Header list of 1ajy.pdb file
Complete list - b 16 2 Bytes
HEADER TRANSCRIPTION REGULATION 12-MAY-97 1AJY TITLE STRUCTURE AND MOBILITY OF THE PUT3 DIMER: A DNA PINCER, NMR, 13 TITLE 2 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: PUT3; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: DNA-BINDING DOMAIN, RESIDUES 31 - 100 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST; SOURCE 4 ORGANISM_TAXID: 4932; SOURCE 5 OTHER_DETAILS: EXPRESSED IN ESCHERICHIA COLI KEYWDS TRANSCRIPTION REGULATION, PUT3 EXPDTA SOLUTION NMR NUMMDL 13 AUTHOR K.J.WALTERS,K.T.DAYIE,R.J.REECE,M.PTASHNE,G.WAGNER REVDAT 3 16-FEB-22 1AJY 1 REMARK LINK REVDAT 2 24-FEB-09 1AJY 1 VERSN REVDAT 1 17-SEP-97 1AJY 0 JRNL AUTH K.J.WALTERS,K.T.DAYIE,R.J.REECE,M.PTASHNE,G.WAGNER JRNL TITL STRUCTURE AND MOBILITY OF THE PUT3 DIMER. JRNL REF NAT.STRUCT.BIOL. V. 4 744 1997 JRNL REFN ISSN 1072-8368 JRNL PMID 9303003 JRNL DOI 10.1038/NSB0997-744 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: PROGRAMS WRITTEN BY MICHAEL NILGES FOR REMARK 3 SYMMETRIC DIMERS WERE USED (NILGES, M. PROTEINS 17, 297-309 REMARK 3 (1993)). STRUCTURES WERE STARTED FROM AN EXTENDED MONOMER REMARK 3 CONFORMATION AND RANDOM ROTATIONS WERE MADE AROUND THE PHI-PSI REMARK 3 ANGLES. THE MONOMER WAS THEN DUPLICATED AND MOLECULAR DYNAMICS REMARK 3 WAS PERFORMED USING NMR DISTANCE RESTRAINTS AND GENERATED REMARK 3 SYMMETRY DISTANCE RESTRAINTS. RMSD CALCULATED BY SUPERIMPOSING REMARK 3 STRUCTURES ON LOWEST ENERGY STRUCTURE FOR RESIDUES 33-62 OF EACH REMARK 3 MONOMER AND 68-98 OF EACH DIMER. RMSD (ANGSTROMS): ATOMS FOR REMARK 3 RESIDUES 33-62: 0.55 ATOMS FOR RESIDUES 33-62: 1.1 BACKBONE REMARK 3 ATOMS FOR RESIDUES 68-98: 0.7 HEAVY ATOMS FOR RESIDUES 68-98: 1.5 REMARK 4 REMARK 4 1AJY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000170909. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY (1H; 13C; 15N); TOCSY; REMARK 210 HNHA; HNHB; P.COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : UP750; AMX600 REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.851 REMARK 210 METHOD USED : MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 13 REMARK 210 CONFORMERS, SELECTION CRITERIA : NO VIOLATION ABOVE 0.5 ANGSTROMS REMARK 210 AND 5 DEGREE DIHEDRAL ANGLE REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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 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 SER A 31 85.10 -167.09 REMARK 500 1 CYS A 34 -179.59 -68.50 REMARK 500 1 CYS A 50 -136.15 -90.31 REMARK 500 1 GLN A 51 -37.36 -136.94 REMARK 500 1 ASN A 57 62.15 39.00 REMARK 500 1 GLU A 64 61.48 -157.52 REMARK 500 1 PRO A 65 -163.53 -62.11 REMARK 