USER MOD reduce.3.24.130724 H: found=0, std=0, add=83, rem=0, adj=0 USER MOD reduce.3.24.130724 removed 77 hydrogens (0 hets) HEADER LIPID BINDING PROTEIN 30-JUL-00 1FH1 TITLE BACKBONE FOLD OF NODF COMPND MOL_ID: 1; COMPND 2 MOLECULE: NODULATION PROTEIN F; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: NODF; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RHIZOBIUM LEGUMINOSARUM; SOURCE 3 ORGANISM_TAXID: 384; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PMP2301 KEYWDS ROOT NODULATION FACTOR, PROTEIN BACKBONE FOLD, LIPID KEYWDS 2 BINDING PROTEIN EXPDTA SOLUTION NMR AUTHOR C.A.FOWLER,F.TIAN,H.M.AL-HASHIMI,J.H.PRESTEGARD REVDAT 2 24-FEB-09 1FH1 1 VERSN REVDAT 1 17-JAN-01 1FH1 0 JRNL AUTH C.A.FOWLER,F.TIAN,H.M.AL-HASHIMI,J.H.PRESTEGARD JRNL TITL RAPID DETERMINATION OF PROTEIN FOLDS USING JRNL TITL 2 RESIDUAL DIPOLAR COUPLINGS. JRNL REF J.MOL.BIOL. V. 304 447 2000 JRNL REFN ISSN 0022-2836 JRNL PMID 11090286 JRNL DOI 10.1006/JMBI.2000.4199 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH R.GHOSE,O.GEIGER,J.H.PRESTEGARD REMARK 1 TITL NMR INVESTIGATIONS OF THE STRUCTURAL PROPERTIES OF REMARK 1 TITL 2 THE NODULATION PROTEIN, NODF, FROM RHIZOBIUM REMARK 1 TITL 3 LEGUMINOSARUM AND ITS HOMOLOGY WITH ESCHERICIA REMARK 1 TITL 4 COLI ACYL CARRIER PROTEIN REMARK 1 REF FEBS LETT. V. 388 66 1996 REMARK 1 REFN ISSN 0014-5793 REMARK 1 DOI 10.1016/0014-5793(96)00512-1 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : POSE REMARK 3 AUTHORS : FOWLER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: SECONDARY STRUCTURAL ELEMENTS (3 REMARK 3 HELICES) WERE IDENTIFIED. THESE WERE SPLIT INTO SMALLER REMARK 3 FRAGMENTS AND INDIVIDUAL FRAGMENTS WERE ORIENTED USING REMARK 3 RESIDUAL DIPOLAR COUPLING DATA AND THE PROGRAM ORDERTEN_SVD REMARK 3 (LOSONCZI, ET AL., J. MAGN. RES., 138, 334-342, 1999). THE REMARK 3 FRAGMENTS WERE REASSEMBLED AND THEN POSITIONED SPATIALLY BY REMARK 3 TRANSLATION USING A LIMITED SET OF NOES TO PRODUCE A BACKBONE REMARK 3 FOLD OF THE NODF PROTEIN. THERE ARE N-CA-C ANGLE ERRORS (AS REMARK 3 COMPARED TO THE STANDARD DICTIONARY) AT RESIDUES 13 AND 80. REMARK 3 RESIDUE 80 LIES SOMEWHAT OUTSIDE ALLOWED RAMACHANDRAN SPACE. REMARK 3 THESE SITES ARE POSITIONS WHERE ORIENTED HELICAL FRAGMENTS REMARK 3 WERE REASSEMBLED INTO COMPLETE HELICES DURING DETERMINATION OF REMARK 3 OF THE BACKBONE FOLD AND ANY SMALLER LOCAL DISTORTIONS FROM REMARK 3 IDEALITY ARE EXPECTED TO CONCENTRATE HERE. THE STRUCTURE REMARK 3 PRESENTED HERE CONTAINS ONLY COORDINATES FOR BACKBONE ATOMS REMARK 3 INVOLVED IN SECONDARY STRUCTURE. THE STRUCTURE IS THE AVERAGE REMARK 3 OF AN ENSEMBLE WITH A HEAVY ATOM RMSD OF 2.4 ANGSTROMS. CB REMARK 3 POSITIONS COME FROM POLYALANINE HELICES USED TO MODEL THE REMARK 3 BACKBONE. REMARK 4 REMARK 4 1FH1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-00. REMARK 100 THE RCSB ID CODE IS RCSB011579. