Header list of 1nyp.pdb file
Complete list - b 23 2 Bytes
HEADER CELL ADHESION 13-FEB-03 1NYP TITLE 4TH LIM DOMAIN OF PINCH PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: PINCH PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: 4TH LIM DOMAIN; COMPND 5 SYNONYM: LIM AND SENESCENT CELL ANTIGEN-LIKE DOMAINS 1; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: LIMS1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-4T1 KEYWDS LIM DOMAIN, PROTEIN RECOGNITION, CELL ADHESION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR A.VELYVIS,J.VAYNBERG,O.VINOGRADOVA,Y.ZHANG,C.WU,J.QIN REVDAT 3 23-FEB-22 1NYP 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 1NYP 1 VERSN REVDAT 1 01-JUL-03 1NYP 0 JRNL AUTH A.VELYVIS,J.VAYNBERG,Y.YANG,O.VINOGRADOVA,Y.ZHANG,C.WU,J.QIN JRNL TITL STRUCTURAL AND FUNCTIONAL INSIGHTS INTO PINCH LIM4 JRNL TITL 2 DOMAIN-MEDIATED INTEGRIN SIGNALING JRNL REF NAT.STRUCT.BIOL. V. 10 558 2003 JRNL REFN ISSN 1072-8368 JRNL PMID 12794636 JRNL DOI 10.1038/NSB938 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE, X-PLOR REMARK 3 AUTHORS : BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 SA PROTOCOL WITHOUT ZN COFACTORS STARTING FROM LINEAR PROTEIN REMARK 3 STRUCTURE, REMARK 3 FOLLOWED BY ADDITION OF ZN INTO STRUCTURES AND MINIMIZATION REMARK 4 REMARK 4 1NYP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-FEB-03. REMARK 100 THE DEPOSITION ID IS D_1000018358. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 0.13 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.7 MM U-15N,13C-LIM4; 95% H2O, REMARK 210 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D-15N,13C-EDITED-NOESY 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 : PIPP, X-PLOR REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 60 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 THR A 57 H GLN A 61 1.44 REMARK 500 O GLU A 56 HD21 ASN A 60 1.50 REMARK 500 H ALA A 35 O ALA A 53 1.54 REMARK 500 O PRO A 6 H ILE A 15 1.60 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 1 MET A 3 167.87 -49.80 REMARK 500 1 GLU A 16 61.47 -160.54 REMARK 500 1 MET A 23 17.19 58.09 REMARK 500 1 LYS A 25 -154.80 -130.23 REMARK 500 1 LYS A 36 -31.69 -138.81 REMARK 500 1 GLU A 38 47.60 71.70 REMARK 500 1 PHE A 41 56.90 -95.78 REMARK 500 1 CYS A 55 177.47 -57.55 REMARK 500 1 PHE A 63 -81.64 -158.58 REMARK 500 2 VAL A 5 117.70 57.16 REMARK 500 2 GLU A 16 62.84 -161.77 REMARK 500 2 MET A 23 16.01 58.38 REMARK 500 2 LYS A 25 -151.11 -133.05 REMARK 500 2 ALA A 35 35.11 -92.46 REMARK 500 2 LYS A 36 -40.23 -142.99 REMARK 500 2 GLU A 38 47.89 75.10 REMARK 500 2 PHE A 41 57.82 -96.21 REMARK 500 2 CYS A 55 175.80 -57.28 REMARK 500 2 PHE A 63 -81.54 -158.49 REMARK 500 2 ASP A 65 80.97 55.92 REMARK 500 3 MET A 3 -167.53 -163.93 REMARK 500 3 GLU A 16 62.02 -159.59 REMARK 500 3 MET A 23 16.96 57.52 REMARK 500 3 LYS A 25 -155.37 -125.38 REMARK 500 3 LYS A 36 -32.03 -138.70 REMARK 500 3 PHE A 41 56.44 -95.78 REMARK 500 3 CYS A 55 178.15 -57.81 