Header list of 1qxn.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 08-SEP-03 1QXN TITLE SOLUTION STRUCTURE OF THE 30 KDA POLYSULFIDE-SULFUR TRANSFERASE TITLE 2 HOMODIMER FROM WOLINELLA SUCCINOGENES COMPND MOL_ID: 1; COMPND 2 MOLECULE: SULFIDE DEHYDROGENASE; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: SUD; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: WOLINELLA SUCCINOGENES; SOURCE 3 ORGANISM_TAXID: 844; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: DH5A; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PQE60_SUD-HIS6 KEYWDS POLYSULFIDE-SULFUR TRANSFERASE, SUD, HOMODIMER, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR Y.J.LIN,F.DANCEA,F.LOEHR,O.KLIMMEK,S.PFEIFFER-MAREK,M.NILGES,H.WIENK, AUTHOR 2 A.KROEGER,H.RUETERJANS REVDAT 3 02-MAR-22 1QXN 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 1QXN 1 VERSN REVDAT 1 24-FEB-04 1QXN 0 JRNL AUTH Y.J.LIN,F.DANCEA,F.LOEHR,O.KLIMMEK,S.PFEIFFER-MAREK, JRNL AUTH 2 M.NILGES,H.WIENK,A.KROEGER,H.RUETERJANS JRNL TITL SOLUTION STRUCTURE OF THE 30 KDA POLYSULFIDE-SULFUR JRNL TITL 2 TRANSFERASE HOMODIMER FROM WOLINELLA SUCCINOGENES JRNL REF BIOCHEMISTRY V. 43 1418 2004 JRNL REFN ISSN 0006-2960 JRNL PMID 14769017 JRNL DOI 10.1021/BI0356597 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, ARIA 1.1 REMARK 3 AUTHORS : BRUKER (XWINNMR), NILGES (ARIA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE FINAL STRUCTURES WERE REFINED IN REMARK 3 EXPLICIT SOLVENT (WATER) REMARK 4 REMARK 4 1QXN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-SEP-03. REMARK 100 THE DEPOSITION ID IS D_1000020193. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 7.6 REMARK 210 IONIC STRENGTH : LESS THAN 100MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1MM SUD NA, 50MM SODIUM REMARK 210 PHOSPHATE NA, 1MM POLYSULFIDE NA, REMARK 210 13MM SULFIDE NA, 100% D2O; 1MM REMARK 210 SUD U-15N, 50MM SODIUM PHOSPHATE REMARK 210 NA, 1MM POLYSULFIDE NA, 13MM REMARK 210 SULFIDE NA, 95% H2O, 5% D2O; 1MM REMARK 210 SUD U-2H,15N, 50MM SODIUM REMARK 210 PHOSPHATE NA, 1MM POLYSULFIDE NA, REMARK 210 13MM SULFIDE NA, 95% H2O, 5% REMARK 210 D2O; 1MM SUD U-15N,13C, 50MM REMARK 210 SODIUM PHOSPHATE NA, 1MM REMARK 210 POLYSULFIDE NA, 13MM SULFIDE NA, REMARK 210 95% H2O, 5% D2O; 1MM SUD U-15N, REMARK 210 13C, 50MM SODIUM PHOSPHATE NA, REMARK 210 1MM POLYSULFIDE NA, 13MM SULFIDE REMARK 210 NA, 100% D2O; 0.55 MM U-15N, REMARK 210 50MM SODIUM PHOSPHATE NA, 1MM REMARK 210 POLYSULFIDE NA, 13MM SULFIDE NA, REMARK 210 6% W/V C8E5/N-OCTANOL (1:0.87), REMARK 210 90% H2O, 10% D2O; 1MM SUD 