Header list of 1cxx.pdb file
Complete list - 3 202 Bytes
HEADER SIGNALING PROTEIN 31-AUG-99 1CXX TITLE MUTANT R122A OF QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, TITLE 2 MINIMIZED STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYSTEINE AND GLYCINE-RICH PROTEIN CRP2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CARBOXYL-TERMINAL LIM-DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: 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: FIBROBLAST; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET3D KEYWDS LIM DOMAIN CONTAINING PROTEINS, METAL-BINDING PROTEIN, SIGNALING KEYWDS 2 PROTEIN EXPDTA SOLUTION NMR AUTHOR K.KLOIBER,R.WEISKIRCHEN,B.KRAEUTLER,K.BISTER,R.KONRAT REVDAT 5 03-NOV-21 1CXX 1 REMARK SEQADV LINK REVDAT 4 24-FEB-09 1CXX 1 VERSN REVDAT 3 01-APR-03 1CXX 1 JRNL REVDAT 2 02-APR-00 1CXX 1 JRNL REVDAT 1 08-SEP-99 1CXX 0 JRNL AUTH K.KLOIBER,R.WEISKIRCHEN,B.KRAUTLER,K.BISTER,R.KONRAT JRNL TITL MUTATIONAL ANALYSIS AND NMR SPECTROSCOPY OF QUAIL CYSTEINE JRNL TITL 2 AND GLYCINE-RICH PROTEIN CRP2 REVEAL AN INTRINSIC SEGMENTAL JRNL TITL 3 FLEXIBILITY OF LIM DOMAINS. JRNL REF J.MOL.BIOL. V. 292 893 1999 JRNL REFN ISSN 0022-2836 JRNL PMID 10525413 JRNL DOI 10.1006/JMBI.1999.3118 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : ANSIG 3.3, X-PLOR 3.1 REMARK 3 AUTHORS : KRAULIS, P. J. (ANSIG), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON 340 NOE REMARK 3 -DERIVED DISTANCE RESTRAINTS AS WELL AS 16 DISTANCE RESTRAINTS REMARK 3 DERIVED FROM HYDROGEN BONDS REMARK 4 REMARK 4 1CXX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-SEP-99. REMARK 100 THE DEPOSITION ID IS D_1000009615. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 299 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.1MM QCRP2(LIM2)R122A 15N; 20MM REMARK 210 POTASSIUM PHOSPHATE; 50MM REMARK 210 POTASSIUM CHLORIDE; 0.5MM DTT; REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 3D-15N- REMARK 210 SEPARATED TOCSY; HNHA 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 : X-PLOR 3.1, NMRPIPE 1.7 REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR REMARK 210 DYNAMICS REFINEMENT, ENERGY REMARK 210 MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 11 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES REMARK 210 WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 15N-EDITED REMARK 210 SPECTRA AND HOMONUCLEAR 2D SPECTRA 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: 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 TYR A 128 -96.07 -79.05 REMARK 500 ALA A 129 -56.56 -171.90 REMARK 500 ALA A 130 69.76 -114.56 REMARK 500 GLU A 131 -62.58 -164.94 REMARK 500 ALA A 136 83.08 63.20 REMARK 500 LYS A 138 107.19 -54.11 REMARK 500 LYS A 149 -64.58 -98.08 REMARK 500 GLU A 155 88.35 -170.65 REMARK 500 LEU A 159 132.04 67.64 REMARK 500 GLU A 163 33.32 -92.02 REMARK 500 GLU A 165 -166.08 140.10 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 1 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 120 SG REMARK 620 2 CYS A 123 SG 107.4 REMARK 620 3 HIS A 141 ND1 107.1 107.6 REMARK 620 4 CYS A 144 SG 111.2 111.0 112.3 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 2 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 147 SG REMARK 620 2 CYS A 150 SG 108.6 REMARK 620 3 CYS A 168 SG 110.6 111.1 REMARK 620 4 CYS A 171 SG 111.9 109.1 105.5 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 ZN A 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1QLI RELATED DB: PDB REMARK 900 RELATED WILD-TYPE PEPTIDE: CARBOXYLTERMINAL LIM DOMAIN OF QCRP2 DBREF 1CXX A 82 194 UNP Q05158 CSRP2_COTJA 82 194 SEQADV 1CXX ALA A 122 UNP Q05158 ARG 122 ENGINEERED MUTATION 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 ALA 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 1 1 HET ZN A 2 1 HETNAM ZN ZINC ION FORMUL 2 ZN 2(ZN 2+) HELIX 1 1 CYS A 168 ASN A 175 1 8 SHEET 1 A 2 VAL A 133 ILE A 134 0 SHEET 2 A 2 PRO A 139 TRP A 140 -1 N TRP A 140 O VAL A 133 SHEET 1 B 2 GLU A 161 LYS A 162 0 SHEET 2 B 2 GLU A 165 ILE A 166 -1 O GLU A 165 N LYS A 162 LINK ZN ZN A 1 SG CYS A 120 1555 1555 2.29 LINK ZN ZN A 1 SG CYS A 123 1555 1555 2.30 LINK ZN ZN A 1 ND1 HIS A 141 1555 1555 2.01 LINK ZN ZN A 1 SG CYS A 144 1555 1555 2.30 LINK ZN ZN A 2 SG CYS A 147 1555 1555 2.30 LINK ZN ZN A 2 SG CYS A 150 1555 1555 2.30 LINK ZN ZN A 2 SG CYS A 168 1555 1555 2.30 LINK ZN ZN A 2 SG CYS A 171 1555 1555 2.29 SITE 1 AC1 4 CYS A 120 CYS A 123 HIS A 141 CYS A 144 SITE 1 AC2 4 CYS A 147 CYS A 150 CYS A 168 CYS A 171 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 - 3 202 Bytes