Header list of 2mrb.pdb file
Complete list - 16 202 Bytes
HEADER METALLOTHIONEIN 14-MAY-90 2MRB
TITLE THREE-DIMENSIONAL STRUCTURE OF RABBIT LIVER CD-7 METALLOTHIONEIN-2A IN
TITLE 2 AQUEOUS SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CD7 METALLOTHIONEIN-2A;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986
KEYWDS METALLOTHIONEIN
EXPDTA SOLUTION NMR
AUTHOR W.BRAUN,A.ARSENIEV,P.SCHULTZE,E.WOERGOETTER,G.WAGNER,M.VASAK,
AUTHOR 2 J.H.R.KAEGI,K.WUTHRICH
REVDAT 8 16-MAR-22 2MRB 1 REMARK LINK
REVDAT 7 24-FEB-09 2MRB 1 VERSN
REVDAT 6 01-APR-03 2MRB 1 JRNL
REVDAT 5 15-JUL-92 2MRB 1 HET
REVDAT 4 15-APR-92 2MRB 1 REMARK SEQRES HET
REVDAT 3 15-OCT-91 2MRB 1 REMARK
REVDAT 2 15-JUL-91 2MRB 1 HEADER COMPND EXPDTA
REVDAT 1 15-APR-91 2MRB 0
JRNL AUTH A.ARSENIEV,P.SCHULTZE,E.WORGOTTER,W.BRAUN,G.WAGNER,M.VASAK,
JRNL AUTH 2 J.H.KAGI,K.WUTHRICH
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF RABBIT LIVER
JRNL TITL 2 [CD7]METALLOTHIONEIN-2A IN AQUEOUS SOLUTION DETERMINED BY
JRNL TITL 3 NUCLEAR MAGNETIC RESONANCE.
JRNL REF J.MOL.BIOL. V. 201 637 1988
JRNL REFN ISSN 0022-2836
JRNL PMID 3418714
JRNL DOI 10.1016/0022-2836(88)90644-4
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.WAGNER,D.NEUHAUS,E.WOERGOETTER,M.VASAK,J.H.R.KAEGI,
REMARK 1 AUTH 2 K.WUTHRICH
REMARK 1 TITL NUCLEAR MAGNETIC RESONANCE IDENTIFICATION OF "HALF-TURN" AND
REMARK 1 TITL 2 310-HELIX SECONDARY STRUCTURE IN RABBIT LIVER
REMARK 1 TITL 3 METALLOTHIONEIN-2
REMARK 1 REF J.MOL.BIOL. V. 187 131 1986
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH W.BRAUN,G.WAGNER,E.WOERGOETTER,M.VASAK,J.H.R.KAEGI,
REMARK 1 AUTH 2 K.WUTHRICH
REMARK 1 TITL POLYPEPTIDE FOLD IN THE TWO METAL CLUSTERS OF
REMARK 1 TITL 2 METALLOTHIONEIN-2 BY NUCLEAR MAGNETIC RESONANCE IN SOLUTION
REMARK 1 REF J.MOL.BIOL. V. 187 125 1986
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH G.WAGNER,D.NEUHAUS,E.WOERGOETTER,M.VASAK,J.H.R.KAEGI,
REMARK 1 AUTH 2 K.WUTHRICH
REMARK 1 TITL SEQUENCE-SPECIFIC 1H-NMR ASSIGNMENTS IN RABBIT-LIVER
REMARK 1 TITL 2 METALLOTHIONEIN-2
REMARK 1 REF EUR.J.BIOCHEM. V. 157 275 1986
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 4
REMARK 1 AUTH D.NEUHAUS,G.WAGNER,M.VASAK,J.H.R.KAEGI,K.WUTHRICH
REMARK 1 TITL SYSTEMATIC APPLICATION OF HIGH-RESOLUTION,PHASE-SENSITIVE
REMARK 1 TITL 2 TWO-DIMENSIONAL 1H-NMR TECHNIQUES FOR THE IDENTIFICATION OF
REMARK 1 TITL 3 THE AMINO-ACID-PROTON SPIN SYSTEMS IN PROTEINS
REMARK 1 REF EUR.J.BIOCHEM. V. 151 257 1985
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 5
REMARK 1 AUTH M.H.FREY,G.WAGNER,M.VASAK,O.W.SORENSEN,D.NEUHAUS,
REMARK 1 AUTH 2 E.WOERGOETTER,J.H.R.KAEGI,R.R.ERNST,K.WUTHRICH
REMARK 1 TITL POLYPEPTIDE-METAL CLUSTER CONNECTIVIES IN METALLO THIONEIN 2
REMARK 1 TITL 2 BY NOVEL 1H-113CD HETERONUCLEAR TWO-DIMENSIONAL NMR
REMARK 1 TITL 3 EXPERIMENTS
REMARK 1 REF J.AM.CHEM.SOC. V. 107 6847 1985
REMARK 1 REFN ISSN 0002-7863
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISMAN
REMARK 3 AUTHORS : BRAUN,GO
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2MRB 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_1000178377.
