Header list of 1qnk.pdb file
Complete list - n 13 2 Bytes
HEADER CHEMOKINE 18-OCT-99 1QNK TITLE TRUNCATED HUMAN GROB[5-73], NMR, 20 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: C-X-C MOTIF CHEMOKINE 2; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: RESIDUES 5-73; COMPND 5 SYNONYM: GROWTH-REGULATED PROTEIN BETA,GRO-BETA,MACROPHAGE COMPND 6 INFLAMMATORY PROTEIN 2-ALPHA,MIP2-ALPHA; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 CELLULAR_LOCATION: BLOOD; SOURCE 6 GENE: CXCL2, GRO2, GROB, MIP2A, SCYB2; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: (LW 14) KEYWDS CHEMOKINE, CHEMOKINE 15-O, HUMAN CHEMOKINE GROB[5-73], CXC CHEMOKINE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR Y.Q.QIAN,K.JOHANSON,P.MCDEVITT REVDAT 3 13-JUN-18 1QNK 1 COMPND SOURCE AUTHOR JRNL REVDAT 3 2 1 DBREF REVDAT 2 24-FEB-09 1QNK 1 VERSN REVDAT 1 04-FEB-00 1QNK 0 JRNL AUTH Y.Q.QIAN,K.O.JOHANSON,P.MCDEVITT JRNL TITL NUCLEAR MAGNETIC RESONANCE SOLUTION STRUCTURE OF TRUNCATED JRNL TITL 2 HUMAN GROBETA [5-73] AND ITS STRUCTURAL COMPARISON WITH CXC JRNL TITL 3 CHEMOKINE FAMILY MEMBERS GROALPHA AND IL-8. JRNL REF J. MOL. BIOL. V. 294 1065 1999 JRNL REFN ISSN 0022-2836 JRNL PMID 10600366 JRNL DOI 10.1006/JMBI.1999.3333 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.KING,R.SCOTT,D.WU,J.STRICKLER,D.MCNULTY,M.SCOTT REMARK 1 TITL CHARACTERIZATION AND PURIFICATION OF A STROMAL CELL DERIVED REMARK 1 TITL 2 HEMATOPOIETIC SYNERGISTIC FACTOR INDUCED BY A NOVEL REMARK 1 TITL 3 HEMATOREGULATORY COMPOUND, SK&F 107647 REMARK 1 REF BLOOD V. 86 310A 1995 REMARK 1 REFN ISSN 0006-4971 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PROGRAM FOR NMR OR THEORETICAL MODELING MODELING REMARK 3 MODELING REMARK 3 AUTHORS : JONES,ZOU,COWAN,KJELDGAARD REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1QNK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-OCT-99. REMARK 100 THE DEPOSITION ID IS D_1290004297. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 5.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 90%H2O/10%D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 80 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: SEE JRNL ARTICLE FOR DETAILS THREE-DIMENSIONAL STRUCTURE REMARK 210 IN AQUEOUS SOLUTION REPRESENTED BY 20 CONFORMERS DETERMINED BY REMARK 210 NUCLEAR MAGNETIC RESONANCE, TORSION ANGLE DYNAMICS AND REMARK 210 RESTRAINED ENERGY REFINEMENT. DATA WERE COLLECTED AT 30 DEGREES REMARK 210 CELSIUS AND AT PH 5.5. THEY CONSIST OF 1878 UPPER LIMITS ON REMARK 210 DISTANCES OBTAINED FROM NOE MEASUREMENTS AND 314 ANGLE REMARK 210 CONSTRAINTS OBTAINED FROM NOE MEASUREMENTS AND COUPLING CONSTANT REMARK 210 MEASUREMENTS. THERE INPUT DATA ARE ALSO AVAILABLE FROM THE REMARK 210 PROTEIN DATA BANK. TORSION ANGLE DYNAMICS CALCULATIONS WERE REMARK 210 PERFORMED WITH THE PROGRAM DYANA (P.GUNTERT, C.MUMENTHALER, REMARK 210 K.WUTHRICH, J.MOL.BIOL. (1997) VOL. 273, 283-298). 