500 1 LYS A 67 -74.91 59.33 REMARK 500 1 LYS A 68 166.84 57.90 REMARK 500 1 VAL A 71 -86.90 -164.02 REMARK 500 1 CYS B 34 -179.76 -64.63 REMARK 500 1 PRO B 45 -71.15 -62.47 REMARK 500 1 CYS B 50 -137.00 -65.07 REMARK 500 1 GLN B 51 -40.04 -140.60 REMARK 500 1 SER B 56 -84.62 -84.64 REMARK 500 1 ASN B 57 39.24 172.91 REMARK 500 1 SER B 66 53.65 -98.06 REMARK 500 1 LYS B 67 -79.40 -45.82 REMARK 500 1 LYS B 68 169.71 55.80 REMARK 500 1 VAL B 71 -87.06 -164.18 REMARK 500 2 CYS A 50 -139.01 -81.01 REMARK 500 2 GLN A 51 -39.51 -135.97 REMARK 500 2 SER A 56 -84.35 -83.69 REMARK 500 2 ASN A 57 39.63 172.13 REMARK 500 2 GLU A 64 68.64 -154.70 REMARK 500 2 SER A 66 -84.51 -95.26 REMARK 500 2 LYS A 67 80.64 -65.07 REMARK 500 2 LYS A 68 104.61 -170.65 REMARK 500 2 VAL A 70 107.60 -166.83 REMARK 500 2 VAL A 71 -114.36 -154.17 REMARK 500 2 SER B 31 176.89 53.56 REMARK 500 2 CYS B 34 -177.56 -64.26 REMARK 500 2 CYS B 50 -136.80 -86.61 REMARK 500 2 GLN B 51 -38.39 -138.60 REMARK 500 2 SER B 56 -84.24 -84.62 REMARK 500 2 ASN B 57 39.92 173.12 REMARK 500 2 TYR B 62 -67.84 -124.00 REMARK 500 2 LEU B 63 32.55 -168.58 REMARK 500 2 GLU B 64 84.34 -170.18 REMARK 500 2 PRO B 65 70.48 -64.33 REMARK 500 2 LYS B 67 90.53 47.91 REMARK 500 2 LYS B 68 107.10 -170.86 REMARK 500 2 VAL B 70 107.89 -166.78 REMARK 500 2 VAL B 71 -114.38 -154.38 REMARK 500 3 SER A 31 47.64 -172.01 REMARK 500 3 CYS A 34 -179.05 -55.87 REMARK 500 3 CYS A 50 -135.20 -90.45 REMARK 500 3 GLN A 51 -39.36 -138.16 REMARK 500 3 SER A 56 -83.20 -84.48 REMARK 500 3 ASN A 57 42.10 170.80 REMARK 500 REMARK 500 THIS ENTRY HAS 236 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 1 ARG A 38 0.26 SIDE CHAIN REMARK 500 1 ARG A 40 0.29 SIDE CHAIN REMARK 500 1 ARG A 92 0.23 SIDE CHAIN REMARK 500 1 ARG A 100 0.32 SIDE CHAIN REMARK 500 1 ARG B 38 0.32 SIDE CHAIN REMARK 500 1 ARG B 40 0.29 SIDE CHAIN REMARK 500 1 ARG B 92 0.22 SIDE CHAIN REMARK 500 1 ARG B 100 0.32 SIDE CHAIN REMARK 500 2 ARG A 38 0.31 SIDE CHAIN REMARK 500 2 ARG A 40 0.32 SIDE CHAIN REMARK 500 2 ARG A 92 0.25 SIDE CHAIN REMARK 500 2 ARG A 100 0.25 SIDE CHAIN REMARK 500 2 ARG B 38 0.28 SIDE CHAIN REMARK 500 2 ARG B 40 0.15 SIDE CHAIN REMARK 500 2 ARG B 92 0.25 SIDE CHAIN REMARK 500 2 ARG B 100 0.25 SIDE CHAIN REMARK 500 3 ARG A 38 0.29 SIDE CHAIN REMARK 500 3 ARG A 40 0.27 SIDE CHAIN REMARK 500 3 ARG A 92 0.30 SIDE CHAIN REMARK 500 3 ARG A 100 0.29 SIDE CHAIN REMARK 500 3 ARG B 38 0.30 SIDE CHAIN REMARK 500 3 ARG B 40 0.30 SIDE CHAIN REMARK 500 3 ARG B 92 0.30 SIDE CHAIN REMARK 500 3 ARG B 100 0.29 SIDE CHAIN REMARK 500 4 ARG A 38 0.17 SIDE CHAIN REMARK 500 4 ARG A 40 0.27 SIDE CHAIN REMARK 500 4 ARG A 92 