Header list of 1a7i.pdb file
Complete list - 16 202 Bytes
HEADER LIM DOMAIN CONTAINING PROTEINS 15-MAR-98 1A7I
TITLE AMINO-TERMINAL LIM DOMAIN FROM QUAIL CYSTEINE AND GLYCINE-RICH
TITLE 2 PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: QCRP2 (LIM1);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL LIM DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: COTURNIX JAPONICA;
SOURCE 3 ORGANISM_COMMON: JAPANESE QUAIL;
SOURCE 4 ORGANISM_TAXID: 93934;
SOURCE 5 GENE: CSRP2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS LIM DOMAIN CONTAINING PROTEINS, METAL-BINDING PROTEIN, ZINC FINGER
EXPDTA SOLUTION NMR
AUTHOR G.KONTAXIS,R.KONRAT,B.KRAEUTLER,R.WEISKIRCHEN,K.BISTER
REVDAT 3 16-FEB-22 1A7I 1 REMARK LINK
REVDAT 2 24-FEB-09 1A7I 1 VERSN
REVDAT 1 27-MAY-98 1A7I 0
JRNL AUTH G.KONTAXIS,R.KONRAT,B.KRAUTLER,R.WEISKIRCHEN,K.BISTER
JRNL TITL STRUCTURE AND INTRAMODULAR DYNAMICS OF THE AMINO-TERMINAL
JRNL TITL 2 LIM DOMAIN FROM QUAIL CYSTEINE- AND GLYCINE-RICH PROTEIN
JRNL TITL 3 CRP2.
JRNL REF BIOCHEMISTRY V. 37 7127 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9585524
JRNL DOI 10.1021/BI973055V
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.WEISKIRCHEN,K.BISTER
REMARK 1 TITL SUPPRESSION IN TRANSFORMED AVIAN FIBROBLASTS OF A GENE (CRP)
REMARK 1 TITL 2 ENCODING A CYSTEINE-RICH PROTEIN CONTAINING LIM DOMAINS
REMARK 1 REF GENE V. 8 2317 1993
REMARK 1 REFN ISSN 0378-1119
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 1A7I 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_1000170489.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 299
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; 2D X
REMARK 210 -FILTERED NOESY; 3D TOCSY-HSQC;
REMARK 210 3D NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR, NMRPIPE, ANSIG, X-PLOR
REMARK 210 METHOD USED : DG/SA/EM
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 15
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION,
REMARK 210 MINIMUM ENERGY
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 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 PRO A 2
REMARK 465 ASN A 3
REMARK 465 TRP A 4
REMARK 465 GLY A 5
REMARK 465 GLY A 6
REMARK 465 GLY A 7
REMARK 465 PRO A 68
REMARK 465 LYS A 69
REMARK 465 GLY A 70
REMARK 465 TYR A 71
REMARK 465 GLY A 72
REMARK 465 TYR A 73
REMARK 465 GLY A 74
REMARK 465 GLN A 75
REMARK 465 GLY A 76
REMARK 465 ALA A 77
REMARK 465 GLY A 78
REMARK 465 THR A 79
REMARK 465 LEU A 80
REMARK 465 ASN A 81
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS A 10 CA - CB - SG ANGL. DEV. = 8.9 DEGREES
REMARK 500 CYS A 13 CA - CB - SG ANGL. DEV. = 14.0 DEGREES
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 ALA A 12 -80.70 -89.68
REMARK 500 CYS A 13 -83.96 -64.44
REMARK 500 TYR A 18 -76.88 -149.71
REMARK 500 HIS A 19 -61.69 -138.36
REMARK 500 GLU A 21 40.46 -91.01
REMARK 500 ASP A 26 -112.42 69.83
REMARK 500 VAL A 39 -83.68 -89.88
REMARK 500 ARG A 41 59.81 87.64
REMARK 500 ASP A 45 -145.24 -167.42
REMARK 500 SER A 46 47.07 -95.22
REMARK 500 THR A 47 -83.57 -84.40
REMARK 500 THR A 48 -135.05 -130.35
REMARK 500 VAL A 49 160.30 162.64
REMARK 500 ASP A 53 -119.76 66.99
REMARK 500 CYS A 58 -148.90 -88.14
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 82 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 10 SG
REMARK 620 2 CYS A 13 SG 137.1
REMARK 620 3 HIS A 31 ND1 94.7 95.6
REMARK 620 4 CYS A 34 SG 102.5 95.7 140.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 83 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 37 SG
REMARK 620 2 CYS A 40 SG 100.5
REMARK 620 3 CYS A 58 SG 102.7 127.7
REMARK 620 4 CYS A 61 SG 137.9 94.4 98.6
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZF1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZF2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 82
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 83
DBREF 1A7I A 2 81 UNP Q05158 CSRP2_COTJA 1 80
SEQRES 1 A 81 MET PRO ASN TRP GLY GLY GLY ASN LYS CYS GLY ALA CYS
SEQRES 2 A 81 GLY ARG THR VAL TYR HIS ALA GLU GLU VAL GLN CYS ASP
SEQRES 3 A 81 GLY ARG SER PHE HIS ARG CYS CYS PHE LEU CYS MET VAL
SEQRES 4 A 81 CYS ARG LYS ASN LEU ASP SER THR THR VAL ALA ILE HIS
SEQRES 5 A 81 ASP ALA GLU VAL TYR CYS LYS SER CYS TYR GLY LYS LYS
SEQRES 6 A 81 TYR GLY PRO LYS GLY TYR GLY TYR GLY GLN GLY ALA GLY
SEQRES 7 A 81 THR LEU ASN
HET ZN A 82 1
HET ZN A 83 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 SER A 60 LYS A 65 1 6
SHEET 1 A 2 GLU A 22 CYS A 25 0
SHEET 2 A 2 ARG A 28 HIS A 31 -1 N PHE A 30 O VAL A 23
SHEET 1 B 2 ALA A 50 HIS A 52 0
SHEET 2 B 2 GLU A 55 TYR A 57 -1 N TYR A 57 O ALA A 50
LINK SG CYS A 10 ZN ZN A 82 1555 1555 2.25
LINK SG CYS A 13 ZN ZN A 82 1555 1555 2.25
LINK ND1 HIS A 31 ZN ZN A 82 1555 1555 2.06
LINK SG CYS A 34 ZN ZN A 82 1555 1555 2.35
LINK SG CYS A 37 ZN ZN A 83 1555 1555 2.36
LINK SG CYS A 40 ZN ZN A 83 1555 1555 2.22
LINK SG CYS A 58 ZN ZN A 83 1555 1555 2.25
LINK SG CYS A 61 ZN ZN A 83 1555 1555 2.34
SITE 1 ZF1 4 CYS A 10 CYS A 13 HIS A 31 CYS A 34
SITE 1 ZF2 4 CYS A 37 CYS A 40 CYS A 58 CYS A 61
SITE 1 AC1 4 CYS A 10 CYS A 13 HIS A 31 CYS A 34
SITE 1 AC2 4 CYS A 37 CYS A 40 CYS A 58 CYS A 61
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