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298; 298 REMARK 210 PH : 6.1; 6.1 REMARK 210 IONIC STRENGTH : 0; 0 REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 2.5 MM NODF ISOTROPIC U-15N, REMARK 210 13C 200 MM PHOSPHATE BUFFER, REMARK 210 PH 6.1; 1.0 MM NODF ALIGNED U- REMARK 210 15N,13C 200 MM PHOSPHATE REMARK 210 BUFFER, PH 6.1 20 MG/ML PF1 REMARK 210 BACTERIOPHAGE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ, 600 MHZ, 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 98, ORDERTEN_SVD, POSE REMARK 210 METHOD USED : OTHER REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: ASSIGNMENTS WERE MADE USING DOUBLE AND TRIPLE-RESONANCE REMARK 210 NMR SPECTROSCOPY. DIPOLAR COUPLINGS WERE MEASURED AND USED TO REMARK 210 PRODUCE THE PROTEIN BACKBONE FOLD. REMARK 215 REMARK 215 NMR STUDY REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON REMARK 215 THESE RECORDS ARE MEANINGLESS. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 RES C SSSEQI REMARK 465 MET A 1 REMARK 465 ALA A 2 REMARK 465 ASP A 3 REMARK 465 GLN A 4 REMARK 465 LYS A 18 REMARK 465 ALA A 19 REMARK 465 GLU A 20 REMARK 465 ASN A 21 REMARK 465 GLY A 22 REMARK 465 GLU A 23 REMARK 465 ARG A 24 REMARK 465 THR A 25 REMARK 465 SER A 26 REMARK 465 VAL A 27 REMARK 465 ALA A 28 REMARK 465 LEU A 29 REMARK 465 GLY A 30 REMARK 465 GLU A 31 REMARK 465 ILE A 32 REMARK 465 THR A 33 REMARK 465 THR A 34 REMARK 465 ASP A 35 REMARK 465 THR A 36 REMARK 465 GLU A 37 REMARK 465 LEU A 38 REMARK 465 THR A 39 REMARK 465 SER A 40 REMARK 465 LEU A 41 REMARK 465 GLY A 42 REMARK 465 ILE A 43 REMARK 465 ASP A 44 REMARK 465 SER A 45 REMARK 465 TYR A 59 REMARK 465 GLY A 60 REMARK 465 ILE A 61 REMARK 465 LYS A 62 REMARK 465 ILE A 63 REMARK 465 GLU A 64 REMARK 465 MET A 65 REMARK 465 ASN A 66 REMARK 465 THR A 67 REMARK 465 ALA A 68 REMARK 465 ASP A 69 REMARK 465 ALA A 70 REMARK 465 TRP A 71 REMARK 465 SER A 72 REMARK 465 ASN A 73 REMARK 465 LEU A 74 REMARK 465 ASN A 75 REMARK 465 LEU A 87 REMARK 465 LEU A 88 REMARK 465 THR A 89 REMARK 465 LYS A 90 REMARK 465 GLU A 91 REMARK 465 VAL A 92 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(RES=RESIDUE NAME; REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 470 RES CSSEQI ATOMS REMARK 470 LEU A 5 CG CD1 CD2 REMARK 470 THR A 6 OG1 CG2 REMARK 470 LEU A 7 CG CD1 CD2 REMARK 470 GLU A 8 CG CD OE1 OE2 REMARK 470 ILE A 9 CG1 CG2 CD1 REMARK 470 ILE A 10 CG1 CG2 CD1 REMARK 470 SER A 11 OG REMARK 470 ILE A 13 CG1 CG2 CD1 REMARK 470 ASN A 14 CG OD1 ND2 REMARK 470 LYS A 15 CG CD CE NZ REMARK 470 LEU A 16 CG CD1 