ) 16 1 1027 ALA ( 22 ) 16 1 1041 ARG ( 36 ) 16 1 1064 ARG ( 59 ) 16 1 1088 HIS ( 16 ) 17 1 1093 CYS ( 21 ) 17 1 1094 ALA ( 22 ) 17 1 1120 SER ( 48 ) 17 1 1152 GLY ( 13 ) 18 1 1157 CYS ( 18 ) 18 1 1160 CYS ( 21 ) 18 1 1161 ALA ( 22 ) 18 1 1165 ILE ( 26 ) 18 1 1191 TYR ( 52 ) 18 1 1198 ARG ( 59 ) 18 1 1202 MET ( 63 ) 18 1 1210 ALA ( 4 ) 19 1 1211 GLU ( 5 ) 19 1 1227 CYS ( 21 ) 19 1 1232 ILE ( 26 ) 19 1 1258 TYR ( 52 ) 19 1 1278 GLU ( 5 ) 20 1 1295 ALA ( 22 ) 20 1 1299 ILE ( 26 ) 20 1 1321 SER ( 48 ) 20 1 1329 GLU ( 56 ) 20 1 6 PHE ( 6 ) 1 2 49 VAL ( 49 ) 1 2 80 GLY ( 13 ) 2 2 124 ALA ( 57 ) 2 2 127 ALA ( 60 ) 2 2 196 GLY ( 62 ) 3 2 206 GLU ( 5 ) 4 2 281 GLY ( 13 ) 5 2 348 GLY ( 13 ) 6 2 349 GLY ( 14 ) 6 2 415 GLY ( 13 ) 7 2 416 GLY ( 14 ) 7 2 452 GLU ( 50 ) 7 2 475 PHE ( 6 ) 8 2 483 GLY ( 14 ) 8 2 485 HIS ( 16 ) 8 2 495 ILE ( 26 ) 8 2 524 GLU ( 55 ) 8 2 528 ARG ( 59 ) 8 2 531 GLY ( 62 ) 8 2 540 ALA ( 4 ) 9 2 548 GLY ( 12 ) 9 2 557 CYS ( 21 ) 9 2 572 ARG ( 36 ) 9 2 589 SER ( 53 ) 9 2 691 CYS ( 21 ) 11 2 692 ALA ( 22 ) 11 2 720 GLU ( 50 ) 11 2 721 PRO ( 51 ) 11 2 727 ALA ( 57 ) 11 2 787 GLU ( 50 ) 12 2 808 ALA ( 4 ) 13 2 809 GLU ( 5 ) 13 2 818 GLY ( 14 ) 13 2 826 ALA ( 22 ) 13 2 840 ARG ( 36 ) 13 2 867 MET ( 63 ) 13 2 884 GLY ( 13 ) 14 2 943 GLU ( 5 ) 15 2 952 GLY ( 14 ) 15 2 954 HIS ( 16 ) 15 2 1011 PHE ( 6 ) 16 2 1085 GLY ( 13 ) 17 2 1108 ARG ( 36 ) 17 2 1143 ALA ( 4 ) 18 2 1144 GLU ( 5 ) 18 2 1228 ALA ( 22 ) 19 2 1286 GLY ( 13 ) 20 2 1333 ALA ( 60 ) 20 2 # 136 # Error: Backbone conformation Z-score very low A comparison of the backbone conformation with database proteins shows that the backbone fold in this structure is very unusual. Backbone conformation Z-score : -6.075 # 137 # Note: Per-model averages for the backbone conformation check The table below gives the per-model Z-scores for the backbone conformation check. Model 1 : -3.734 Model 2 : -5.581 Model 3 : -6.606 Model 4 : -5.073 Model 5 : -5.203 Model 6 : -7.883 Model 7 : -7.439 Model 8 : -6.280 Model 9 : -6.159 Model 10 : -8.064 Model 11 : -6.215 Model 12 : -4.742 Model 13 : -6.422 Model 14 : -5.214 Model 15 : -6.729 Model 16 : -6.214 Model 17 : -5.572 Model 18 : -5.619 Model 19 : -5.495 Model 20 : -7.257 # 138 # Error: HIS, ASN, GLN side chain flips Listed here are Histidine, Asparagine or Glutamine residues for which the orientation determined from hydrogen bonding analysis are different from the assignment given in the input. Either they could form energetically more favorable hydrogen bonds if the terminal group was rotated by 180 degrees, or there is no assignment in the input file (atom type 'A') but an assignment could be made. If a residue is marked ``flexible'' the flipped conformation is only slightly better than the non-flipped conformation. 