Header list of 1cld.pdb file
Complete list - b 16 2 Bytes
HEADER TRANSCRIPTION REGULATION 06-JUN-95 1CLD TITLE DNA-BINDING PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: CD2-LAC9; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS; SOURCE 3 ORGANISM_TAXID: 28985; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ZINC-BINDING DOMAIN, TRANSCRIPTION REGULATION EXPDTA SOLUTION NMR NUMMDL 29 AUTHOR K.H.GARDNER,J.E.COLEMAN REVDAT 5 16-FEB-22 1CLD 1 REMARK LINK REVDAT 4 24-FEB-09 1CLD 1 VERSN REVDAT 3 01-APR-03 1CLD 1 JRNL REVDAT 2 09-JUN-99 1CLD 3 JRNL ATOM REVDAT 1 15-SEP-95 1CLD 0 JRNL AUTH K.H.GARDNER,S.F.ANDERSON,J.E.COLEMAN JRNL TITL SOLUTION STRUCTURE OF THE KLUYVEROMYCES LACTIS LAC9 CD2 CYS6 JRNL TITL 2 DNA-BINDING DOMAIN. JRNL REF NAT.STRUCT.BIOL. V. 2 898 1995 JRNL REFN ISSN 1072-8368 JRNL PMID 7552715 JRNL DOI 10.1038/NSB1095-898 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH K.H.GARDNER,J.E.COLEMAN REMARK 1 TITL 113CD-1H HETEROTOCSY: A METHOD FOR DETERMINING METAL-PROTEIN REMARK 1 TITL 2 CONNECTIVITIES REMARK 1 REF J.BIOMOL.NMR V. 4 761 1994 REMARK 1 REFN ISSN 0925-2738 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1CLD 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_1000172370. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 29 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL 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: 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 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 MODELS 1-29 REMARK 465 RES C SSSEQI REMARK 465 MET A 84 REMARK 465 LYS A 85 REMARK 465 LYS A 86 REMARK 465 SER A 87 REMARK 465 SER A 88 REMARK 465 GLU A 89 REMARK 465 VAL A 90 REMARK 465 MET A 91 REMARK 465 HIS A 92 REMARK 465 PRO A 126 REMARK 465 GLN A 127 REMARK 465 VAL A 128 REMARK 465 VAL A 129 REMARK 465 ARG A 130 REMARK 465 THR A 131 REMARK 465 PRO A 132 REMARK 465 LEU A 133 REMARK 465 THR A 134 REMARK 465 ARG A 135 REMARK 465 ALA A 136 REMARK 465 HIS A 137 REMARK 465 LEU A 138 REMARK 465 THR A 139 REMARK 465 GLU A 140 REMARK 465 MET A 141 REMARK 465 GLU A 142 REMARK 465 ASN A 143 REMARK 465 ARG A 144 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 LYS A 104 145.14 57.21 REMARK 500 1 LYS A 107 57.97 74.60 REMARK 500 1 ASN A 119 82.04 48.01 REMARK 500 2 LYS A 104 93.84 37.14 REMARK 500 2 LYS A 107 64.86 84.52 REMARK 500 2 ASN A 119 85.76 43.48 REMARK 500 3 ALA A 94 -167.66 -177.64 REMARK 500 3 LYS A 104 95.06 35.84 REMARK 500 3 LYS A 107 70.79 81.65 REMARK 500 3 CYS A 112 155.64 -46.10 REMARK 500 3 ASN A 119 84.33 56.24 REMARK 500 4 ALA A 94 167.22 62.52 REMARK 500 4 LYS A 104 97.01 36.75 REMARK 500 4 LYS A 107 60.71 81.70 REMARK 500 4 LYS A 117 -70.16 -65.98 REMARK 500 4 ASN A 119 81.25 41.11 REMARK 500 5 LYS A 104 96.84 35.39 REMARK 500 5 LYS A 107 62.67 82.82 REMARK 500 5 ASN A 119 82.53 44.21 REMARK 500 5 ASP A 121 103.98 -51.39 REMARK 500 6 ALA A 94 154.48 58.24 REMARK 500 6 LYS A 104 96.04 34.93 REMARK 500 6 LYS A 107 69.04 83.50 REMARK 500 6 ASN A 119 73.86 61.14 REMARK 500 7 ALA A 94 153.54 60.29 REMARK 500 7 LYS A 102 59.42 71.63 REMARK 500 7 LYS A 104 97.35 35.02 REMARK 500 7 LYS A 107 73.37 80.82 REMARK 500 7 ASN A 119 80.53 45.24 REMARK 500 8 LYS A 104 135.17 56.83 REMARK 500 8 LYS A 107 62.86 76.60 REMARK 500 8 ASN A 119 72.28 47.94 REMARK 500 9 LYS A 104 96.76 34.90 REMARK 500 9 LYS A 107 77.08 83.18 REMARK 500 9 CYS A 112 