CD2 REMARK 470 VAL A 17 CG1 CG2 REMARK 470 LEU A 46 CG CD1 CD2 REMARK 470 LEU A 48 CG CD1 CD2 REMARK 470 ASP A 50 CG OD1 OD2 REMARK 470 VAL A 51 CG1 CG2 REMARK 470 LEU A 52 CG CD1 CD2 REMARK 470 TRP A 53 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 53 CZ3 CH2 REMARK 470 ASP A 54 CG OD1 OD2 REMARK 470 LEU A 55 CG CD1 CD2 REMARK 470 GLU A 56 CG CD OE1 OE2 REMARK 470 GLN A 57 CG CD OE1 NE2 REMARK 470 LEU A 58 CG CD1 CD2 REMARK 470 ASN A 76 CG OD1 ND2 REMARK 470 ILE A 77 CG1 CG2 CD1 REMARK 470 ASP A 79 CG OD1 OD2 REMARK 470 VAL A 80 CG1 CG2 REMARK 470 VAL A 81 CG1 CG2 REMARK 470 GLU A 82 CG CD OE1 OE2 REMARK 470 VAL A 84 CG1 CG2 REMARK 470 ARG A 85 CG CD NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O LEU A 7 CB ILE A 10 1.11 REMARK 500 O VAL A 81 N ALA A 83 1.74 REMARK 500 O GLU A 8 N SER A 11 1.88 REMARK 500 O LEU A 7 CA ILE A 10 1.95 REMARK 500 O LEU A 7 N ILE A 10 2.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ILE A 9 N - CA - C ANGL. DEV. = -25.9 DEGREES REMARK 500 ILE A 13 N - CA - CB ANGL. DEV. = -23.0 DEGREES REMARK 500 ILE A 13 N - CA - C ANGL. DEV. = 43.9 DEGREES REMARK 500 ASP A 50 N - CA - C ANGL. DEV. = 29.4 DEGREES REMARK 500 TRP A 53 N - CA - CB ANGL. DEV. = 20.1 DEGREES REMARK 500 VAL A 80 N - CA - CB ANGL. DEV. = -52.0 DEGREES REMARK 500 VAL A 80 N - CA - C ANGL. DEV. = 43.5 DEGREES REMARK 500 GLU A 82 N - CA - CB ANGL. DEV. = -19.1 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 50 -89.30 -99.36 REMARK 500 TRP A 53 -80.70 -44.84 REMARK 500 VAL A 80 7.41 145.50 REMARK 500 GLU A 82 -24.02 -22.06 REMARK 500 REMARK 500 REMARK: NULL DBREF 1FH1 A 1 92 UNP P04685 NODF_RHILV 1 92 SEQRES 1 A 92 MET ALA ASP GLN LEU THR LEU GLU ILE ILE SER ALA ILE SEQRES 2 A 92 ASN LYS LEU VAL LYS ALA GLU ASN GLY GLU ARG THR SER SEQRES 3 A 92 VAL ALA LEU GLY GLU ILE THR THR ASP THR GLU LEU THR SEQRES 4 A 92 SER LEU GLY ILE ASP SER LEU GLY LEU ALA ASP VAL LEU SEQRES 5 A 92 TRP ASP LEU GLU GLN LEU TYR GLY ILE LYS ILE GLU MET SEQRES 6 A 92 ASN THR ALA ASP ALA TRP SER ASN LEU ASN ASN ILE GLY SEQRES 7 A 92 ASP VAL VAL GLU ALA VAL ARG GLY LEU LEU THR LYS GLU SEQRES 8 A 92 VAL HELIX 1 1 LEU A 5 VAL A 17 1 13 HELIX 2 2 ASP A 50 LEU A 58 1 9 HELIX 3 3 VAL A 81 GLY A 86 1 6 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000 ATOM 1 N LEU A 5 16.326 32.357 -3.542 1.00 0.00 N ATOM 2 CA LEU A 5 15.537 31.975 -2.375 1.00 0.00 C ATOM 3 C LEU A 5 14.541 30.896 -2.724 1.00 0.00 C ATOM 4 O LEU A 5 14.388 29.893 -2.019 1.00 0.00 O ATOM 5 CB LEU A 5 14.869 33.249 -1.827 1.00 0.00 C ATOM 0 HA LEU A 5 16.172 31.545 -1.600 1.00 0.00 H new ATOM 8 N THR A 6 13.835 31.094 -3.823 1.00 0.00 N ATOM 9 CA THR A 6 12.835 30.135 -4.283 1.00 0.00 C ATOM 10 C THR A 6 13.450 28.769 -4.485 1.00 0.00 C ATOM 11 O THR A 6 12.910 27.740 -4.059 1.00 0.00 O ATOM 12 CB THR A 6 12.205 30.700 -5.567 1.00 0.00 C ATOM 0 H THR A 6 13.934 31.915 -4.420 1.00 0.00 H new ATOM 0 HA THR A 6 12.054 29.997 -3.535 1.00 0.00 H new ATOM 15 N LEU A 7 14.585 28.738 -5.154 1.00 0.00 N ATOM 16 CA LEU A 7 15.292 27.490 -5.423 1.00 0.00 C ATOM 17 C LEU A 7 15.602 26.755 -4.142 1.00 0.00 C ATOM 18 O LEU A 7 15.389 25.544 -4.012 1.00 0.00 O ATOM 19 CB LEU A 7 16.552 27.832 -6.235 1.00 0.00 C ATOM 0 H LEU A 7 15.046 29.568 -5.527 1.00 0.00 H new ATOM 0 HA LEU A 7 14.670 26.810 -6.005 1.00 0.00 H new ATOM 22 N GLU A 8 16.126 27.482 -3.171 1.00 0.00 N ATOM 23 CA GLU A 8 16.477 26.905 -1.877 1.00 0.00 C ATOM 24 C GLU A 8 15.280 26.250 -1.233 1.00 0.00 C ATOM 25 O GLU A 8 15.342 25.124 -0.725 1.00 0.00 O ATOM 26 CB GLU A 8 17.074 28.030 -1.013 1.00 0.00 C ATOM 0 H GLU A 8 16.320 28.480 -3.251 1.00 0.00 H new ATOM 0 HA GLU A 8 17.216 26.113 -1.993 1.00 0.00 H new ATOM 29 N ILE A 9 14.162 26.952 -1.236 1.00 0.00 N ATOM 30 CA ILE A 9 12.926 26.444 -0.649 1.00 0.00 C ATOM 31 C ILE A 9 13.293 25.144 -1.319 1.00 0.00 C ATOM 32 O ILE A 9 12.972 24.047 -0.847 1.00 0.00 O ATOM 33 CB ILE A 9 11.786 27.187 -1.370 1.00 0.00 C ATOM 0 H ILE A 9 14.080 27.884 -1.641 1.00 0.00 H new ATOM 0 HA ILE A 9 12.646 26.469 0.404 1.00 0.00 H new ATOM 36 N ILE A 10 13.969 25.245 -2.451 1.00 0.00 N ATOM 37 CA ILE A 10 14.391 24.070 -3.208 1.00 0.00 C ATOM 38 C ILE A 10 15.240 23.155 -2.359 1.00 0.00 C ATOM 39 O ILE A 10 15.052 21.932 -2.324 1.00 0.00 O ATOM 40 CB ILE A 10 15.125 24.566 -4.466 1.00 0.00 C ATOM 0 H ILE A 10 14.241 26.134 -2.872 1.00 0.00 H new ATOM 0 HA ILE A 10 13.531 23.473 -3.510 1.00 0.00 H new ATOM 43 N SER A 11 16.202 23.735 -1.665 1.00 0.00 N ATOM 44 CA SER A 11 17.098 22.973 -0.802 1.00 0.00 C ATOM 45 C SER A 11 16.321 22.196 0.234 1.00 0.00 C ATOM 46 O SER A 11 16.561 21.007 0.475 1.00 0.00 O ATOM 47 CB SER A 11 18.096 23.964 -0.178 1.00 0.00 C ATOM 0 H SER A 11 16.387 24.738 -1.680 1.00 0.00 H new ATOM 0 HA SER A 11 17.648 22.226 -1.375 1.00 0.00 H new ATOM 50 N ALA A 12 15.380 22.862 0.875 1.00 0.00 N ATOM 51 CA ALA A 12 14.551 22.237 1.899 1.00 0.00 C ATOM 52 C ALA A 12 13.831 21.028 1.354 1.00 0.00 C ATOM 53 O ALA A 12 13.795 19.955 1.965 1.00 0.00 O ATOM 54 CB ALA A 12 13.588 23.311 2.437 1.00 0.00 C ATOM 0 H ALA A 12 15.166 23.845 0.706 1.00 0.00 H new ATOM 0 HA ALA A 12 15.164 21.864 2.719 1.00 0.00 H new ATOM 0 HB1 ALA A 12 12.951 22.876 3.207 1.00 0.00 H new ATOM 0 HB2 ALA A 12 14.162 24.134 2.863 1.00 0.00 H new ATOM 0 HB3 ALA A 12 12.968 23.685 1.622 1.00 0.00 H new ATOM 57 N ILE A 13 13.234 21.190 0.186 1.00 0.00 N ATOM 58 CA ILE A 13 12.500 20.106 -0.462 1.00 0.00 C ATOM 