Header list of 1ibi.pdb file
Complete list - b 23 2 Bytes
HEADER METAL BINDING PROTEIN 28-MAR-01 1IBI TITLE QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, 15 MINIMIZED MODEL TITLE 2 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYSTEINE-RICH PROTEIN 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL LIM DOMAIN, RESIDUES 82-194; COMPND 5 SYNONYM: CRP2; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: COTURNIX JAPONICA; SOURCE 3 ORGANISM_COMMON: JAPANESE QUAIL; SOURCE 4 ORGANISM_TAXID: 93934; SOURCE 5 GENE: CSRP2; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3D-QCRP2(LIM2) KEYWDS LIM DOMAIN CONTAINING PROTEINS, METAL-BINDING PROTEIN, METAL BINDING KEYWDS 2 PROTEIN EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR W.SCHULER,K.KLOIBER,T.MATT,K.BISTER,R.KONRAT REVDAT 3 23-FEB-22 1IBI 1 REMARK LINK REVDAT 2 24-FEB-09 1IBI 1 VERSN REVDAT 1 05-SEP-01 1IBI 0 JRNL AUTH W.SCHULER,K.KLOIBER,T.MATT,K.BISTER,R.KONRAT JRNL TITL APPLICATION OF CROSS-CORRELATED NMR SPIN RELAXATION TO THE JRNL TITL 2 ZINC-FINGER PROTEIN CRP2(LIM2): EVIDENCE FOR COLLECTIVE JRNL TITL 3 MOTIONS IN LIM DOMAINS. JRNL REF BIOCHEMISTRY V. 40 9596 2001 JRNL REFN ISSN 0006-2960 JRNL PMID 11583159 JRNL DOI 10.1021/BI010509M REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH R.KONRAT,B.KRAEUTLER,R.WEISKIRCHEN,K.BISTER REMARK 1 TITL STRUCTURE OF CYSTEINE- AND GLYCINE-RICH PROTEIN CRP2 REMARK 1 REF J.BIOL.CHEM. V. 273 23233 1998 REMARK 1 REFN ISSN 0021-9258 REMARK 1 DOI 10.1074/JBC.273.36.23233 REMARK 1 REFERENCE 2 REMARK 1 AUTH R.KONRAT,R.WEISKIRCHEN,B.KRAEUTLER,K.BISTER REMARK 1 TITL SOLUTION STRUCTURE OF THE CARBOXYL-TERMINAL LIM DOMAIN FROM REMARK 1 TITL 2 QUAIL CYSTEIN-RICH PROTEIN CRP2 REMARK 1 REF J.BIOL.CHEM. V. 272 12001 1997 REMARK 1 REFN ISSN 0021-9258 REMARK 1 DOI 10.1074/JBC.272.18.12001 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR V6.1 REV.B, X-PLOR 3.851 REMARK 3 AUTHORS : VARIAN ASSOCIATES, INC. (VNMR), BRUNGER, A. (X REMARK 3 -PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THIS ENTRY REPRESENTS THE C-TERMINAL REMARK 3 LIM DOMAIN OF THE QUAIL CYSTEINE RICH PROTEIN CRP2(LIM2) REMARK 3 CONSISTING OF 15 MINIMIZED FINAL STRUCTURES. RESIDUES MET 82 - REMARK 3 ALA 117 AND ASN 175 - GLN 194 WERE NOT OBSERVED AND THERE IS NO REMARK 3 INFORMATION REGARDING THE CONFORMATION THAT THESE RESIDUES MAY REMARK 3 ADOPT IN SOLUTION. THE ONLY STRETCH OF RESIDUES FOR WHICH THERE REMARK 3 IS STRUCTURAL INFORMATION IS GLU 118 - LYS 174 SO THE REMARK 3 SIMULATIONS WERE RESTRICTED TO THE CENTRAL PART ALA 117 - ASN REMARK 3 175, CONTAINING THE TWO ZINC KNUCKLES. IN AN INITIAL STAGE ZINC REMARK 3 WAS COVALENTLY ATTACHED TO A LINEARIZED TEMPLATE STRUCTURE, THEN REMARK 3 TETRAHEDRAL COORDINATION WAS ENFORCED BY DISTANCE CONSTRAINTS. REMARK 3 FINALLY THE ZINC IONS WERE COVALENTLY ATTACHED TO THE REMARK 3 COORDINATING RESIDUES USING STANDARD FORCE FIELD PARAMETERS. 