Header list of 1mrt.pdb file
Complete list - 23 202 Bytes
HEADER METALLOTHIONEIN 14-MAY-90 1MRT TITLE CONFORMATION OF CD-7 METALLOTHIONEIN-2 FROM RAT LIVER IN AQUEOUS TITLE 2 SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY COMPND MOL_ID: 1; COMPND 2 MOLECULE: CD7 METALLOTHIONEIN-2; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS RATTUS; SOURCE 3 ORGANISM_COMMON: BLACK RAT; SOURCE 4 ORGANISM_TAXID: 10117 KEYWDS METALLOTHIONEIN EXPDTA SOLUTION NMR AUTHOR W.BRAUN,P.SCHULTZE,E.WOERGOETTER,G.WAGNER,M.VASAK,J.H.R.KAEGI, AUTHOR 2 K.WUTHRICH REVDAT 6 23-FEB-22 1MRT 1 REMARK LINK REVDAT 5 24-FEB-09 1MRT 1 VERSN REVDAT 4 01-APR-03 1MRT 1 JRNL REVDAT 3 15-JUL-92 1MRT 1 HET REVDAT 2 15-JUL-91 1MRT 1 HEADER COMPND EXPDTA AUTHOR REVDAT 1 15-APR-91 1MRT 0 JRNL AUTH P.SCHULTZE,E.WORGOTTER,W.BRAUN,G.WAGNER,M.VASAK,J.H.KAGI, JRNL AUTH 2 K.WUTHRICH JRNL TITL CONFORMATION OF [CD7]-METALLOTHIONEIN-2 FROM RAT LIVER IN JRNL TITL 2 AQUEOUS SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE JRNL TITL 3 SPECTROSCOPY. JRNL REF J.MOL.BIOL. V. 203 251 1988 JRNL REFN ISSN 0022-2836 JRNL PMID 3184190 JRNL DOI 10.1016/0022-2836(88)90106-4 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.ARSENIEV,P.SCHULTZE,E.WOERGOETTER,W.BRAUN,G.WAGNER, REMARK 1 AUTH 2 M.VASAK,J.H.R.KAEGI,K.WUTHRICH REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF RABBIT LIVER CD-7 REMARK 1 TITL 2 METALLOTHIONEIN-2A IN AQUEOUS SOLUTION DETERMINED BY NUCLEAR REMARK 1 TITL 3 MAGNETIC RESONANCE. REMARK 1 REF J.MOL.BIOL. V. 201 637 1988 REMARK 1 REFN ISSN 0022-2836 REMARK 1 REFERENCE 2 REMARK 1 AUTH E.WOERGOETTER,G.WAGNER,M.VASAK,J.H.R.KAEGI,K.WUTHRICH REMARK 1 TITL SEQUENCE-SPECIFIC 1H-NMR ASSIGNMENTS IN RAT-LIVER REMARK 1 TITL 2 METALLOTHIONEIN-2 REMARK 1 REF EUR.J.BIOCHEM. V. 167 457 1987 REMARK 1 REFN ISSN 0014-2956 REMARK 1 REFERENCE 3 REMARK 1 AUTH M.VASAK,E.WOERGOETTER,G.WAGNER,J.H.R.KAEGI,K.WUTHRICH REMARK 1 TITL METAL CO-ORDINATION IN RAT LIVER METALLOTHIONEIN-2 PREPARED REMARK 1 TITL 2 WITH OR WITHOUT RECONSTITUTION OF THE METAL CLUSTERS, AND REMARK 1 TITL 3 COMPARISON WITH RABBIT LIVER METALLOTHIONEIN-2. REMARK 1 REF J.MOL.BIOL. V. 196 711 1987 REMARK 1 REFN ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NULL REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1MRT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000175138. 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 : 1 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 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 ALA A 42 H SER A 45 1.57 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 CYS A 33 -48.35 -144.78 REMARK 500 VAL A 39 62.99 179.68 REMARK 500 CYS A 41 153.87 -37.60 REMARK 500 SER A 45 -78.15 -38.13 REMARK 500 CYS A 48 81.67 -57.17 REMARK 500 GLU A 52 102.14 179.09 REMARK 500 ALA A 53 89.25 169.22 REMARK 500 SER A 54 36.06 -88.32 REMARK 500 ASP A 55 -13.85 148.96 REMARK 500 LYS A 56 148.04 -170.48 REMARK 500 CYS A 60 -91.96 -134.38 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 105 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 33 SG REMARK 620 2 CYS A 34 SG 125.2 REMARK 620 3 CYS