REMARK 500 3 PHE A 63 -81.93 -160.13 REMARK 500 3 ASP A 65 25.27 -172.55 REMARK 500 4 SER A 2 43.49 -166.43 REMARK 500 4 MET A 3 -128.48 50.62 REMARK 500 4 VAL A 5 129.27 57.13 REMARK 500 4 GLU A 16 62.12 -159.19 REMARK 500 4 MET A 23 18.14 58.10 REMARK 500 4 LYS A 25 -154.67 -130.32 REMARK 500 4 LYS A 36 -39.07 -134.10 REMARK 500 4 GLU A 38 46.94 73.70 REMARK 500 4 LYS A 50 20.94 44.73 REMARK 500 4 CYS A 55 172.03 -56.57 REMARK 500 4 PHE A 63 -83.88 -156.11 REMARK 500 4 ASP A 65 81.46 56.38 REMARK 500 5 SER A 2 -120.49 -165.90 REMARK 500 5 MET A 3 98.56 51.63 REMARK 500 5 VAL A 5 116.19 56.67 REMARK 500 5 GLU A 16 62.41 -161.26 REMARK 500 5 MET A 23 14.46 58.31 REMARK 500 5 LYS A 25 -154.83 -120.21 REMARK 500 5 LYS A 36 -33.21 -138.09 REMARK 500 5 PHE A 41 56.35 -96.08 REMARK 500 5 LYS A 50 21.66 42.33 REMARK 500 REMARK 500 THIS ENTRY HAS 211 RAMACHANDRAN OUTLIERS. 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 67 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 8 SG REMARK 620 2 CYS A 11 SG 109.6 REMARK 620 3 HIS A 28 ND1 104.8 108.0 REMARK 620 4 HIS A 31 ND1 123.1 106.4 104.1 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 68 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 34 SG REMARK 620 2 CYS A 37 SG 104.5 REMARK 620 3 CYS A 55 SG 117.0 92.2 REMARK 620 4 HIS A 58 ND1 117.7 97.0 119.8 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 67 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 68 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1G47 RELATED DB: PDB REMARK 900 ANOTHER LIM DOMAIN FROM THE SAME MULTI-DOMAIN ADAPTOR PROTEIN DBREF 1NYP A 3 66 UNP P48059 PINC_HUMAN 188 251 SEQADV 1NYP GLY A 1 UNP P48059 CLONING ARTIFACT SEQADV 1NYP SER A 2 UNP P48059 CLONING ARTIFACT SEQRES 1 A 66 GLY SER MET GLY VAL PRO ILE CYS GLY ALA CYS ARG ARG SEQRES 2 A 66 PRO ILE GLU GLY ARG VAL VAL ASN ALA MET GLY LYS GLN SEQRES 3 A 66 TRP HIS VAL GLU HIS PHE VAL CYS ALA LYS CYS GLU LYS SEQRES 4 A 66 PRO PHE LEU GLY HIS ARG HIS TYR GLU ARG LYS GLY LEU SEQRES 5 A 66 ALA TYR CYS GLU THR HIS TYR ASN GLN LEU PHE GLY ASP SEQRES 6 A 66 VAL HET ZN A 67 1 HET ZN A 68 1 HETNAM ZN ZINC ION FORMUL 2 ZN 2(ZN 2+) HELIX 1 1 CYS A 55 PHE A 63 1 9 SHEET 1 A 2 ILE A 7 CYS A 8 0 SHEET 2 A 2 ARG A 13 PRO A 14 -1 O ARG A 13 N CYS A 8 SHEET 1 B 2 VAL A 19 VAL A 20 0 SHEET 2 B 2 TRP A 27 HIS A 28 -1 O TRP A 27 N VAL A 20 SHEET 1 C 2 TYR A 47 ARG A 49 0 SHEET 2 C 2 LEU A 52 TYR A 54 -1 O TYR A 54 N TYR A 47 LINK SG CYS A 8 ZN ZN A 67 1555 1555 2.30 LINK SG CYS A 11 ZN ZN A 67 1555 1555 2.30 LINK ND1 HIS A 28 ZN ZN A 67 1555 1555 2.00 LINK ND1 HIS A 31 ZN ZN A 67 1555 1555 2.00 LINK SG CYS A 34 ZN ZN A 68 1555 1555 2.30 LINK SG CYS A 37 ZN ZN A 68 1555 1555 2.30 LINK SG CYS A 55 ZN ZN A 68 1555 1555 2.30 LINK ND1 HIS A 58 ZN ZN A 68 1555 1555 2.00 SITE 1 AC1 4 CYS A 8 CYS A 11 HIS A 28 HIS A 31 SITE 1 AC2 4 CYS A 34 CYS A 37 CYS A 55 HIS A 58 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 MODEL 1
Complete list - b 23 2 Bytes