70 ASN ( 3 ) 2 101 HIS ( 34 ) 2 235 HIS ( 34 ) 4 302 HIS ( 34 ) 5 369 HIS ( 34 ) 6 436 HIS ( 34 ) 7 539 ASN ( 3 ) 9 771 HIS ( 34 ) 12 972 HIS ( 34 ) 15 1039 HIS ( 34 ) 16 # 139 # Note: Histidine type assignments For all complete HIS residues in the structure a tentative assignment to HIS-D (protonated on ND1), HIS-E (protonated on NE2), or HIS-H (protonated on both ND1 and NE2, positively charged) is made based on the hydrogen bond network. A second assignment is made based on which of the Engh and Huber [REF] histidine geometries fits best to the structure. In the table below all normal histidine residues are listed. The assignment based on the geometry of the residue is listed first, together with the RMS Z-score for the fit to the Engh and Huber parameters. For all residues where the H-bond assignment is different, the assignment is listed in the last columns, together with its RMS Z-score to the Engh and Huber parameters. As always, the RMS Z-scores should be close to 1.0 if the residues were restrained to the Engh and Huber parameters during refinement. Please note that because the differences between the geometries of the different types are small it is possible that the geometric assignment given here does not correspond to the type used in refinement. This is especially true if the RMS Z-scores are much higher than 1.0. If the two assignments differ, or the ``geometry'' RMS Z-score is high, it is advisable to verify the hydrogen bond assignment, check the HIS type used during the refinement and possibly adjust it. 16 HIS ( 16 ) 1 HIS-E 1.21 34 HIS ( 34 ) 1 HIS-E 1.21 40 HIS ( 40 ) 1 HIS-E 1.23 83 HIS ( 16 ) 2 HIS-E 1.21 101 HIS ( 34 ) 2 HIS-E 1.17 HIS-D 1.82 107 HIS ( 40 ) 2 HIS-E 1.22 150 HIS ( 16 ) 3 HIS-E 1.17 HIS-D 1.83 168 HIS ( 34 ) 3 HIS-E 1.20 174 HIS ( 40 ) 3 HIS-E 1.22 217 HIS ( 16 ) 4 HIS-E 1.20 HIS-D 1.85 235 HIS ( 34 ) 4 HIS-E 1.18 HIS-D 1.84 241 HIS ( 40 ) 4 HIS-E 1.21 284 HIS ( 16 ) 5 HIS-E 1.18 302 HIS ( 34 ) 5 HIS-E 1.20 HIS-D 1.85 308 HIS ( 40 ) 5 HIS-E 1.18 351 HIS ( 16 ) 6 HIS-E 1.23 HIS-D 1.86 369 HIS ( 34 ) 6 HIS-E 1.18 HIS-D 1.84 375 HIS ( 40 ) 6 HIS-E 1.21 418 HIS ( 16 ) 7 HIS-E 1.20 436 HIS ( 34 ) 7 HIS-E 1.20 HIS-D 1.86 442 HIS ( 40 ) 7 HIS-E 1.21 485 HIS ( 16 ) 8 HIS-E 1.20 503 HIS ( 34 ) 8 HIS-E 1.18 509 HIS ( 40 ) 8 HIS-E 1.21 552 HIS ( 16 ) 9 HIS-E 1.21 570 HIS ( 34 ) 9 HIS-E 1.19 576 HIS ( 40 ) 9 HIS-E 1.22 619 HIS ( 16 ) 10 HIS-E 1.20 HIS-D 1.87 637 HIS ( 34 ) 10 HIS-E 1.19 643 HIS ( 40 ) 10 HIS-E 1.22 686 HIS ( 16 ) 11 HIS-E 1.21 704 HIS ( 34 ) 11 HIS-E 1.20 HIS-D 1.85 710 HIS ( 40 ) 11 HIS-E 1.20 753 HIS ( 16 ) 12 HIS-E 1.18 771 HIS ( 34 ) 12 HIS-E 1.19 HIS-D 1.85 777 HIS ( 40 ) 12 HIS-E 1.21 820 HIS ( 16 ) 13 HIS-E 1.23 838 HIS ( 34 ) 13 HIS-E 1.19 844 HIS ( 40 ) 13 HIS-E 1.21 887 HIS ( 16 ) 14 HIS-E 1.20 905 HIS ( 34 ) 14 HIS-E 1.21 911 HIS ( 40 ) 14 HIS-E 1.19 954 HIS ( 16 ) 15 HIS-E 1.19 972 HIS ( 34 ) 15 HIS-E 1.19 HIS-D 1.84 978 HIS ( 40 ) 15 HIS-E 1.18 1021 HIS ( 16 ) 16 HIS-E 1.22 HIS-D 1.87 1039 HIS ( 34 ) 16 HIS-E 1.22 HIS-D 1.90 1045 HIS ( 40 ) 16 HIS-E 1.21 1088 HIS ( 16 ) 17 HIS-E 1.18 1106 HIS ( 34 ) 17 HIS-E 1.20 1112 HIS ( 40 ) 17 HIS-E 1.20 1155 HIS ( 16 ) 18 HIS-E 1.21 1173 HIS ( 34 ) 18 HIS-E 1.20 1179 HIS ( 40 ) 18 HIS-E 1.21 1222 HIS ( 16 ) 19 HIS-E 1.18 1240 HIS ( 34 ) 19 HIS-E 1.19 1246 HIS ( 40 ) 19 HIS-E 1.22 1289 HIS ( 16 ) 20 HIS-E 1.20 1307 HIS ( 34 ) 20 HIS-E 1.20 1313 HIS ( 40 ) 20 HIS-E 1.20 # 140 # Warning: Buried unsatisfied hydrogen bond donors The buried hydrogen bond donors listed in the table below have a hydrogen atom that is not involved in a hydrogen bond in the optimized hydrogen bond network. Hydrogen bond donors that are buried inside the protein normally use all of their hydrogens to form hydrogen bonds within the protein. If there are any non hydrogen bonded buried hydrogen bond donors in the structure they will be listed here. In very good structures the number of listed atoms will tend to zero. 10 LEU ( 10 ) 1 N 14 GLY ( 14 ) 1 N 25 PHE ( 25 ) 1 N 27 ASP ( 27 ) 1 N 55 GLU ( 55 ) 1 N 77 LEU ( 10 ) 2 N 81 GLY ( 14 ) 2 N 82 LEU ( 15 ) 2 N 83 HIS ( 16 ) 2 N 84 ARG ( 17 ) 2 N 85 CYS ( 18 ) 2 N 92 PHE ( 25 ) 2 N 94 ASP ( 27 ) 2 N 95 SER ( 28 ) 2 N 97 ASN ( 30 ) 2 N 124 ALA ( 57 ) 2 N 144 LEU ( 10 ) 3 N 149 LEU ( 15 ) 3 N 150 HIS ( 16 ) 3 N 161 ASP ( 27 ) 3 N 211 LEU ( 10 ) 4 N 216 LEU ( 15 ) 4 N 217 HIS ( 16 ) 4 N 219 CYS ( 18 ) 4 N 228 ASP ( 27 ) 4 N 229 SER ( 28 ) 4 N 231 ASN ( 30 ) 4 N 256 GLU ( 55 ) 4 N 278 LEU ( 10 ) 5 N 285 ARG ( 17 ) 5 N 293 PHE ( 25 ) 5 N 295 ASP ( 27 ) 5 N 318 GLU ( 50 ) 5 N 350 LEU ( 15 ) 6 N 351 HIS ( 16 ) 6 N 355 ALA ( 20 ) 6 N 360 PHE ( 25 ) 6 N 362 ASP ( 27 ) 6 N 363 SER ( 28 ) 6 N 365 ASN ( 30 ) 6 N 392 ALA ( 57 ) 6 N 393 GLU ( 58 ) 6 N 409 ASP ( 7 ) 7 N 412 LEU ( 10 ) 7 N 417 LEU ( 15 ) 7 N 418 HIS ( 16 ) 7 N 419 ARG ( 17 ) 7 N 427 PHE ( 25 ) 7 N 429 ASP ( 27 ) 7 N 432 ASN ( 30 ) 7 N 457 GLU ( 55 ) 7 N 476 ASP ( 7 ) 8 N 479 LEU ( 10 ) 8 N 484 LEU ( 15 ) 8 N 485 HIS ( 16 ) 8 N 494 PHE ( 25 ) 8 N 496 ASP ( 27 ) 8 N 499 ASN ( 30 ) 8 N 536 VAL ( 67 ) 8 N 546 LEU ( 10 ) 9 N 550 GLY ( 14 ) 9 N 553 ARG ( 17 ) 9 N 553 ARG ( 17 ) 9 NE 561 PHE ( 25 ) 9 N 563 ASP ( 27 ) 9 N 564 SER ( 28 ) 9 N 566 ASN ( 30 ) 9 N 593 ALA ( 