Header list of 1qjl.pdb file
Complete list - 16 201 Bytes
HEADER METALLOTHIONEIN 24-JUN-99 1QJL
TITLE METALLOTHIONEIN MTA FROM SEA URCHIN (BETA DOMAIN)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METALLOTHIONEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BETA DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: CADMIUM 3-METAL CLUSTER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STRONGYLOCENTROTUS PURPURATUS;
SOURCE 3 ORGANISM_COMMON: PURPLE SEA URCHIN;
SOURCE 4 ORGANISM_TAXID: 7668;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS METALLOTHIONEIN, METAL-BINDING, DETOXIFICATION, RADICAL SCAVENGER
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR R.RIEK,B.PRECHEUR,Y.WANG,E.A.MACKAY,G.WIDER,P.GUNTERT,A.LIU,
AUTHOR 2 J.H.R.KAEGI,K.WUTHRICH
REVDAT 3 16-JAN-19 1QJL 1 JRNL
REVDAT 2 24-FEB-09 1QJL 1 VERSN
REVDAT 1 31-AUG-99 1QJL 0
JRNL AUTH R.RIEK,B.PRECHEUR,Y.WANG,E.A.MACKAY,G.WIDER,P.GUNTERT,A.LIU,
JRNL AUTH 2 J.H.KAGI,K.WUTHRICH
JRNL TITL NMR STRUCTURE OF THE SEA URCHIN (STRONGYLOCENTROTUS
JRNL TITL 2 PURPURATUS) METALLOTHIONEIN MTA.
JRNL REF J. MOL. BIOL. V. 291 417 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10438629
JRNL DOI 10.1006/JMBI.1999.2967
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.A.MESSERLE,A.SCHAFFER,M.VASAK,J.H.R.KAEGI,K.WUTHRICH
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF HUMAN
REMARK 1 TITL 2 [113CD7]-METALLOTHIONEIN-2 IN SOLUTION DETERMINED BY NUCLEAR
REMARK 1 TITL 3 MAGNETIC RESONANCE SPECTROSCOPY
REMARK 1 REF J.MOL.BIOL. V. 214 765 1990
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 2388267
REMARK 1 DOI 10.1016/0022-2836(90)90291-S
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA (VERSION 1.1) 1.1) 1.1)
REMARK 3 AUTHORS : GUNTERT
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QJL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUN-99.
REMARK 100 THE DEPOSITION ID IS D_1290002875.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 50 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS; AMX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
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: 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 ASN A 40 97.46 -62.06
REMARK 500 ASN A 47 98.39 -40.53
REMARK 500 LYS A 50 42.12 -94.14
REMARK 500 SER A 53 46.07 -150.53
REMARK 500 SER A 56 61.10 -155.34
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 101 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 45 SG
REMARK 620 2 CYS A 49 SG 103.9
REMARK 620 3 CYS A 64 SG 99.5 116.3
REMARK 620 4 CYS A 51 SG 117.2 117.6 101.4
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 38 SG
REMARK 620 2 CYS A 43 SG 102.8
REMARK 620 3 CYS A 51 SG 117.4 113.0
REMARK 620 4 CYS A 55 SG 102.9 102.3 116.4
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 43 SG
REMARK 620 2 CYS A 57 SG 99.5
REMARK 620 3 CYS A 62 SG 111.7 103.8
REMARK 620 4 CYS A 64 SG 115.2 102.5 120.4
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 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 103
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4MT2 RELATED DB: PDB
REMARK 900 RELATED ID: 1QJK RELATED DB: PDB
REMARK 900 THE NMR CHEMICAL SHIFTS ARE DEPOSITED WITH THE BIOMAGRESBANK (BMRB).
DBREF 1QJL A 37 64 UNP P04734 MTA_STRPU 37 64
SEQRES 1 A 28 ILE CYS THR ASN ALA ALA CYS LYS CYS ALA ASN GLY CYS
SEQRES 2 A 28 LYS CYS GLY SER GLY CYS SER CYS THR GLU GLY ASN CYS
SEQRES 3 A 28 ALA CYS
HET CD A 101 1
HET CD A 102 1
HET CD A 103 1
HETNAM CD CADMIUM ION
FORMUL 2 CD 3(CD 2+)
LINK CD CD A 101 SG CYS A 45 1555 1555 2.60
LINK CD CD A 101 SG CYS A 49 1555 1555 2.54
LINK CD CD A 101 SG CYS A 64 1555 1555 2.70
LINK CD CD A 101 SG CYS A 51 1555 1555 2.60
LINK CD CD A 102 SG CYS A 38 1555 1555 2.58
LINK CD CD A 102 SG CYS A 43 1555 1555 2.60
LINK CD CD A 102 SG CYS A 51 1555 1555 2.64
LINK CD CD A 102 SG CYS A 55 1555 1555 2.60
LINK CD CD A 103 SG CYS A 43 1555 1555 2.69
LINK CD CD A 103 SG CYS A 57 1555 1555 2.60
LINK CD CD A 103 SG CYS A 62 1555 1555 2.54
LINK CD CD A 103 SG CYS A 64 1555 1555 2.59
SITE 1 AC1 4 CYS A 45 CYS A 49 CYS A 51 CYS A 64
SITE 1 AC2 4 CYS A 38 CYS A 43 CYS A 51 CYS A 55
SITE 1 AC3 4 CYS A 43 CYS A 57 CYS A 62 CYS A 64
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 - 16 201 Bytes