653 REMARK 3 INTER- AND INTRA-RESIDUE NOE RESTRAINTS WERE DEFINED AS STRONG, REMARK 3 MEDIUM, WEAK AND VERY WEAK AND APPLIED DURING THE FINAL REMARK 3 REFINEMENT AS WELL AS 28 TORSION ANGLE RESTRAINTS AND 15 REMARK 3 HYDROGEN BOND RESTRAINTS. OMEGA DIHEDRAL ANGLES WERE RESTRAINED REMARK 3 TO TRANS (E). AVERAGE RMSD FROM EXP. DISTANCE REMARK 3 RESTRAINTS(ANGSTROMS) 0.01, AVERAGE RMSD FROM IDEALIZED COVALENT REMARK 3 GEOMETRY: BONDS(ANGSTROMS): 0.01; ANGLES(DEG) 1.98; REMARK 4 REMARK 4 1IBI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-01. REMARK 100 THE DEPOSITION ID IS D_1000013127. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 299 REMARK 210 PH : 7.2 REMARK 210 IONIC STRENGTH : 20MM POTASSIUM PHOSPHATE; 50MM REMARK 210 KCL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1-2MM QCRP2(LIM2) U-15N,13C; 20 REMARK 210 MM POTASSIUM PHOSPHATE, 50MM KCL, REMARK 210 0.5MM DITHIOTHREITOL, 90% H2O, REMARK 210 10% D2O; 1-2MM QCRP2(LIM2) U-15N; REMARK 210 20 MM POTASSIUM PHOSPHATE, 50MM REMARK 210 KCL, 0.5MM DITHIOTHREITOL, 90% REMARK 210 H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-HSQC; 3D HNCA; 3D HNCACB; 3D REMARK 210 HNCO; 3D CBCA(CO)NH; 3D HCCH-TOCSY; 3D_CCH-TOCSY-NNH; 3D_13C- REMARK 210 NOESY-HSQC_(CA-CENTERED); 3D_13C-NOESY-HSQC_(METHYL-CENTERED); REMARK 210 3D_15N-NOESY-HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS 500 REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE V1.8 REV 2001.030.21.27, REMARK 210 ANSIG V3.3, CNS 1.0 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES REMARK 210 WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: PROJECTION DATA RELATED TO THE BACKBONE DIHEDRALS PHI, PSI REMARK 210 FROM CAHA(I)-DD/C'(I)-CSA AND CAHA(I)-DD/C'(I-1)-CSA RELAXATION REMARK 210 AND 15N(I)-1HN(I)-DD/13CO(I)-CSA AND 1H(I)-15N(I)-13C'(I) DD-CSA REMARK 210 CROSS CORRELATION EXPERIMENTS. SIDE-CHAIN DIHEDRAL ANGLES CHI1 REMARK 210 FROM 2D QUANTITATIVE J-SPECTROSCOPY EXPERIMENTS GIVING ACCESS TO REMARK 210 3J(CO,CGAMMA) AND 3J(N,CGAMMA). DIFFERENTIAL RELAXATION OF REMARK 210 MULTIPLE-QUANTUM COHERENCES GAMMA(I,J)=R(DQ)-R(ZQ), I,J DENOTE REMARK 210 15N,1HN OR 13C',15N, RESPECTIVELY. 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: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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: 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 4 TYR A 172 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES REMARK 500 4 TYR A 172 CB - CG - CD1 ANGL. DEV. = 3.9 DEGREES REMARK 500 9 GLU A 163 N - CA - CB ANGL. DEV. = 12.2 DEGREES REMARK 500 