0.32 SIDE CHAIN REMARK 500 4 ARG A 100 0.30 SIDE CHAIN REMARK 500 4 ARG B 38 0.31 SIDE CHAIN REMARK 500 4 ARG B 40 0.30 SIDE CHAIN REMARK 500 4 ARG B 92 0.32 SIDE CHAIN REMARK 500 4 ARG B 100 0.30 SIDE CHAIN REMARK 500 5 ARG A 38 0.26 SIDE CHAIN REMARK 500 5 ARG A 40 0.32 SIDE CHAIN REMARK 500 5 ARG A 92 0.27 SIDE CHAIN REMARK 500 5 ARG A 100 0.27 SIDE CHAIN REMARK 500 5 ARG B 38 0.19 SIDE CHAIN REMARK 500 5 ARG B 40 0.32 SIDE CHAIN REMARK 500 5 ARG B 92 0.27 SIDE CHAIN REMARK 500 5 ARG B 100 0.27 SIDE CHAIN REMARK 500 6 ARG A 38 0.30 SIDE CHAIN REMARK 500 6 ARG A 40 0.30 SIDE CHAIN REMARK 500 6 ARG A 92 0.29 SIDE CHAIN REMARK 500 6 ARG A 100 0.29 SIDE CHAIN REMARK 500 6 ARG B 38 0.26 SIDE CHAIN REMARK 500 6 ARG B 40 0.31 SIDE CHAIN REMARK 500 6 ARG B 92 0.29 SIDE CHAIN REMARK 500 6 ARG B 100 0.29 SIDE CHAIN REMARK 500 7 ARG A 38 0.19 SIDE CHAIN REMARK 500 7 ARG A 40 0.32 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 104 PLANE DEVIATIONS. 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 101 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 34 SG REMARK 620 2 CYS A 37 SG 110.0 REMARK 620 3 CYS A 44 SG 94.8 123.9 REMARK 620 4 CYS A 50 SG 74.6 127.1 107.4 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 102 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 34 SG REMARK 620 2 CYS A 50 SG 81.3 REMARK 620 3 CYS A 53 SG 132.6 98.1 REMARK 620 4 CYS A 60 SG 122.2 75.3 102.9 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN B 101 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS B 34 SG REMARK 620 2 CYS B 37 SG 107.0 REMARK 620 3 CYS B 44 SG 106.8 128.7 REMARK 620 4 CYS B 50 SG 75.6 120.3 104.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN B 102 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS B 34 SG REMARK 620 2 CYS B 50 SG 82.6 REMARK 620 3 CYS B 53 SG 131.8 103.7 REMARK 620 4 CYS B 60 SG 126.8 72.5 100.0 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 101 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 102 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 101 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 102 DBREF 1AJY A 31 100 UNP P25502 PUT3_YEAST 31 100 DBREF 1AJY B 31 100 UNP P25502 PUT3_YEAST 31 100 SEQRES 1 A 71 MET SER VAL ALA CYS LEU SER CYS ARG LYS ARG HIS ILE SEQRES 2 A 71 LYS CYS PRO GLY GLY ASN PRO CYS GLN LYS CYS VAL THR SEQRES 3 A 71 SER ASN ALA ILE CYS GLU TYR LEU GLU PRO SER LYS LYS SEQRES 4 A 71 ILE VAL VAL SER THR LYS TYR LEU GLN GLN LEU GLN LYS SEQRES 5 A 71 ASP LEU ASN ASP LYS THR GLU GLU ASN ASN ARG LEU LYS SEQRES 6 A 71 ALA LEU LEU LEU GLU ARG SEQRES 1 B 71 MET SER VAL ALA CYS LEU SER CYS ARG LYS ARG HIS ILE SEQRES 2 B 