50% REMARK 210 ASYM. U-2H,15N, 50MM SODIUM REMARK 210 PHOSPHATE NA, 1MM POLYSULFIDE NA, REMARK 210 13MM SULFIDE NA, 95% H2O, 5% REMARK 210 D2O; 1MM SUD 50% ASYM. U-13C, REMARK 210 50MM SODIUM PHOSPHATE NA, 1MM REMARK 210 POLYSULFIDE NA, 13MM SULFIDE NA, REMARK 210 95% H2O, 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 4D_15N/15N-SEPARATED_NOESY; 3D_CT_CH3_13C- REMARK 210 SEPARATED_NOESY; 3D_13C-SEPARATED_NOESY; [15N-1H]-TROSY; 4D_CT_J- REMARK 210 RESOLVED_13C-SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : AURELIA 97, NMRPIPE 1.6, CNS REMARK 210 1.1, ARIA 1.1 REMARK 210 METHOD USED : SIMULATED ANNEALING WITH TORSION REMARK 210 ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 8 REMARK 210 REMARK 210 REMARK: NULL 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 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 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 HB3 ASP A 44 HE1 TYR A 62 1.31 REMARK 500 HB THR B 91 H ALA B 92 1.33 REMARK 500 HD2 ARG A 46 H ASP A 47 1.33 REMARK 500 OD2 ASP B 21 HZ1 LYS B 100 1.54 REMARK 500 HZ3 LYS B 32 OE1 GLU B 36 1.57 REMARK 500 HZ1 LYS A 28 OE2 GLU A 123 1.60 REMARK 500 O LEU A 97 HG1 THR A 101 1.60 REMARK 500 OE2 GLU B 82 HZ2 LYS B 83 1.60 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 3 ASP A 47 CB ASP A 47 CG 2.260 REMARK 500 3 ASP B 47 CB ASP B 47 CG 2.265 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 3 ASP A 47 CB - CG - OD1 ANGL. DEV. = -42.5 DEGREES REMARK 500 3 ASP A 47 CB - CG - OD2 ANGL. DEV. = 9.7 DEGREES REMARK 500 3 ASP B 47 CA - CB - CG ANGL. DEV. = 29.0 DEGREES REMARK 500 3 ASP B 47 CB - CG - OD1 ANGL. DEV. = -37.7 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 1 ASP A 2 42.62 -167.72 REMARK 500 1 LEU A 25 -168.47 -118.20 REMARK 500 1 PRO A 38 3.73 -67.02 REMARK 500 1 ASN A 61 76.80 -110.89 REMARK 500 1 SER A 66 -105.09 -91.96 REMARK 500 1 ARG A 67 -131.64 57.10 REMARK 500 1 LYS A 69 43.09 -152.05 REMARK 500 1 LEU A 70 -2.52 70.54 REMARK 500 1 PRO A 81 9.19 -69.77 REMARK 500 1 CYS A 89 62.75 67.47 REMARK 500 1 THR A 91 -86.08 -76.50 REMARK 500 1 ARG A 94 58.45 74.87 REMARK 500 1 LYS A 108 -72.83 -61.32 REMARK 500 1 SER A 131 104.51 -57.52 REMARK 500 1 ARG B 67 -129.43 -144.47 REMARK 500 1 LYS B 69 44.13 -152.21 REMARK 500 1 LEU B 70 -6.16 68.66 REMARK 500 1 PRO B 81 16.49 -60.95 REMARK 500 1 CYS B 89 67.68 75.26 REMARK 500 1 THR B 91 -109.09 -77.25 REMARK 500 1 ARG B 94 71.02 61.99 REMARK 500 1 LYS B 108 -70.27 -61.26 REMARK 500 1 PRO B 126 108.68 -57.21 REMARK 500 1 HIS B 134 29.75 -151.87 REMARK 500 2 ASP A 2 45.10 -83.80 REMARK 500 2 ARG A 46 -164.27 -162.51 REMARK 500 2 ARG A 67 -96.25 60.38 REMARK 500 2 LYS A 69 16.41 82.25 REMARK 500 2 LEU A 70 -26.52 71.16 REMARK 500 2 PRO A 81 2.67 -68.74 REMARK 500 2 CYS A 89 175.69 173.11 REMARK 500 2 THR A 91 -101.37 -165.55 REMARK 500 2 ARG A 94 -46.10 -136.99 REMARK 500 2 LYS A 108 -87.25 -62.88 REMARK 500 2 ARG A 130 -50.38 69.63 REMARK 500 2 SER A 131 81.61 62.28 REMARK 500 2 ASP B 2 -36.23 -150.76 REMARK 500 2 ASN B 61 71.06 -115.72 REMARK 500 2 ARG B 67 -95.74 61.32 REMARK 500 2 LYS B 69 16.40 81.90 REMARK 500 2 LEU B 70 -26.54 64.36 REMARK 500 2 PRO B 81 6.34 -66.16 REMARK 500 2 CYS B 89 170.28 156.66 REMARK 500 2 THR B 91 -82.21 -11.93 REMARK 500 2 ARG B 94 -29.91 -169.69 REMARK 500 2 LYS B 108 -77.70 -75.55 REMARK 500 2 GLU B 114 30.16 -71.99 REMARK 500 2 ARG B 130 -88.80 50.85 REMARK 500 2 SER B 131 -108.55 62.04 REMARK 500 2 HIS B 132 -104.39 -169.37 REMARK 500 REMARK 500 THIS ENTRY HAS 190 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 3 ASP A 47 0.20 SIDE CHAIN REMARK 500 3 ASP B 47 0.21 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PS5 A 138 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PS5 B 139 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4776 RELATED DB: BMRB REMARK 900 BACKBONE CHEMICAL SHIFT ASSIGNMENTS DBREF 1QXN A 1 129 UNP Q56748 Q56748_WOLSU 21 149 DBREF 1QXN B 1 129 UNP Q56748 Q56748_WOLSU 21 149 SEQADV 1QXN ARG A 130 UNP Q56748 EXPRESSION TAG SEQADV 1QXN SER A 131 UNP Q56748 EXPRESSION TAG SEQADV 1QXN HIS A 132 UNP Q56748 EXPRESSION TAG SEQADV 1QXN HIS A 133 UNP Q56748 EXPRESSION TAG SEQADV 1QXN HIS A 134 UNP Q56748 EXPRESSION TAG SEQADV 1QXN HIS A 135 UNP Q56748 EXPRESSION TAG SEQADV 1QXN HIS A 136 UNP Q56748 EXPRESSION TAG SEQADV 1QXN HIS A 137 UNP Q56748 EXPRESSION TAG SEQADV 1QXN ARG B 130 UNP Q56748 EXPRESSION TAG SEQADV 1QXN SER B 131 UNP Q56748 EXPRESSION TAG SEQADV 1QXN HIS B 132 UNP Q56748 EXPRESSION TAG SEQADV 1QXN HIS B 133 UNP Q56748 EXPRESSION TAG SEQADV 1QXN HIS B 134 UNP Q56748 EXPRESSION TAG SEQADV 1QXN HIS B 135 UNP Q56748 EXPRESSION TAG SEQADV 1QXN HIS B 136 UNP Q56748 EXPRESSION TAG SEQADV 1QXN HIS B 137 UNP Q56748 EXPRESSION TAG SEQRES 1 A 137 ALA ASP MET GLY GLU LYS PHE ASP ALA THR PHE LYS ALA SEQRES 2 A 137 GLN VAL LYS ALA ALA LYS ALA ASP MET VAL MET LEU SER SEQRES 3 A 137 PRO LYS ASP ALA TYR LYS LEU LEU GLN GLU ASN PRO ASP SEQRES 4 A 137 ILE THR LEU ILE ASP VAL ARG ASP PRO ASP GLU LEU LYS SEQRES 5 A 137 ALA MET GLY LYS PRO ASP VAL LYS ASN TYR LYS HIS MET SEQRES 6 A 137 SER ARG GLY LYS LEU GLU PRO LEU LEU ALA LYS