59 C ILE A 13 12.228 18.667 -0.828 1.00 0.00 C ATOM 60 O ILE A 13 11.246 18.054 -0.391 1.00 0.00 O ATOM 61 CB ILE A 13 12.184 21.085 -1.608 1.00 0.00 C ATOM 0 H ILE A 13 13.241 22.065 -0.339 1.00 0.00 H new ATOM 0 HA ILE A 13 12.317 19.444 0.385 1.00 0.00 H new ATOM 64 N ASN A 14 13.093 18.105 -1.651 1.00 0.00 N ATOM 65 CA ASN A 14 12.955 16.719 -2.091 1.00 0.00 C ATOM 66 C ASN A 14 12.912 15.779 -0.909 1.00 0.00 C ATOM 67 O ASN A 14 12.074 14.874 -0.822 1.00 0.00 O ATOM 68 CB ASN A 14 14.119 16.419 -3.050 1.00 0.00 C ATOM 0 H ASN A 14 13.906 18.587 -2.034 1.00 0.00 H new ATOM 0 HA ASN A 14 12.013 16.568 -2.618 1.00 0.00 H new ATOM 71 N LYS A 15 13.832 15.973 0.016 1.00 0.00 N ATOM 72 CA LYS A 15 13.911 15.139 1.213 1.00 0.00 C ATOM 73 C LYS A 15 12.612 15.167 1.978 1.00 0.00 C ATOM 74 O LYS A 15 12.080 14.134 2.408 1.00 0.00 O ATOM 75 CB LYS A 15 15.107 15.633 2.047 1.00 0.00 C ATOM 0 H LYS A 15 14.542 16.704 -0.034 1.00 0.00 H new ATOM 0 HA LYS A 15 14.070 14.094 0.949 1.00 0.00 H new ATOM 78 N LEU A 16 12.081 16.359 2.176 1.00 0.00 N ATOM 79 CA LEU A 16 10.827 16.539 2.900 1.00 0.00 C ATOM 80 C LEU A 16 9.713 15.748 2.259 1.00 0.00 C ATOM 81 O LEU A 16 8.938 15.050 2.922 1.00 0.00 O ATOM 82 CB LEU A 16 10.532 18.049 2.956 1.00 0.00 C ATOM 0 H LEU A 16 12.500 17.228 1.844 1.00 0.00 H new ATOM 0 HA LEU A 16 10.908 16.156 3.917 1.00 0.00 H new ATOM 85 N VAL A 17 9.608 15.856 0.947 1.00 0.00 N ATOM 86 CA VAL A 17 8.580 15.148 0.191 1.00 0.00 C ATOM 87 C VAL A 17 8.662 13.659 0.430 1.00 0.00 C ATOM 88 O VAL A 17 7.659 12.979 0.675 1.00 0.00 O ATOM 89 CB VAL A 17 8.746 15.526 -1.291 1.00 0.00 C ATOM 0 H VAL A 17 10.226 16.432 0.375 1.00 0.00 H new ATOM 0 HA VAL A 17 7.583 15.441 0.521 1.00 0.00 H new ATOM 92 N LEU A 46 3.975 9.882 9.468 1.00 0.00 N ATOM 93 CA LEU A 46 3.341 9.752 8.158 1.00 0.00 C ATOM 94 C LEU A 46 2.727 11.059 7.721 1.00 0.00 C ATOM 95 O LEU A 46 2.890 11.511 6.582 1.00 0.00 O ATOM 96 CB LEU A 46 2.312 8.610 8.251 1.00 0.00 C ATOM 0 HA LEU A 46 4.077 9.507 7.392 1.00 0.00 H new ATOM 99 N GLY A 47 1.995 11.685 8.623 1.00 0.00 N ATOM 100 CA GLY A 47 1.340 12.959 8.341 1.00 0.00 C ATOM 101 C GLY A 47 2.345 13.999 7.902 1.00 0.00 C ATOM 102 O GLY A 47 2.151 14.722 6.918 1.00 0.00 O ATOM 0 H GLY A 47 1.835 11.332 9.567 1.00 0.00 H new ATOM 0 HA2 GLY A 47 0.590 12.822 7.562 1.00 0.00 H new ATOM 0 HA3 GLY A 47 0.816 13.307 9.231 1.00 0.00 H new ATOM 106 N LEU A 48 3.436 14.095 8.637 1.00 0.00 N ATOM 107 CA LEU A 48 4.493 15.055 8.331 1.00 0.00 C ATOM 108 C LEU A 48 5.015 14.856 6.927 1.00 0.00 C ATOM 109 O LEU A 48 5.187 15.804 6.153 1.00 0.00 O ATOM 110 CB LEU A 48 5.587 14.900 9.401 1.00 0.00 C ATOM 0 H LEU A 48 3.619 13.518 9.458 1.00 0.00 H new ATOM 0 HA