57 ) 9 N 613 LEU ( 10 ) 10 N 619 HIS ( 16 ) 10 N 620 ARG ( 17 ) 10 N 630 ASP ( 27 ) 10 N 632 THR ( 29 ) 10 N 642 ASP ( 39 ) 10 N 653 GLU ( 50 ) 10 N 670 VAL ( 67 ) 10 N 680 LEU ( 10 ) 11 N 685 LEU ( 15 ) 11 N 686 HIS ( 16 ) 11 N 687 ARG ( 17 ) 11 N 695 PHE ( 25 ) 11 N 697 ASP ( 27 ) 11 N 700 ASN ( 30 ) 11 N 720 GLU ( 50 ) 11 N 725 GLU ( 55 ) 11 N 744 ASP ( 7 ) 12 N 747 LEU ( 10 ) 12 N 751 GLY ( 14 ) 12 N 753 HIS ( 16 ) 12 N 758 CYS ( 21 ) 12 N 762 PHE ( 25 ) 12 N 764 ASP ( 27 ) 12 N 767 ASN ( 30 ) 12 N 814 LEU ( 10 ) 13 N 819 LEU ( 15 ) 13 N 820 HIS ( 16 ) 13 N 829 PHE ( 25 ) 13 N 831 ASP ( 27 ) 13 N 834 ASN ( 30 ) 13 N 838 HIS ( 34 ) 13 NE2 854 GLU ( 50 ) 13 N 859 GLU ( 55 ) 13 N 881 LEU ( 10 ) 14 N 888 ARG ( 17 ) 14 NE 888 ARG ( 17 ) 14 NH1 888 ARG ( 17 ) 14 NH2 889 CYS ( 18 ) 14 N 896 PHE ( 25 ) 14 N 898 ASP ( 27 ) 14 N 901 ASN ( 30 ) 14 N 905 HIS ( 34 ) 14 NE2 928 ALA ( 57 ) 14 N 931 ALA ( 60 ) 14 N 948 LEU ( 10 ) 15 N 953 LEU ( 15 ) 15 N 954 HIS ( 16 ) 15 N 955 ARG ( 17 ) 15 N 956 CYS ( 18 ) 15 N 963 PHE ( 25 ) 15 N 965 ASP ( 27 ) 15 N 968 ASN ( 30 ) 15 N 991 SER ( 53 ) 15 N 1012 ASP ( 7 ) 16 N 1015 LEU ( 10 ) 16 N 1019 GLY ( 14 ) 16 N 1022 ARG ( 17 ) 16 N 1022 ARG ( 17 ) 16 NE 1023 CYS ( 18 ) 16 N 1028 ARG ( 23 ) 16 N 1029 TYR ( 24 ) 16 N 1030 PHE ( 25 ) 16 N 1032 ASP ( 27 ) 16 N 1033 SER ( 28 ) 16 N 1061 GLU ( 56 ) 16 N 1079 ASP ( 7 ) 17 N 1082 LEU ( 10 ) 17 N 1088 HIS ( 16 ) 17 N 1092 ALA ( 20 ) 17 N 1097 PHE ( 25 ) 17 N 1099 ASP ( 27 ) 17 N 1100 SER ( 28 ) 17 N 1122 GLU ( 50 ) 17 N 1124 TYR ( 52 ) 17 N 1149 LEU ( 10 ) 18 N 1154 LEU ( 15 ) 18 N 1155 HIS ( 16 ) 18 N 1166 ASP ( 27 ) 18 N 1169 ASN ( 30 ) 18 N 1173 HIS ( 34 ) 18 NE2 1188 VAL ( 49 ) 18 N 1189 GLU ( 50 ) 18 N 1195 GLU ( 56 ) 18 N 1196 ALA ( 57 ) 18 N 1213 ASP ( 7 ) 19 N 1216 LEU ( 10 ) 19 N 1233 ASP ( 27 ) 19 N 1234 SER ( 28 ) 19 N 1261 GLU ( 55 ) 19 N 1267 ALA ( 61 ) 19 N 1280 ASP ( 7 ) 20 N 1283 LEU ( 10 ) 20 N 1286 GLY ( 13 ) 20 N 1300 ASP ( 27 ) 20 N 1303 ASN ( 30 ) 20 N 1328 GLU ( 55 ) 20 N # 141 # Warning: Buried unsatisfied hydrogen bond acceptors The buried side-chain hydrogen bond acceptors listed in the table below are not involved in a hydrogen bond in the optimized hydrogen bond network. Side-chain hydrogen bond acceptors that are buried inside the protein normally form hydrogen bonds within the protein. If there are any not hydrogen bonded in the optimized hydrogen bond network they will be listed here. 704 HIS ( 34 ) 11 NE2 # 142 # Note: Summary report for users of a structure This is an overall summary of the quality of the structure as compared with current reliable structures. This summary is most useful for biologists seeking