A 44 SG 105.2 101.4 REMARK 620 4 CYS A 48 SG 88.8 111.2 127.2 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CD A 107 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 34 SG REMARK 620 2 CYS A 36 SG 116.0 REMARK 620 3 CYS A 37 SG 95.4 126.8 REMARK 620 4 CYS A 37 N 68.8 87.8 63.9 REMARK 620 5 CYS A 50 SG 127.4 94.0 99.4 159.5 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CD A 106 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 37 SG REMARK 620 2 CYS A 41 SG 101.3 REMARK 620 3 CYS A 44 SG 116.3 113.7 REMARK 620 4 CYS A 60 SG 93.1 101.3 126.7 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CD A 101 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 50 SG REMARK 620 2 CYS A 57 SG 108.2 REMARK 620 3 CYS A 59 SG 98.3 108.5 REMARK 620 4 CYS A 60 SG 103.9 109.9 126.1 REMARK 620 5 CYS A 60 N 167.1 72.5 93.5 64.6 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: CD1 REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: NULL REMARK 800 REMARK 800 SITE_IDENTIFIER: CD5 REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: NULL REMARK 800 REMARK 800 SITE_IDENTIFIER: CD6 REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: NULL REMARK 800 REMARK 800 SITE_IDENTIFIER: CD7 REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: NULL REMARK 800 REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 101 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 105 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 106 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 107 DBREF 1MRT A 31 61 UNP P04355 MT2_RAT 31 61 SEQRES 1 A 31 LYS SER CYS CYS SER CYS CYS PRO VAL GLY CYS ALA LYS SEQRES 2 A 31 CYS SER GLN GLY CYS ILE CYS LYS GLU ALA SER ASP LYS SEQRES 3 A 31 CYS SER CYS CYS ALA HET CD A 101 1 HET CD A 105 1 HET CD A 106 1 HET CD A 107 1 HETNAM CD CADMIUM ION FORMUL 2 CD 4(CD 2+) LINK SG CYS A 33 CD CD A 105 1555 1555 2.56 LINK SG CYS A 34 CD CD A 105 1555 1555 2.48 LINK SG CYS A 34 CD CD A 107 1555 1555 2.48 LINK SG CYS A 36 CD CD A 107 1555 1555 2.48 LINK SG CYS A 37 CD CD A 106 1555 1555 2.81 LINK SG CYS A 37 CD CD A 107 1555 1555 2.53 LINK N CYS A 37 CD CD A 107 1555 1555 3.15 LINK SG CYS A 41 CD CD A 106 1555 1555 2.53 LINK SG CYS A 44 CD CD A 105 1555 1555 2.53 LINK SG CYS A 44 CD CD A 106 1555 1555 2.50 LINK SG CYS A 48 CD CD A 105 1555 1555 2.51 LINK SG CYS A 50 CD CD A 101 1555 1555 2.56 LINK SG CYS A 50 CD CD A 107 1555 1555 2.65 LINK SG CYS A 57 CD CD A 101 1555 1555 2.50 LINK SG CYS A 59 CD CD A 101 1555 1555 2.53 LINK SG CYS A 60 CD CD A 101 1555 1555 2.60 LINK N CYS A 60 CD CD A 101 1555 1555 3.11 LINK SG CYS A 60 CD CD A 106 1555 1555 2.50 SITE 1 CD1 4 CYS A 50 CYS A 57 CYS A 59 CYS A 60 SITE 1 CD5 4 CYS A 33 CYS A 34 CYS A 44 CYS A 48 SITE 1 CD6 4 CYS A 37 CYS A 41 CYS A 44 CYS A 60 SITE 1 CD7 4 CYS A 34 CYS A 36 CYS A 37 CYS A 50 SITE 1 AC1 4 CYS A 50 CYS A 57 CYS A 59 CYS A 60 SITE 1 AC2 4 CYS A 33 CYS A 34 CYS A 44 CYS A 48 SITE 1 AC3 5 CYS A 37 CYS A 41 CYS A 44 CYS A 50 SITE 2 AC3 5 CYS A 60 SITE 1 AC4 4 CYS A 34 CYS A 36 CYS A 37 CYS A 50 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
Complete list - 23 202 Bytes