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 ASN A 4 H ALA A 23 1.46
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 PRO A 3 -71.13 -75.02
REMARK 500 CYS A 5 124.04 -170.29
REMARK 500 CYS A 7 -152.76 -105.68
REMARK 500 ALA A 9 106.54 60.92
REMARK 500 ASN A 17 -67.58 -92.63
REMARK 500 ALA A 23 58.99 -142.53
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 104 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 5 SG
REMARK 620 2 CYS A 7 SG 111.7
REMARK 620 3 CYS A 21 SG 115.2 100.1
REMARK 620 4 CYS A 24 SG 107.3 110.6 111.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 103 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 7 SG
REMARK 620 2 CYS A 13 SG 108.5
REMARK 620 3 CYS A 15 SG 89.4 113.5
REMARK 620 4 CYS A 26 SG 96.4 109.8 131.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 102 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 15 SG
REMARK 620 2 CYS A 19 SG 113.9
REMARK 620 3 CYS A 24 SG 100.3 104.2
REMARK 620 4 CYS A 29 SG 108.2 110.7 119.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CD2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: CD3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: CD4
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 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 104
DBREF 2MRB A 1 30 UNP P18055 MT2A_RABIT 1 31
SEQRES 1 A 31 MET ASP PRO ASN CYS SER CYS ALA ALA ALA GLY ASP SER
SEQRES 2 A 31 CYS THR CYS ALA ASN SER CYS THR CYS LYS ALA CYS LYS
SEQRES 3 A 31 CYS THR SER CYS LYS
HET CD A 102 1
HET CD A 103 1
HET CD A 104 1
HETNAM CD CADMIUM ION
FORMUL 2 CD 3(CD 2+)
LINK SG CYS A 5 CD CD A 104 1555 1555 2.53
LINK SG CYS A 7 CD CD A 103 1555 1555 2.70
LINK SG CYS A 7 CD CD A 104 1555 1555 2.54
LINK SG CYS A 13 CD CD A 103 1555 1555 2.53
LINK SG CYS A 15 CD CD A 102 1555 1555 2.60
LINK SG CYS A 15 CD CD A 103 1555 1555 2.53
LINK SG CYS A 19 CD CD A 102 1555 1555 2.53
LINK SG CYS A 21 CD CD A 104 1555 1555 2.53
LINK SG CYS A 24 CD CD A 102 1555 1555 2.54
LINK SG CYS A 24 CD CD A 104 1555 1555 2.61
LINK SG CYS A 26 CD CD A 103 1555 1555 2.54
LINK SG CYS A 29 CD CD A 102 1555 1555 2.53
SITE 1 CD2 4 CYS A 15 CYS A 19 CYS A 24 CYS A 29
SITE 1 CD3 4 CYS A 7 CYS A 13 CYS A 15 CYS A 26
SITE 1 CD4 4 CYS A 5 CYS A 7 CYS A 21 CYS A 24
SITE 1 AC1 4 CYS A 15 CYS A 19 CYS A 24 CYS A 29
SITE 1 AC2 4 CYS A 7 CYS A 13 CYS A 15 CYS A 26
SITE 1 AC3 4 CYS A 5 CYS A 7 CYS A 21 CYS A 24
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 - 16 202 Bytes