Header list of 1qli.pdb file
Complete list - 2 202 Bytes
HEADER METAL BINDING PROTEIN 17-FEB-97 1QLI
TITLE QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, MINIMIZED AVERAGE
TITLE 2 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTEINE AND GLYCINE-RICH PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL LIM DOMAIN RESIDUES 82 - 194;
COMPND 5 SYNONYM: QCRP2(LIM2), ZN(II)-QCRP2(LIM2);
COMPND 6 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 CELL_LINE: BL21;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3D-QCRP2(LIM2)
KEYWDS LIM DOMAIN CONTAINING PROTEINS, METAL-BINDING PROTEIN, METAL BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
AUTHOR R.KONRAT,R.WEISKIRCHEN,B.KRAUTLER,K.BISTER
REVDAT 3 02-MAR-22 1QLI 1 KEYWDS REMARK LINK
REVDAT 2 24-FEB-09 1QLI 1 VERSN
REVDAT 1 20-AUG-97 1QLI 0
JRNL AUTH R.KONRAT,R.WEISKIRCHEN,B.KRAUTLER,K.BISTER
JRNL TITL SOLUTION STRUCTURE OF THE CARBOXYL-TERMINAL LIM DOMAIN FROM
JRNL TITL 2 QUAIL CYSTEINE-RICH PROTEIN CRP2.
JRNL REF J.BIOL.CHEM. V. 272 12001 1997
JRNL REFN ISSN 0021-9258
JRNL PMID 9115265
JRNL DOI 10.1074/JBC.272.18.12001
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 1QLI 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_1000175918.
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 : 3D 15N-NOESY-HSQC; 3D 15N-TOCSY
REMARK 210 -HSQC; 2D NOESY; 2D TOCSY; 2D X-
REMARK 210 FILTERED NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS 500
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DG/SA/EM
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 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 82
REMARK 465 ASP A 83
REMARK 465 ARG A 84
REMARK 465 GLY A 85
REMARK 465 GLU A 86
REMARK 465 ARG A 87
REMARK 465 LEU A 88
REMARK 465 GLY A 89
REMARK 465 ILE A 90
REMARK 465 LYS A 91
REMARK 465 PRO A 92
REMARK 465 GLU A 93
REMARK 465 SER A 94
REMARK 465 SER A 95
REMARK 465 PRO A 96
REMARK 465 SER A 97
REMARK 465 PRO A 98
REMARK 465 HIS A 99
REMARK 465 ARG A 100
REMARK 465 PRO A 101
REMARK 465 THR A 102
REMARK 465 THR A 103
REMARK 465 ASN A 104
REMARK 465 PRO A 105
REMARK 465 ASN A 106
REMARK 465 THR A 107
REMARK 465 SER A 108
REMARK 465 LYS A 109
REMARK 465 PHE A 110
REMARK 465 ALA A 111
REMARK 465 GLN A 112
REMARK 465 LYS A 113
REMARK 465 PHE A 114
REMARK 465 GLY A 115
REMARK 465 GLY A 116
REMARK 465 PHE A 176
REMARK 465 GLY A 177
REMARK 465 PRO A 178
REMARK 465 LYS A 179
REMARK 465 GLY A 180
REMARK 465 PHE A 181
REMARK 465 GLY A 182
REMARK 465 TYR A 183
REMARK 465 GLY A 184
REMARK 465 GLN A 185
REMARK 465 GLY A 186
REMARK 465 ALA A 187
REMARK 465 GLY A 188
REMARK 465 ALA A 189
REMARK 465 LEU A 190
REMARK 465 VAL A 191
REMARK 465 HIS A 192
REMARK 465 ALA A 193
REMARK 465 GLN A 194
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER A 121 CB SER A 121 OG 0.114
REMARK 500 SER A 126 CB SER A 126 OG 0.112
REMARK 500 HIS A 141 CG HIS A 141 CD2 0.058
