Header list of 1xj1.pdb file
Complete list - r 25 2 Bytes
HEADER VIRAL PROTEIN 22-SEP-04 1XJ1 TITLE 3D SOLUTION STRUCTURE OF THE C-TERMINAL CYSTEINE-RICH DOMAIN OF THE TITLE 2 VHV1.1 POLYDNAVIRAL GENE PRODUCT COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYSTEINE-RICH OMEGA-CONOTOXIN HOMOLOG VHV1.1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL CYS-MOTIF; COMPND 5 SYNONYM: VHV1.1 PROTEIN; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CAMPOLETIS SONORENSIS ICHNOVIRUS; SOURCE 3 ORGANISM_TAXID: 10484; SOURCE 4 GENE: PVX900; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-32B(+) KEYWDS POLYDNAVIRUS, CYSTINE KNOT, CYS-MOTIF, BETA-SHEET STRUCTURE, KEYWDS 2 DISULFIDE BONDING PATTERNS, VIRAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 25 AUTHOR J.EINERWOLD,J.JASEJA,K.HAPNER,B.WEBB,V.COPIE REVDAT 3 10-AUG-11 1XJ1 1 SOURCE VERSN REVDAT 2 24-FEB-09 1XJ1 1 VERSN REVDAT 1 05-OCT-04 1XJ1 0 JRNL AUTH J.EINERWOLD,J.JASEJA,K.HAPNER,B.WEBB,V.COPIE JRNL TITL SOLUTION STRUCTURE OF THE CARBOXYL-TERMINAL CYSTEINE-RICH JRNL TITL 2 DOMAIN OF THE VHV1.1 POLYDNAVIRAL GENE PRODUCT: COMPARISON JRNL TITL 3 WITH OTHER CYSTINE KNOT STRUCTURAL FOLDS JRNL REF BIOCHEMISTRY V. 40 14404 2001 JRNL REFN ISSN 0006-2960 JRNL PMID 11724552 JRNL DOI 10.1021/BI011499S REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.0 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 280 NOE- REMARK 3 DERIVED INTERPROTON DISTANCE CONSTRAINTS, 24 DISTANCE RESTRAINTS REMARK 3 FROM 12 HYDROGEN BONDS REMARK 4 REMARK 4 1XJ1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-SEP-04. REMARK 100 THE RCSB ID CODE IS RCSB030408. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 315; 310; 305 REMARK 210 PH : 5.7; 5.7; 5.0 REMARK 210 IONIC STRENGTH : 100MM NACL; 100MM NACL; 100MM REMARK 210 NACL REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 1MM C-TERM VHV1.1, 25MM SODIUM REMARK 210 PHOSPHATE, 100MM NACL, 1MM EDTA, REMARK 210 0.01% SODIUM AZIDE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 2.6, CNS 1.0 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS AND REMARK 210 SIMULATED ANNEALING PROTOCOLS REMARK 210 USING CNS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 25 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 17 REMARK 210 REMARK 210 REMARK: THIS ENSEMBLE OF NMR STRUCTURES WAS DETERMINED USING REMARK 210 STANDARD 2D 1H HOMONUCLEAR NMR TECHNIQUES 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 MODELS 1-25 REMARK 465 RES C SSSEQI REMARK 465 ALA A 1 REMARK 465 MET A 2 REMARK 465 VAL A 3 REMARK 465 SER A 4 REMARK 465 SER A 5 REMARK 465 GLY A 53 REMARK 465 VAL A 54 REMARK 465 ARG A 55 REMARK 465 GLY A 56 REMARK 465 LEU A 57 REMARK 465 PRO A 58 REMARK 465 ASN A 59 REMARK 465 GLY A 60 REMARK 465 ALA A 61 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 ASN A 16 