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 H LEU A 44 O GLN A 48 1.48 REMARK 500 O VAL A 26 H VAL B 28 1.49 REMARK 500 H LEU B 44 O GLN B 48 1.50 REMARK 500 H VAL A 28 O VAL B 26 1.51 REMARK 500 O LYS B 27 H ILE B 41 1.59 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 ARG A 8 -144.23 -135.42 REMARK 500 1 GLN A 16 68.33 -102.55 REMARK 500 1 SER A 30 173.72 -48.29 REMARK 500 1 PRO A 54 48.49 -74.99 REMARK 500 1 ALA A 55 29.60 -164.49 REMARK 500 1 ASN A 69 -78.09 62.03 REMARK 500 1 SER A 72 88.16 -177.57 REMARK 500 1 ARG B 8 -145.57 -134.40 REMARK 500 1 SER B 30 173.51 -46.71 REMARK 500 1 ASN B 69 -78.33 61.67 REMARK 500 1 SER B 72 88.18 -170.65 REMARK 500 2 ARG A 8 -145.01 -135.11 REMARK 500 2 SER A 30 170.66 -45.44 REMARK 500 2 GLU A 39 83.04 -155.90 REMARK 500 2 ASN A 69 -78.62 61.60 REMARK 500 2 LYS A 71 -73.29 -79.25 REMARK 500 2 SER A 72 68.90 -170.13 REMARK 500 2 ARG B 8 -144.43 -136.06 REMARK 500 2 SER B 30 171.13 -56.01 REMARK 500 2 ASN B 69 -77.62 61.94 REMARK 500 2 SER B 72 -60.52 -176.10 REMARK 500 3 ARG A 8 -143.60 -135.81 REMARK 500 3 SER A 30 171.13 -47.32 REMARK 500 3 PRO A 54 48.17 -75.01 REMARK 500 3 ALA A 55 32.91 -169.93 REMARK 500 3 ASN A 69 -78.41 61.75 REMARK 500 3 LYS A 71 -86.59 -94.01 REMARK 500 3 SER A 72 108.33 79.94 REMARK 500 3 ARG B 8 -143.58 -135.36 REMARK 500 3 SER B 30 167.58 -48.84 REMARK 500 3 ASN B 69 -77.31 62.41 REMARK 500 3 LYS B 71 -173.37 -68.98 REMARK 500 3 SER B 72 -53.01 80.83 REMARK 500 4 GLU A 6 77.76 -114.97 REMARK 500 4 ARG A 8 -143.37 -135.70 REMARK 500 4 SER A 30 176.57 -48.17 REMARK 500 4 PRO A 54 45.84 -74.96 REMARK 500 4 ALA A 55 25.83 -158.97 REMARK 500 4 ASN A 69 -78.23 61.73 REMARK 500 4 SER A 72 -56.46 -175.62 REMARK 500 4 ARG B 8 -142.77 -135.69 REMARK 500 4 ASN B 69 -78.06 61.86 REMARK 500 4 LYS B 71 -68.08 -106.11 REMARK 500 4 SER B 72 103.38 -179.85 REMARK 500 5 ARG A 8 -144.78 -136.55 REMARK 500 5 ILE A 18 164.74 55.60 REMARK 500 5 SER A 30 174.84 -53.97 REMARK 500 5 GLU A 39 113.78 -168.91 REMARK 500 5 ASN A 69 -78.90 61.62 REMARK 500 5 LYS A 71 -68.37 -154.59 REMARK 500 REMARK 500 THIS ENTRY HAS 223 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED. REMARK 700 REMARK 700 SHEET REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED. DBREF 1QNK A 5 73 UNP P19875 CXCL2_HUMAN 39 107 DBREF 1QNK B 5 73 UNP P19875 CXCL2_HUMAN 39 107 SEQRES 1 A 69 THR GLU LEU ARG CYS GLN CYS LEU GLN THR LEU GLN GLY SEQRES 2 A 69 ILE HIS LEU LYS ASN ILE GLN SER VAL LYS VAL LYS SER SEQRES 3 A 69 PRO GLY PRO HIS CYS ALA GLN THR GLU VAL ILE ALA THR SEQRES 4 A 69 LEU LYS ASN GLY GLN LYS ALA CYS LEU ASN PRO ALA SER SEQRES 5 A 69 PRO MET VAL LYS LYS ILE ILE GLU LYS MET LEU LYS ASN SEQRES 6 A 69 GLY LYS SER ASN SEQRES 1 B 69 THR GLU LEU ARG CYS GLN CYS LEU GLN THR LEU GLN GLY SEQRES 2 B 69 ILE HIS LEU LYS ASN ILE GLN SER VAL LYS VAL LYS SER SEQRES 3 B 69 PRO GLY PRO HIS CYS ALA GLN THR GLU VAL ILE ALA THR SEQRES 4 B 69 LEU LYS ASN GLY GLN LYS ALA CYS LEU ASN PRO ALA SER SEQRES 5 B 69 PRO MET VAL LYS LYS ILE ILE GLU LYS MET LEU LYS ASN SEQRES 6 B 69 GLY LYS SER ASN HELIX 1 1 MET A 58 LYS A 68 1 11 HELIX 2 2 MET B 58 LYS B 68 1 11 SHEET 1 1 6 LYS A 49 LEU A 52 0 SHEET 2 1 6 GLU A 39 LEU A 44 -1 SHEET 3 1 6 SER A 25 LYS A 29 -1 SHEET 4 1 6 SER B 25 LYS B 29 -1 SHEET 5 1 6 GLU B 39 LEU B 44 -1 SHEET 6 1 6 LYS B 49 LEU B 52 -1 SSBOND 1 CYS A 9 CYS A 35 1555 1555 2.01 SSBOND 2 CYS A 11 CYS A 51 1555 1555 1.91 SSBOND 3 CYS B 9 CYS B 35 1555 1555 1.94 SSBOND 4 CYS B 11 CYS B 51 1555 1555 1.96 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 - n 13 2 Bytes