155.91 -45.09 REMARK 500 9 ASN A 119 81.45 42.00 REMARK 500 10 TRP A 103 30.91 -99.97 REMARK 500 10 LYS A 104 100.12 36.14 REMARK 500 10 LYS A 107 74.59 81.31 REMARK 500 10 ASN A 119 71.67 48.75 REMARK 500 11 LYS A 104 98.41 36.40 REMARK 500 11 LYS A 107 65.27 80.15 REMARK 500 11 CYS A 112 156.55 -44.68 REMARK 500 11 ASN A 119 80.46 44.99 REMARK 500 12 ALA A 94 142.76 65.03 REMARK 500 12 LYS A 104 97.06 35.09 REMARK 500 12 LYS A 107 72.87 81.10 REMARK 500 12 ASN A 119 83.51 47.68 REMARK 500 13 LYS A 102 47.50 74.47 REMARK 500 13 TRP A 103 30.42 -95.65 REMARK 500 REMARK 500 THIS ENTRY HAS 130 RAMACHANDRAN OUTLIERS. 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 CD A 145 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 95 SG REMARK 620 2 CYS A 98 SG 110.9 REMARK 620 3 CYS A 105 SG 103.1 121.5 REMARK 620 4 CYS A 112 SG 87.6 128.5 98.2 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CD A 146 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 95 SG REMARK 620 2 CYS A 112 SG 86.8 REMARK 620 3 CYS A 115 SG 132.1 97.6 REMARK 620 4 CYS A 122 SG 107.7 111.5 114.6 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 CD A 145 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 146 DBREF 1CLD A 85 144 UNP P08657 LAC9_KLULA 85 144 SEQRES 1 A 61 MET LYS LYS SER SER GLU VAL MET HIS GLN ALA CYS ASP SEQRES 2 A 61 ALA CYS ARG LYS LYS LYS TRP LYS CYS SER LYS THR VAL SEQRES 3 A 61 PRO THR CYS THR ASN CYS LEU LYS TYR ASN LEU ASP CYS SEQRES 4 A 61 VAL TYR SER PRO GLN VAL VAL ARG THR PRO LEU THR ARG SEQRES 5 A 61 ALA HIS LEU THR GLU MET GLU ASN ARG HET CD A 145 1 HET CD A 146 1 HETNAM CD CADMIUM ION FORMUL 2 CD 2(CD 2+) HELIX 1 H1 ASP A 96 LYS A 101 1 6 HELIX 2 H2 THR A 113 TYR A 118 1 6 LINK SG CYS A 95 CD CD A 145 1555 1555 2.52 LINK SG CYS A 95 CD CD A 146 1555 1555 2.53 LINK SG CYS A 98 CD CD A 145 1555 1555 2.45 LINK SG CYS A 105 CD CD A 145 1555 1555 2.46 LINK SG CYS A 112 CD CD A 145 1555 1555 2.51 LINK SG CYS A 112 CD CD A 146 1555 1555 2.53 LINK SG CYS A 115 CD CD A 146 1555 1555 2.51 LINK SG CYS A 122 CD CD A 146 1555 1555 2.53 CISPEP 1 VAL A 109 PRO A 110 1 -0.58 CISPEP 2 VAL A 109 PRO A 110 2 -0.69 CISPEP 3 VAL A 109 PRO A 110 3 -0.72 CISPEP 4 VAL A 109 PRO A 110 4 -0.61 CISPEP 5 VAL A 109 PRO A 110 5 -0.61 CISPEP 6 VAL A 109 PRO A 110 6 -0.74 CISPEP 7 VAL A 109 PRO A 110 7 -0.85 CISPEP 8 VAL A 109 PRO A 110 8 -0.65 CISPEP 9 VAL A 109 PRO A 110 9 -0.99 CISPEP 10 VAL A 109 PRO A 110 10 -0.46 CISPEP 11 VAL A 109 PRO A 110 11 -0.61 CISPEP 12 VAL A 109 PRO A 110 12 -0.65 CISPEP 13 VAL A 109 PRO A 110 13 -0.89 CISPEP 14 VAL A 109 PRO A 110 14 -0.53 CISPEP 15 VAL A 109 PRO A 110 15 -0.94 CISPEP 16 VAL A 109 PRO A 110 16 -0.46 CISPEP 17 VAL A 109 PRO A 110 17 -0.64 CISPEP 18 VAL A 109 PRO A 110 18 -0.51 CISPEP 19 VAL A 109 PRO A 110 19 -0.64 CISPEP 20 VAL A 109 PRO A 110 20 -0.78 CISPEP 21 VAL A 109 PRO A 110 21 -0.45 CISPEP 22 VAL A 109 PRO A 110 22 -0.61 CISPEP 23 VAL A 109 PRO A 110 23 -1.00 CISPEP 24 VAL A 109 PRO A 110 24 -0.71 CISPEP 25 VAL A 109 PRO A 110 25 -0.68 CISPEP 26 VAL A 109 PRO A 110 26 -0.93 CISPEP 27 VAL A 109 PRO A 110 27 -0.59 CISPEP 28 VAL A 109 PRO A 110 28 -0.53 CISPEP 29 VAL A 109 PRO A 110 29 -0.55 SITE 1 AC1 5 CYS A 95 CYS A 98 CYS A 105 CYS A 112 SITE 2 AC1 5 CD A 146 SITE 1 AC2 6 CYS A 95 ALA A 97 CYS A 112 CYS A 115 SITE 2 AC2 6 CYS A 122 CD A 145 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