29.74 -147.78 REMARK 500 1 ALA A 17 -170.22 -177.33 REMARK 500 1 ASP A 18 -77.52 -71.21 REMARK 500 1 LYS A 19 52.93 -170.73 REMARK 500 1 CYS A 22 -175.50 -67.14 REMARK 500 1 TYR A 28 -46.03 -174.02 REMARK 500 1 ASP A 51 164.71 59.62 REMARK 500 2 ASP A 18 -166.47 -107.08 REMARK 500 2 LYS A 19 132.87 64.21 REMARK 500 2 VAL A 26 41.44 -95.93 REMARK 500 2 ARG A 27 -176.10 55.91 REMARK 500 2 ASP A 30 -61.97 -135.45 REMARK 500 2 ASP A 51 -177.47 61.08 REMARK 500 3 TYR A 11 68.20 61.40 REMARK 500 3 ASP A 18 -170.43 -56.92 REMARK 500 3 CYS A 22 -178.48 -69.69 REMARK 500 3 TYR A 28 -51.25 -134.45 REMARK 500 3 SER A 31 81.23 -66.35 REMARK 500 3 ASP A 42 37.40 -99.16 REMARK 500 3 GLU A 44 -59.09 -146.93 REMARK 500 3 ASP A 51 105.82 60.82 REMARK 500 4 TYR A 28 31.65 -163.88 REMARK 500 4 ASP A 30 -169.56 -67.06 REMARK 500 4 SER A 31 170.75 60.68 REMARK 500 4 LYS A 32 80.81 -155.25 REMARK 500 4 ASP A 51 106.11 58.61 REMARK 500 5 HIS A 10 140.29 -179.03 REMARK 500 5 TYR A 11 79.27 63.60 REMARK 500 5 VAL A 26 76.71 -178.67 REMARK 500 5 PHE A 37 114.18 -160.06 REMARK 500 5 GLU A 44 27.77 -141.04 REMARK 500 5 ASP A 51 104.71 59.96 REMARK 500 6 TYR A 11 62.89 61.09 REMARK 500 6 CYS A 22 -178.17 -60.05 REMARK 500 6 VAL A 26 53.15 -93.88 REMARK 500 6 ARG A 27 161.36 61.20 REMARK 500 6 SER A 31 36.01 -172.76 REMARK 500 6 ASP A 42 39.50 -97.12 REMARK 500 6 GLU A 44 -63.90 -124.93 REMARK 500 6 ASP A 51 106.48 58.54 REMARK 500 7 CYS A 7 129.35 -179.16 REMARK 500 7 HIS A 10 137.88 -171.38 REMARK 500 7 VAL A 15 49.66 -90.20 REMARK 500 7 ASN A 16 -39.84 -178.66 REMARK 500 7 ASP A 18 41.95 -147.42 REMARK 500 7 ARG A 27 43.87 -100.04 REMARK 500 7 ASP A 42 37.03 -98.16 REMARK 500 7 PHE A 50 -167.27 -160.09 REMARK 500 7 ASP A 51 95.70 -169.59 REMARK 500 8 CYS A 7 120.84 62.84 REMARK 500 REMARK 500 THIS ENTRY HAS 160 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1X17 RELATED DB: PDB REMARK 900 ENERGY-MINIMIZED NMR AVERAGE STRUCTURE OBTAINED FROM THE REMARK 900 ENSEMBLE OF 25 DBREF 1XJ1 A 3 61 UNP Q89632 Q89632_CSV 159 217 SEQADV 1XJ1 ALA A 1 UNP Q89632 CLONING ARTIFACT SEQADV 1XJ1 MET A 2 UNP Q89632 CLONING ARTIFACT SEQRES 1 A 61 ALA MET VAL SER SER THR CYS ILE GLY HIS TYR GLN LYS SEQRES 2 A 61 CYS VAL ASN ALA ASP LYS PRO CYS CYS SER LYS THR VAL SEQRES 3 A 61 ARG TYR GLY ASP SER LYS ASN VAL ARG LYS PHE ILE CYS SEQRES 4 A 61 ASP ARG ASP GLY GLU GLY VAL CYS VAL PRO PHE ASP GLY SEQRES 5 A 61 GLY VAL ARG GLY LEU PRO ASN GLY ALA SHEET 1 A 4 GLN A 12 LYS A 13 0 SHEET 2 A 4 VAL A 46 PHE A 50 -1 O CYS A 47 N GLN A 12 SHEET 3 A 4 ASN A 33 ASP A 40 -1 N LYS A 36 O PHE A 50 SHEET 4 A 4 LYS A 24 VAL A 26 -1 N LYS A 24 O ARG A 35 SSBOND 1 CYS A 7 CYS A 22 1555 1555 2.03 SSBOND 2 CYS A 14 CYS A 39 1555 1555 2.03 SSBOND 3 CYS A 21 CYS A 47 1555 1555 2.03 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 - r 25 2 Bytes