a good structure to use for modelling calculations. The second part of the table mostly gives an impression of how well the model conforms to common refinement constraint values. The first part of the table shows a number of constraint-independent quality indicators. Structure Z-scores, positive is better than average: 1st generation packing quality : -5.553 (poor) 2nd generation packing quality : -6.781 (bad) Ramachandran plot appearance : -6.551 (bad) chi-1/chi-2 rotamer normality : -5.676 (bad) Backbone conformation : -6.075 (bad) RMS Z-scores, should be close to 1.0: Bond lengths : 0.517 (tight) Bond angles : 0.902 Omega angle restraints : 0.000 (tight) Side chain planarity : 0.040 (tight) Improper dihedral distribution : 0.879 Inside/Outside distribution : 1.117 REFERENCES ========== WHAT IF G.Vriend, WHAT IF: a molecular modelling and drug design program, J. Mol. Graph. 8, 52--56 (1990). WHAT_CHECK (verification routines from WHAT IF) R.W.W.Hooft, G.Vriend, C.Sander and E.E.Abola, Errors in protein structures Nature 381, 272 (1996). Bond lengths and angles, protein residues R.Engh and R.Huber, Accurate bond and angle parameters for X-ray protein structure refinement, Acta Crystallogr. A47, 392--400 (1991). Bond lengths and angles, DNA/RNA G.Parkinson, J.Voitechovsky, L.Clowney, A.T.Bruenger and H.Berman, New parameters for the refinement of nucleic acid-containing structures Acta Crystallogr. D52, 57--64 (1996). DSSP W.Kabsch and C.Sander, Dictionary of protein secondary structure: pattern recognition of hydrogen bond and geometrical features Biopolymers 22, 2577--2637 (1983). Hydrogen bond networks R.W.W.Hooft, C.Sander and G.Vriend, Positioning hydrogen atoms by optimizing hydrogen bond networks in protein structures PROTEINS, 26, 363--376 (1996). Matthews' Coefficient B.W.Matthews Solvent content of Protein Crystals J. Mol. Biol. 33, 491--497 (1968). Protein side chain planarity R.W.W. Hooft, C. Sander and G. Vriend, Verification of protein structures: side-chain planarity J. Appl. Cryst. 29, 714--716 (1996). Puckering parameters D.Cremer and J.A.Pople, A general definition of ring puckering coordinates J. Am. Chem. Soc. 97, 1354--1358 (1975). Quality Control G.Vriend and C.Sander, Quality control of protein models: directional atomic contact analysis, J. Appl. Cryst. 26, 47--60 (1993). Ramachandran plot G.N.Ramachandran, C.Ramakrishnan and V.Sasisekharan, Stereochemistry of Polypeptide Chain Conformations J. Mol. Biol. 7, 95--99 (1963). Symmetry Checks R.W.W.Hooft, C.Sander and G.Vriend, Reconstruction of symmetry related molecules from protein data bank (PDB) files J. Appl. Cryst. 27, 1006--1009 (1994).