SER GLY SEQRES 7 A 137 LEU ASP PRO GLU LYS PRO VAL VAL VAL PHE CYS LYS THR SEQRES 8 A 137 ALA ALA ARG ALA ALA LEU ALA GLY LYS THR LEU ARG GLU SEQRES 9 A 137 TYR GLY PHE LYS THR ILE TYR ASN SER GLU GLY GLY MET SEQRES 10 A 137 ASP LYS TRP LEU GLU GLU GLY LEU PRO SER LEU ASP ARG SEQRES 11 A 137 SER HIS HIS HIS HIS HIS HIS SEQRES 1 B 137 ALA ASP MET GLY GLU LYS PHE ASP ALA THR PHE LYS ALA SEQRES 2 B 137 GLN VAL LYS ALA ALA LYS ALA ASP MET VAL MET LEU SER SEQRES 3 B 137 PRO LYS ASP ALA TYR LYS LEU LEU GLN GLU ASN PRO ASP SEQRES 4 B 137 ILE THR LEU ILE ASP VAL ARG ASP PRO ASP GLU LEU LYS SEQRES 5 B 137 ALA MET GLY LYS PRO ASP VAL LYS ASN TYR LYS HIS MET SEQRES 6 B 137 SER ARG GLY LYS LEU GLU PRO LEU LEU ALA LYS SER GLY SEQRES 7 B 137 LEU ASP PRO GLU LYS PRO VAL VAL VAL PHE CYS LYS THR SEQRES 8 B 137 ALA ALA ARG ALA ALA LEU ALA GLY LYS THR LEU ARG GLU SEQRES 9 B 137 TYR GLY PHE LYS THR ILE TYR ASN SER GLU GLY GLY MET SEQRES 10 B 137 ASP LYS TRP LEU GLU GLU GLY LEU PRO SER LEU ASP ARG SEQRES 11 B 137 SER HIS HIS HIS HIS HIS HIS HET PS5 A 138 5 HET PS5 B 139 5 HETNAM PS5 PENTASULFIDE-SULFUR FORMUL 3 PS5 2(S5 2-) HELIX 1 1 MET A 3 ASP A 21 1 19 HELIX 2 2 SER A 26 ASN A 37 1 12 HELIX 3 3 ASP A 47 MET A 54 1 8 HELIX 4 4 LEU A 73 GLY A 78 1 6 HELIX 5 5 ARG A 94 GLY A 106 1 13 HELIX 6 6 GLY A 116 GLU A 123 1 8 HELIX 7 7 MET B 3 ASP B 21 1 19 HELIX 8 8 SER B 26 ASN B 37 1 12 HELIX 9 9 ASP B 47 GLY B 55 1 9 HELIX 10 10 LEU B 70 ALA B 75 1 6 HELIX 11 11 ALA B 95 GLU B 104 1 10 HELIX 12 12 GLY B 116 GLU B 123 1 8 SHEET 1 A 5 VAL A 23 LEU A 25 0 SHEET 2 A 5 ILE A 110 SER A 113 1 O ASN A 112 N LEU A 25 SHEET 3 A 5 VAL A 85 PHE A 88 1 N VAL A 87 O TYR A 111 SHEET 4 A 5 THR A 41 ASP A 44 1 N ILE A 43 O VAL A 86 SHEET 5 A 5 TYR A 62 HIS A 64 1 O LYS A 63 N LEU A 42 SHEET 1 B 2 LYS A 56 PRO A 57 0 SHEET 2 B 2 SER A 127 LEU A 128 -1 O LEU A 128 N LYS A 56 SHEET 1 C 5 VAL B 23 LEU B 25 0 SHEET 2 C 5 ILE B 110 SER B 113 1 O ASN B 112 N LEU B 25 SHEET 3 C 5 VAL B 85 PHE B 88 1 N VAL B 87 O TYR B 111 SHEET 4 C 5 THR B 41 ASP B 44 1 N ILE B 43 O VAL B 86 SHEET 5 C 5 TYR B 62 HIS B 64 1 O LYS B 63 N LEU B 42 SHEET 1 D 2 LYS B 56 PRO B 57 0 SHEET 2 D 2 SER B 127 LEU B 128 -1 O LEU B 128 N LYS B 56 LINK SG CYS A 89 S1 PS5 A 138 1555 1555 2.03 LINK SG CYS B 89 S1 PS5 B 139 1555 1555 2.03 SITE 1 AC1 6 CYS A 89 THR A 91 ALA A 92 GLY A 115 SITE 2 AC1 6 GLY A 116 MET A 117 SITE 1 AC2 8 ARG B 46 CYS B 89 THR B 91 ALA B 92 SITE 2 AC2 8 ALA B 93 GLY B 116 MET B 117 ASP B 118 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 MODEL 1
Complete list - r 2 2 Bytes