9 GLU A 163 O - C - N ANGL. DEV. = -10.8 DEGREES REMARK 500 10 GLU A 163 N - CA - CB ANGL. DEV. = 12.5 DEGREES REMARK 500 10 GLU A 163 O - C - N ANGL. DEV. = -10.7 DEGREES REMARK 500 11 GLU A 163 N - CA - CB ANGL. DEV. = 13.9 DEGREES REMARK 500 11 GLU A 163 O - C - N ANGL. DEV. = -10.6 DEGREES REMARK 500 11 TYR A 172 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES REMARK 500 11 TYR A 172 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES REMARK 500 12 GLU A 163 N - CA - CB ANGL. DEV. = 12.5 DEGREES REMARK 500 12 GLU A 163 O - C - N ANGL. DEV. = -10.7 DEGREES REMARK 500 13 GLU A 163 O - C - N ANGL. DEV. = -11.1 DEGREES REMARK 500 14 GLU A 163 N - CA - CB ANGL. DEV. = 12.3 DEGREES REMARK 500 14 GLU A 163 O - C - N ANGL. DEV. = -10.8 DEGREES REMARK 500 15 GLU A 163 N - CA - CB ANGL. DEV. = 12.8 DEGREES REMARK 500 15 GLU A 163 O - C - N ANGL. DEV. = -10.6 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 TYR A 128 -74.01 -98.98 REMARK 500 1 ALA A 129 49.79 -156.78 REMARK 500 1 ALA A 130 -90.19 -86.77 REMARK 500 1 LYS A 149 -73.09 -89.56 REMARK 500 1 GLU A 155 -136.51 -82.06 REMARK 500 1 SER A 156 -157.43 -79.78 REMARK 500 2 GLU A 118 -158.98 -152.65 REMARK 500 2 TYR A 128 -97.03 -143.08 REMARK 500 2 ALA A 130 -99.73 -84.80 REMARK 500 2 ALA A 136 -63.09 -96.09 REMARK 500 2 GLU A 155 -84.65 -77.33 REMARK 500 2 GLU A 163 96.01 -27.11 REMARK 500 3 TYR A 128 -49.43 -150.26 REMARK 500 3 ALA A 129 51.98 -157.93 REMARK 500 3 ALA A 130 -100.75 -95.72 REMARK 500 3 ALA A 136 -62.06 -102.33 REMARK 500 3 CYS A 144 32.37 -91.02 REMARK 500 3 SER A 156 -156.31 63.90 REMARK 500 4 GLU A 118 -137.03 -143.94 REMARK 500 4 TYR A 128 -88.56 -106.22 REMARK 500 4 ALA A 129 42.36 -143.41 REMARK 500 4 ALA A 130 -82.29 -87.32 REMARK 500 4 ALA A 136 -73.34 -93.23 REMARK 500 4 CYS A 144 26.13 -150.08 REMARK 500 4 LYS A 149 -71.08 -89.68 REMARK 500 4 GLU A 155 -104.12 -85.43 REMARK 500 4 SER A 156 -137.78 -96.82 REMARK 500 5 GLU A 118 -136.08 -147.52 REMARK 500 5 TYR A 128 -68.33 -98.57 REMARK 500 5 ALA A 129 71.43 -162.26 REMARK 500 5 ALA A 130 -96.63 -93.06 REMARK 500 5 GLU A 131 41.74 -105.81 REMARK 500 5 CYS A 144 33.14 -89.88 REMARK 500 5 GLU A 155 -58.75 -130.39 REMARK 500 6 TYR A 128 -89.52 -135.95 REMARK 500 6 ALA A 130 -87.70 -86.95 REMARK 500 6 ALA A 136 -64.39 -90.68 REMARK 500 6 LYS A 149 -75.15 -104.39 REMARK 500 6 GLU A 155 -88.67 -82.25 REMARK 500 6 SER A 156 -146.86 -103.64 REMARK 500 7 GLU A 118 -157.21 -152.91 REMARK 500 7 TYR A 128 -92.72 -146.54 REMARK 500 7 ALA A 130 -95.58 -88.19 REMARK 500 7 ALA A 136 -85.11 -92.41 REMARK 500 7 CYS A 144 32.76 -98.83 REMARK 500 7 LYS A 149 -72.97 -89.52 REMARK 500 7 GLU A 155 -90.85 -81.75 REMARK 500 7 SER A 156 -125.46 -104.23 REMARK 500 7 THR A 157 -137.31 -86.25 REMARK 500 7 THR A 158 62.00 68.06 REMARK 500 REMARK 500 THIS ENTRY HAS 107 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 9 GLU A 163 14.37 REMARK 500 10 GLU A 163 14.40 REMARK 500 11 GLU A 163 14.43 REMARK 500 12 GLU A 163 14.52 REMARK 500 13 GLU A 163 14.33 REMARK 500 14 GLU A 163 14.57 REMARK 500 15 GLU A 163 14.14 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 195 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 120 SG REMARK 620 2 CYS A 123 SG 108.5 REMARK 620 3 HIS A 141 ND1 108.7 108.8 REMARK 620 4 CYS A 144 SG 107.7 111.8 111.1 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 196 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 147 SG REMARK 620 2 CYS A 150 SG 112.4 REMARK 620 3 CYS A 168 SG 106.7 107.3 REMARK 620 4 CYS A 171 SG 107.0 113.5 109.8 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 195 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 196 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1QLI RELATED DB: PDB REMARK 900 QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, MINIMIZED AVERAGE REMARK 900 STRUCTURE DBREF 1IBI A 82 194 UNP Q05158 CSRP2_COTJA 81 193 SEQRES 1 A 113 MET ASP ARG GLY GLU ARG LEU GLY ILE LYS PRO GLU SER SEQRES 2 A 113 SER PRO SER PRO HIS ARG PRO THR THR ASN PRO ASN THR SEQRES 3 A 113 SER LYS PHE ALA GLN LYS PHE GLY GLY ALA GLU LYS CYS SEQRES 4 A 113 SER ARG CYS GLY ASP SER VAL TYR ALA ALA GLU LYS VAL SEQRES 5 A 113 ILE GLY ALA GLY LYS PRO TRP HIS LYS ASN CYS PHE ARG SEQRES 6 A 113 CYS ALA LYS CYS GLY LYS SER LEU GLU SER THR THR LEU SEQRES 7 A 113 THR GLU LYS GLU GLY GLU ILE TYR CYS LYS GLY CYS TYR SEQRES 8 A 113 ALA LYS ASN PHE GLY PRO LYS GLY PHE GLY TYR GLY GLN SEQRES 9 A 113 GLY ALA GLY ALA LEU VAL HIS ALA GLN HET ZN A 195 1 HET ZN A 196 1 HETNAM ZN ZINC ION FORMUL 2 ZN 2(ZN 2+) HELIX 1 1 CYS A 168 ASN A 175 1 8 SHEET 1 A 2 GLU A 118 LYS A 119 0 SHEET 2 A 2 SER A 126 VAL A 127 -1 O VAL A 127 N GLU A 118 SHEET 1 B 2 VAL A 133 ILE A 134 0 SHEET 2 B 2 PRO A 139 TRP A 140 -1 N TRP A 140 O VAL A 133 SHEET 1 C 2 PHE A 145 ARG A 146 0 SHEET 2 C 2 SER A 153 LEU A 154 -1 O LEU A 154 N PHE A 145 SHEET 1 D 2 THR A 160 LYS A 162 0 SHEET 2 D 2 GLU A 165 TYR A 167 -1 O GLU A 165 N LYS A 162 LINK SG CYS A 120 ZN ZN A 195 1555 1555 2.29 LINK SG CYS A 123 ZN ZN A 195 1555 1555 2.31 LINK ND1 HIS A 141 ZN ZN A 195 1555 1555 2.00 LINK SG CYS A 144 ZN ZN A 195 1555 1555 2.30 LINK SG CYS A 147 ZN ZN A 196 1555 1555 2.27 LINK SG CYS A 150 ZN ZN A 196 1555 1555 2.31 LINK SG CYS A 168 ZN ZN A 196 1555 1555 2.28 LINK SG CYS A 171 ZN ZN A 196 1555 1555 2.29 SITE 1 AC1 4 CYS A 120 CYS A 123 HIS A 141 CYS A 144 SITE 1 AC2 4 CYS A 147 CYS A 150 CYS A 168 CYS A 171 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 - b 23 2 Bytes