71 LYS CYS PRO GLY GLY ASN PRO CYS GLN LYS CYS VAL THR SEQRES 3 B 71 SER ASN ALA ILE CYS GLU TYR LEU GLU PRO SER LYS LYS SEQRES 4 B 71 ILE VAL VAL SER THR LYS TYR LEU GLN GLN LEU GLN LYS SEQRES 5 B 71 ASP LEU ASN ASP LYS THR GLU GLU ASN ASN ARG LEU LYS SEQRES 6 B 71 ALA LEU LEU LEU GLU ARG HET ZN A 101 1 HET ZN A 102 1 HET ZN B 101 1 HET ZN B 102 1 HETNAM ZN ZINC ION FORMUL 3 ZN 4(ZN 2+) HELIX 1 1 LEU A 35 LYS A 39 1 5 HELIX 2 2 LYS A 52 THR A 55 1 4 HELIX 3 3 THR A 73 LEU A 97 1 25 HELIX 4 4 LEU B 35 ARG B 40 1 6 HELIX 5 5 LYS B 52 THR B 55 1 4 HELIX 6 6 THR B 73 LEU B 97 1 25 SHEET 1 A 2 ILE A 69 THR A 73 0 SHEET 2 A 2 ILE B 69 THR B 73 -1 LINK SG CYS A 34 ZN ZN A 101 1555 1555 2.67 LINK SG CYS A 34 ZN ZN A 102 1555 1555 2.32 LINK SG CYS A 37 ZN ZN A 101 1555 1555 2.61 LINK SG CYS A 44 ZN ZN A 101 1555 1555 2.32 LINK SG CYS A 50 ZN ZN A 101 1555 1555 2.74 LINK SG CYS A 50 ZN ZN A 102 1555 1555 2.69 LINK SG CYS A 53 ZN ZN A 102 1555 1555 2.85 LINK SG CYS A 60 ZN ZN A 102 1555 1555 2.85 LINK SG CYS B 34 ZN ZN B 101 1555 1555 2.61 LINK SG CYS B 34 ZN ZN B 102 1555 1555 2.28 LINK SG CYS B 37 ZN ZN B 101 1555 1555 2.75 LINK SG CYS B 44 ZN ZN B 101 1555 1555 2.36 LINK SG CYS B 50 ZN ZN B 101 1555 1555 2.74 LINK SG CYS B 50 ZN ZN B 102 1555 1555 2.67 LINK SG CYS B 53 ZN ZN B 102 1555 1555 2.89 LINK SG CYS B 60 ZN ZN B 102 1555 1555 2.86 CISPEP 1 ASN A 48 PRO A 49 1 -0.79 CISPEP 2 ASN B 48 PRO B 49 1 -0.75 CISPEP 3 ASN A 48 PRO A 49 2 -0.81 CISPEP 4 ASN B 48 PRO B 49 2 -0.55 CISPEP 5 ASN A 48 PRO A 49 3 -0.77 CISPEP 6 ASN B 48 PRO B 49 3 -1.07 CISPEP 7 ASN A 48 PRO A 49 4 -0.74 CISPEP 8 ASN B 48 PRO B 49 4 -1.05 CISPEP 9 ASN A 48 PRO A 49 5 -0.74 CISPEP 10 ASN B 48 PRO B 49 5 -0.48 CISPEP 11 ASN A 48 PRO A 49 6 -0.97 CISPEP 12 ASN B 48 PRO B 49 6 -0.95 CISPEP 13 ASN A 48 PRO A 49 7 -0.67 CISPEP 14 ASN B 48 PRO B 49 7 -0.52 CISPEP 15 ASN A 48 PRO A 49 8 -0.72 CISPEP 16 ASN B 48 PRO B 49 8 -0.97 CISPEP 17 ASN A 48 PRO A 49 9 -0.64 CISPEP 18 ASN B 48 PRO B 49 9 -0.84 CISPEP 19 ASN A 48 PRO A 49 10 -0.84 CISPEP 20 ASN B 48 PRO B 49 10 -0.77 CISPEP 21 ASN A 48 PRO A 49 11 -0.79 CISPEP 22 ASN B 48 PRO B 49 11 -0.79 CISPEP 23 ASN A 48 PRO A 49 12 -0.83 CISPEP 24 ASN B 48 PRO B 49 12 -0.90 CISPEP 25 ASN A 48 PRO A 49 13 -0.76 CISPEP 26 ASN B 48 PRO B 49 13 -0.68 SITE 1 AC1 5 CYS A 34 CYS A 37 CYS A 44 CYS A 50 SITE 2 AC1 5 ZN A 102 SITE 1 AC2 6 CYS A 34 CYS A 50 CYS A 53 ILE A 59 SITE 2 AC2 6 CYS A 60 ZN A 101 SITE 1 AC3 5 CYS B 34 CYS B 37 CYS B 44 CYS B 50 SITE 2 AC3 5 ZN B 102 SITE 1 AC4 6 CYS B 34 CYS B 50 CYS B 53 ILE B 59 SITE 2 AC4 6 CYS B 60 ZN B 101 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 16 2 Bytes