LEU A 48 4.111 16.076 8.358 1.00 0.00 H new ATOM 113 N ALA A 49 5.288 13.611 6.583 1.00 0.00 N ATOM 114 CA ALA A 49 5.800 13.270 5.260 1.00 0.00 C ATOM 115 C ALA A 49 4.862 13.750 4.177 1.00 0.00 C ATOM 116 O ALA A 49 5.270 14.351 3.176 1.00 0.00 O ATOM 117 CB ALA A 49 6.021 11.748 5.223 1.00 0.00 C ATOM 0 H ALA A 49 5.164 12.811 7.203 1.00 0.00 H new ATOM 0 HA ALA A 49 6.749 13.772 5.070 1.00 0.00 H new ATOM 0 HB1 ALA A 49 6.405 11.460 4.244 1.00 0.00 H new ATOM 0 HB2 ALA A 49 6.740 11.466 5.992 1.00 0.00 H new ATOM 0 HB3 ALA A 49 5.075 11.238 5.406 1.00 0.00 H new ATOM 120 N ASP A 50 3.583 13.480 4.357 1.00 0.00 N ATOM 121 CA ASP A 50 2.565 13.883 3.393 1.00 0.00 C ATOM 122 C ASP A 50 1.533 14.964 3.174 1.00 0.00 C ATOM 123 O ASP A 50 1.790 15.999 2.547 1.00 0.00 O ATOM 124 CB ASP A 50 2.328 12.645 2.509 1.00 0.00 C ATOM 0 H ASP A 50 3.218 12.979 5.167 1.00 0.00 H new ATOM 0 HA ASP A 50 2.950 14.890 3.554 1.00 0.00 H new ATOM 127 N VAL A 51 0.336 14.732 3.681 1.00 0.00 N ATOM 128 CA VAL A 51 -0.759 15.688 3.547 1.00 0.00 C ATOM 129 C VAL A 51 -0.376 17.032 4.116 1.00 0.00 C ATOM 130 O VAL A 51 -0.594 18.089 3.508 1.00 0.00 O ATOM 131 CB VAL A 51 -1.995 15.080 4.232 1.00 0.00 C ATOM 0 H VAL A 51 0.092 13.885 4.194 1.00 0.00 H new ATOM 0 HA VAL A 51 -0.989 15.871 2.497 1.00 0.00 H new ATOM 134 N LEU A 52 0.195 17.016 5.306 1.00 0.00 N ATOM 135 CA LEU A 52 0.616 18.241 5.979 1.00 0.00 C ATOM 136 C LEU A 52 1.584 19.022 5.123 1.00 0.00 C ATOM 137 O LEU A 52 1.470 20.241 4.951 1.00 0.00 O ATOM 138 CB LEU A 52 1.212 17.844 7.341 1.00 0.00 C ATOM 0 H LEU A 52 0.381 16.163 5.834 1.00 0.00 H new ATOM 0 HA LEU A 52 -0.232 18.906 6.143 1.00 0.00 H new ATOM 141 N TRP A 53 2.567 18.328 4.580 1.00 0.00 N ATOM 142 CA TRP A 53 3.576 18.952 3.728 1.00 0.00 C ATOM 143 C TRP A 53 2.909 19.885 2.748 1.00 0.00 C ATOM 144 O TRP A 53 2.871 21.109 2.928 1.00 0.00 O ATOM 145 CB TRP A 53 4.931 18.422 3.220 1.00 0.00 C ATOM 0 H TRP A 53 2.693 17.324 4.712 1.00 0.00 H new ATOM 0 HA TRP A 53 4.135 19.289 4.601 1.00 0.00 H new ATOM 148 N ASP A 54 2.378 19.320 1.679 1.00 0.00 N ATOM 149 CA ASP A 54 1.701 20.101 0.648 1.00 0.00 C ATOM 150 C ASP A 54 0.567 20.906 1.235 1.00 0.00 C ATOM 151 O ASP A 54 0.400 22.100 0.960 1.00 0.00 O ATOM 152 CB ASP A 54 1.235 19.124 -0.445 1.00 0.00 C ATOM 0 H ASP A 54 2.401 18.317 1.497 1.00 0.00 H new ATOM 0 HA ASP A 54 2.379 20.832 0.207 1.00 0.00 H new ATOM 155 N LEU A 55 -0.243 20.256 2.052 1.00 0.00 N ATOM 156 CA LEU A 55 -1.382 20.908 2.693 1.00 0.00 C ATOM 157 C LEU A 55 -0.936 22.106 3.498 1.00 0.00 C ATOM 158 O LEU A 55 -1.520 23.193 3.431 1.00 0.00 O ATOM 159 CB LEU A 55 -2.102 19.850 3.545 1.00 0.00 C ATOM 0 H LEU A 55 -0.136 19.270 2.291 1.00 0.00 H new