Header list of 1b2t.pdb file
Complete list - b 16 2 Bytes
HEADER CHEMOKINE 01-DEC-98 1B2T TITLE SOLUTION STRUCTURE OF THE CX3C CHEMOKINE DOMAIN OF FRACTALKINE COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (FRACTALKINE); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CHEMOKINE DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: DISULFIDE BETWEEN 8 AND 34 AND 12 AND 50 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 8 EXPRESSION_SYSTEM_VARIANT: PLYSS; SOURCE 9 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM KEYWDS CHEMOKINE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.M.HANDEL,L.S.MIZOUE,J.F.BAZAN,E.C.JOHNSON REVDAT 5 16-FEB-22 1B2T 1 REMARK SEQADV REVDAT 4 24-FEB-09 1B2T 1 VERSN REVDAT 3 18-APR-01 1B2T 1 REVDAT SOURCE REMARK REVDAT 2 08-APR-99 1B2T 3 ATOM REVDAT 1 08-APR-99 1B2T 0 JRNL AUTH L.S.MIZOUE,J.F.BAZAN,E.C.JOHNSON,T.M.HANDEL JRNL TITL SOLUTION STRUCTURE AND DYNAMICS OF THE CX3C CHEMOKINE DOMAIN JRNL TITL 2 OF FRACTALKINE AND ITS INTERACTION WITH AN N-TERMINAL JRNL TITL 3 FRAGMENT OF CX3CR1. JRNL REF BIOCHEMISTRY V. 38 1402 1999 JRNL REFN ISSN 0006-2960 JRNL PMID 9931005 JRNL DOI 10.1021/BI9820614 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JOURNAL CITATION ABOVE REMARK 4 REMARK 4 1B2T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-DEC-98. REMARK 100 THE DEPOSITION ID IS D_1000000185. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 295.5 REMARK 210 PH : 5.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 15N-EDITED; 3D 13C-EDITED; 4D REMARK 210 13C/13C-EDITED NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : RESTRAINED MOLECULAR DYNAMICS REMARK 210 -SIMULATED ANNEALING COUPLED REMARK 210 WITH THE AMBIGUOUS RESTRAINTS REMARK 210 FOR ITERATIVE ASSIGNMENT (ARIA) REMARK 210 EXTENSION OF NILGES (M.NILGES, REMARK 210 J. MOL. BIOL. 245, 645-660, 1995) REMARK 210 . REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 70 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED PROTEIN. 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 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 HIS A 2 -53.63 -157.83 REMARK 500 1 VAL A 5 52.50 -117.62 REMARK 500 1 THR A 6 -163.59 -121.65 REMARK 500 1 LYS A 7 101.90 170.90 REMARK 500 1 CYS A 8 131.82 63.81 REMARK 500 1 GLN A 28 -169.12 -101.10 REMARK 500 1 CYS A 34 -79.85 -109.58 REMARK 500 1 ARG A 37 88.91 -64.18 REMARK 500 1 ALA A 38 -152.61 -126.94 REMARK 500 1 ALA A 71 169.57 -48.43 REMARK 500 1 LEU A 72 -77.33 58.49 REMARK 500 1 ARG A 74 47.69 -86.93 REMARK 500 2 GLN A 1 40.90 36.22 REMARK 500 2 HIS A 2 -63.39 -145.42 REMARK 500 2 HIS A 3 56.16 179.73 REMARK 500 2 VAL A 5 53.09 -113.53 REMARK 500 2 THR A 6 -162.40 -124.06 REMARK 500 2 LYS A 7 45.34 176.96 REMARK 500 2 THR A 16 -168.75 -110.95 REMARK 500 2 ALA A 32 81.67 -55.58 REMARK 500 2 SER A 33 -41.11 176.30 REMARK 500 2 ARG A 37 85.71 -66.23 REMARK 500 2 ALA A 38 -157.19 -124.23 REMARK 500 2 HIS A 46 35.96 86.21 REMARK 500 2 GLN A 68 -80.28 -162.52 REMARK 500 2 LEU A 72 -78.06 -113.49 REMARK 500 3 GLN A 1 -157.08 57.87 REMARK 500 3 HIS A 2 95.55 -43.68 REMARK 500 3 HIS A 3 -46.89 173.34 REMARK 500 3 ASN A 9 -34.26 -34.38 REMARK 500 3 GLN A 28 -166.61 -120.62 REMARK 500 3 ALA A 32 84.91 -67.15 REMARK 500 3 SER A 33 -35.08 -173.51 REMARK 500 3 ARG A 37 85.38 -69.83 REMARK 500 3 ALA A 38 -166.06 -114.20 REMARK 500 3 GLN A 68 -69.91 -127.13 REMARK 500 3 ALA A 71 -176.64 -48.48 REMARK 500 3 LEU A 72 -83.60 54.00 REMARK 500 3 ARG A 74 -90.26 -36.36 REMARK 500 4 VAL A 5 78.27 -109.87 REMARK 500 4 LYS A 7 91.69 67.60 REMARK 500 4 CYS A 8 110.96 72.24 REMARK 500 4 ASN A 9 -34.96 -34.24 REMARK 500 4 SER A 13 88.44 -59.22 REMARK 500 4 LYS A 14 150.35 85.70 REMARK 500 4 THR A 16 -168.06 -75.78 REMARK 500 4 ALA A 32 82.99 -65.45 REMARK 500 4 SER A 33 -24.77 163.64 REMARK 500 4 ALA A 38 -167.17 -113.24 REMARK 500 4 ARG A 67 46.15 -87.67 REMARK 500 REMARK 500 THIS ENTRY HAS 202 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1B2T A 1 76 UNP P78423 X3CL1_HUMAN 25 100 SEQADV 1B2T MET A 0 UNP P78423 CLONING ARTIFACT SEQRES 1 A 77 MET GLN HIS HIS GLY VAL THR LYS CYS ASN ILE THR CYS SEQRES 2 A 77 SER LYS MET THR SER LYS ILE PRO VAL ALA LEU LEU ILE SEQRES 3 A 77 HIS TYR GLN GLN ASN GLN ALA SER CYS GLY LYS ARG ALA SEQRES 4 A 77 ILE ILE LEU GLU THR ARG GLN HIS ARG LEU PHE CYS ALA SEQRES 5 A 77 ASP PRO LYS GLU GLN TRP VAL LYS ASP ALA MET GLN HIS SEQRES 6 A 77 LEU ASP ARG GLN ALA ALA ALA LEU THR ARG ASN GLY HELIX 1 H1 PRO A 20 LEU A 23 51 TURN OF 3/10 4 HELIX 2 H2 GLN A 56 ARG A 67 1 12 SHEET 1 S1 1 LEU A 24 GLN A 29 0 SHEET 1 S2 1 ILE A 39 THR A 43 0 SHEET 1 S3 1 LEU A 48 ALA A 51 0 SSBOND 1 CYS A 8 CYS A 34 1555 1555 2.03 SSBOND 2 CYS A 12 CYS A 50 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 - b 16 2 Bytes