REMARK 500 SER A 156 CB SER A 156 OG 0.113
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 ARG A 122 -62.40 -101.31
REMARK 500 TYR A 128 -25.35 -160.17
REMARK 500 ALA A 129 88.85 -163.23
REMARK 500 ALA A 130 -115.22 -160.87
REMARK 500 ASN A 143 -27.64 173.12
REMARK 500 SER A 156 155.24 76.22
REMARK 500 THR A 158 113.57 -172.90
REMARK 500 LEU A 159 -141.84 -168.09
REMARK 500 GLU A 165 -142.10 -135.00
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 196 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 120 SG
REMARK 620 2 CYS A 123 SG 107.6
REMARK 620 3 HIS A 141 ND1 108.9 108.7
REMARK 620 4 CYS A 144 SG 111.1 109.2 111.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 195 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 147 SG
REMARK 620 2 CYS A 150 SG 106.8
REMARK 620 3 CYS A 168 SG 108.3 111.1
REMARK 620 4 CYS A 171 SG 111.3 109.7 109.6
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZN1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: FIRST ZINC BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZN2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: SECOND ZINC BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 195
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 196
DBREF 1QLI A 82 194 UNP Q05158 CSRP2_COTJA 81 193
SEQRES 1 A 113 MET ASP ARG GLY GLU ARG LEU GLY ILE LYS PRO GLU SER
SEQRES 2 A 113 SER PRO SER PRO HIS ARG PRO THR THR ASN PRO ASN THR
SEQRES 3 A 113 SER LYS PHE ALA GLN LYS PHE GLY GLY ALA GLU LYS CYS
SEQRES 4 A 113 SER ARG CYS GLY ASP SER VAL TYR ALA ALA GLU LYS VAL
SEQRES 5 A 113 ILE GLY ALA GLY LYS PRO TRP HIS LYS ASN CYS PHE ARG
SEQRES 6 A 113 CYS ALA LYS CYS GLY LYS SER LEU GLU SER THR THR LEU
SEQRES 7 A 113 THR GLU LYS GLU GLY GLU ILE TYR CYS LYS GLY CYS TYR
SEQRES 8 A 113 ALA LYS ASN PHE GLY PRO LYS GLY PHE GLY TYR GLY GLN
SEQRES 9 A 113 GLY ALA GLY ALA LEU VAL HIS ALA GLN
HET ZN A 195 1
HET ZN A 196 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 GLY A 170 LYS A 174 1 5
SHEET 1 A 2 GLU A 118 CYS A 120 0
SHEET 2 A 2 GLY A 124 TYR A 128 -1
SHEET 1 B 2 LYS A 132 GLY A 135 0
SHEET 2 B 2 LYS A 138 LYS A 142 -1
SHEET 1 C 2 PHE A 145 CYS A 147 0
SHEET 2 C 2 LYS A 152 LEU A 154 -1
SHEET 1 D 2 THR A 160 LYS A 162 0
SHEET 2 D 2 GLU A 165 LYS A 169 -1
LINK SG CYS A 120 ZN ZN A 196 1555 1555 2.28
LINK SG CYS A 123 ZN ZN A 196 1555 1555 2.29
LINK ND1 HIS A 141 ZN ZN A 196 1555 1555 2.00
LINK SG CYS A 144 ZN ZN A 196 1555 1555 2.30
LINK SG CYS A 147 ZN ZN A 195 1555 1555 2.27
LINK SG CYS A 150 ZN ZN A 195 1555 1555 2.29
LINK SG CYS A 168 ZN ZN A 195 1555 1555 2.28
LINK SG CYS A 171 ZN ZN A 195 1555 1555 2.28
SITE 1 ZN1 4 CYS A 120 CYS A 123 HIS A 141 CYS A 144
SITE 1 ZN2 4 CYS A 147 CYS A 150 CYS A 168 CYS A 171
SITE 1 AC1 4 CYS A 147 CYS A 150 CYS A 168 CYS A 171
SITE 1 AC2 4 CYS A 120 CYS A 123 HIS A 141 CYS A 144
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 - 2 202 Bytes