ATOM 0 HA LEU A 55 -2.077 21.299 1.950 1.00 0.00 H new ATOM 162 N GLU A 56 0.103 21.916 4.288 1.00 0.00 N ATOM 163 CA GLU A 56 0.642 22.985 5.125 1.00 0.00 C ATOM 164 C GLU A 56 1.029 24.181 4.290 1.00 0.00 C ATOM 165 O GLU A 56 0.715 25.334 4.611 1.00 0.00 O ATOM 166 CB GLU A 56 1.823 22.404 5.918 1.00 0.00 C ATOM 0 H GLU A 56 0.597 21.028 4.372 1.00 0.00 H new ATOM 0 HA GLU A 56 -0.110 23.349 5.825 1.00 0.00 H new ATOM 169 N GLN A 57 1.736 23.927 3.206 1.00 0.00 N ATOM 170 CA GLN A 57 2.181 24.987 2.305 1.00 0.00 C ATOM 171 C GLN A 57 1.010 25.790 1.794 1.00 0.00 C ATOM 172 O GLN A 57 1.021 27.027 1.780 1.00 0.00 O ATOM 173 CB GLN A 57 2.989 24.327 1.174 1.00 0.00 C ATOM 0 H GLN A 57 2.019 22.989 2.921 1.00 0.00 H new ATOM 0 HA GLN A 57 2.818 25.700 2.828 1.00 0.00 H new ATOM 176 N LEU A 58 -0.023 25.095 1.355 1.00 0.00 N ATOM 177 CA LEU A 58 -1.225 25.740 0.833 1.00 0.00 C ATOM 178 C LEU A 58 -1.824 26.675 1.856 1.00 0.00 C ATOM 179 O LEU A 58 -2.188 27.820 1.565 1.00 0.00 O ATOM 180 CB LEU A 58 -2.196 24.630 0.400 1.00 0.00 C ATOM 0 H LEU A 58 -0.058 24.076 1.348 1.00 0.00 H new ATOM 0 HA LEU A 58 -0.990 26.364 -0.030 1.00 0.00 H new ATOM 183 N ASN A 76 1.250 22.708 -4.017 1.00 0.00 N ATOM 184 CA ASN A 76 1.293 23.421 -5.291 1.00 0.00 C ATOM 185 C ASN A 76 2.716 23.717 -5.699 1.00 0.00 C ATOM 186 O ASN A 76 3.126 23.508 -6.846 1.00 0.00 O ATOM 187 CB ASN A 76 0.437 24.691 -5.142 1.00 0.00 C ATOM 0 HA ASN A 76 0.883 22.808 -6.094 1.00 0.00 H new ATOM 190 N ILE A 77 3.493 24.226 -4.761 1.00 0.00 N ATOM 191 CA ILE A 77 4.892 24.562 -5.011 1.00 0.00 C ATOM 192 C ILE A 77 5.656 23.356 -5.505 1.00 0.00 C ATOM 193 O ILE A 77 6.418 23.418 -6.478 1.00 0.00 O ATOM 194 CB ILE A 77 5.471 25.145 -3.710 1.00 0.00 C ATOM 0 H ILE A 77 3.180 24.419 -3.810 1.00 0.00 H new ATOM 0 HA ILE A 77 4.979 25.307 -5.802 1.00 0.00 H new ATOM 197 N GLY A 78 5.475 22.239 -4.828 1.00 0.00 N ATOM 198 CA GLY A 78 6.150 20.998 -5.191 1.00 0.00 C ATOM 199 C GLY A 78 5.846 20.613 -6.619 1.00 0.00 C ATOM 200 O GLY A 78 6.731 20.254 -7.405 1.00 0.00 O ATOM 0 H GLY A 78 4.862 22.161 -4.016 1.00 0.00 H new ATOM 0 HA2 GLY A 78 7.226 21.115 -5.064 1.00 0.00 H new ATOM 0 HA3 GLY A 78 5.834 20.199 -4.520 1.00 0.00 H new ATOM 204 N ASP A 79 4.574 20.671 -6.975 1.00 0.00 N ATOM 205 CA ASP A 79 4.133 20.327 -8.322 1.00 0.00 C ATOM 206 C ASP A 79 4.839 21.173 -9.356 1.00 0.00 C ATOM 207 O ASP A 79 5.333 20.681 -10.379 1.00 0.00 O ATOM 208 CB ASP A 79 2.604 20.487 -8.367 1.00 0.00 C ATOM 0 H ASP A 79 3.822 20.955 -6.347 1.00 0.00 H new ATOM 0 HA ASP A 79 4.390 19.296 -8.563 1.00 0.00 H new ATOM 211 N VAL A 80 4.889 22.469 -9.110 1.00 0.00 N ATOM 212 CA VAL A 80 5.538 23.406 -10.019 1.00 0.00 C ATOM 213 C VAL A 80 5.700 24.733 -10.720 1.00 0.00 C ATOM 214 O VAL A 80 6.525 24.901 -11.625 1.00 0.00 O ATOM 215 CB VAL A 80 4.264 22.658 -10.447 1.00 0.00 C ATOM 0 H VAL A 80 4.485 22.904 -8.281 1.00 0.00 H new ATOM 0 HA VAL A 80 6.599 23.633 -9.911 1.00 0.00 H new ATOM 218 N VAL A 81 4.899 25.702 -10.315 1.00 0.00 N ATOM 219 CA VAL A 81 4.946 27.038 -10.902 1.00 0.00 C ATOM 220 C VAL A 81 6.327 27.635 -10.784 1.00 0.00 C ATOM 221 O VAL A 81 6.885 28.194 -11.738 1.00 0.00 O ATOM 222 CB VAL A 81 3.867 27.888 -10.206 1.00 0.00 C ATOM 0 H VAL A 81 4.203 25.592 -9.578 1.00 0.00 H new ATOM 0 HA VAL A 81 4.737 27.001 -11.971 1.00 0.00 H new ATOM 225 N GLU A 82 6.902 27.537 -9.598 1.00 0.00 N ATOM 226 CA GLU A 82 8.236 28.068 -9.339 1.00 0.00 C ATOM 227 C GLU A 82 8.881 28.151 -10.702 1.00 0.00 C ATOM 228 O GLU A 82 9.819 28.924 -10.936 1.00 0.00 O ATOM 229 CB GLU A 82 8.635 26.798 -8.567 1.00 0.00 C ATOM 0 H GLU A 82 6.465 27.092 -8.791 1.00 0.00 H new ATOM 0 HA GLU A 82 8.428 29.024 -8.852 1.00 0.00 H new ATOM 232 N ALA A 83 8.394 27.342 -11.624 1.00 0.00 N ATOM 233 CA ALA A 83 8.922 27.314 -12.985 1.00 0.00 C ATOM 234 C ALA A 83 8.845 28.680 -13.624 1.00 0.00 C ATOM 235 O ALA A 83 9.798 29.170 -14.241 1.00 0.00 O ATOM 236 CB ALA A 83 8.136 26.246 -13.766 1.00 0.00 C ATOM 0 H ALA A 83 7.628 26.689 -11.458 1.00 0.00 H new ATOM 0 HA ALA A 83 9.980 27.051 -12.987 1.00 0.00 H new ATOM 0 HB1 ALA A 83 8.506 26.198 -14.790 1.00 0.00 H new ATOM 0 HB2 ALA A 83 8.267 25.275 -13.287 1.00 0.00 H new ATOM 0 HB3 ALA A 83 7.078 26.507 -13.774 1.00 0.00 H new ATOM 239 N VAL A 84 7.695 29.317 -13.494 1.00 0.00 N ATOM 240 CA VAL A 84 7.477 30.645 -14.058 1.00 0.00 C ATOM 241 C VAL A 84 8.499 31.628 -13.539 1.00 0.00 C ATOM 242 O VAL A 84 9.099 32.408 -14.287 1.00 0.00 O ATOM 243 CB VAL A 84 6.032 31.057 -13.733 1.00 0.00 C ATOM 0 H VAL A 84 6.889 28.935 -12.999 1.00 0.00 H new ATOM 0 HA VAL A 84 7.608 30.635 -15.140 1.00 0.00 H new ATOM 246 N ARG A 85 8.704 31.614 -12.234 1.00 0.00 N ATOM 247 CA ARG A 85 9.662 32.510 -11.592 1.00 0.00 C ATOM 248 C ARG A 85 11.041 32.337 -12.180 1.00 0.00 C ATOM 249 O ARG A 85 11.742 33.303 -12.502 1.00 0.00 O ATOM 250 CB ARG A 85 9.618 32.231 -10.080 1.00 0.00 C ATOM 0 H ARG A 85 8.218 30.989 -11.590 1.00 0.00 H new ATOM 0 HA ARG A 85 9.399 33.553 -11.768 1.00 0.00 H new ATOM 253 N GLY A 86 11.460 31.093 -12.317 1.00 0.00 N ATOM 254 CA GLY A 86 12.774 30.775 -12.869 1.00 0.00 C ATOM 255 C GLY A 86 12.937 31.367 -14.249 1.00 0.00 C ATOM 256 O GLY A 86 13.958 31.982 -14.581 1.00 0.00 O ATOM 0 H GLY A 86 10.908 30.277 -12.053 1.00 0.00 H new ATOM 0 HA2 GLY A 86 13.552 31.159 -12.210 1.00 0.00 H new ATOM 0 HA3 GLY A 86 12.901 29.693 -12.916 1.00 0.00 H new TER 260 GLY A 86 END