Header list of 1hum.pdb file
Complete list - 23 20 Bytes
HEADER CYTOKINE(CHEMOTACTIC) 31-JAN-94 1HUM
TITLE SOLUTION STRUCTURE OF THE CHEMOKINE HMIP-1BETA(SLASH)ACT-2 BY MULTI-
TITLE 2 DIMENSIONAL NMR: A NOVEL CHEMOKINE DIMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HUMAN MACROPHAGE INFLAMMATORY PROTEIN 1 BETA;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS CYTOKINE(CHEMOTACTIC)
EXPDTA SOLUTION NMR
AUTHOR G.M.CLORE,P.J.LODI,D.S.GARRETT,A.M.GRONENBORN
REVDAT 3 23-FEB-22 1HUM 1 REMARK
REVDAT 2 24-FEB-09 1HUM 1 VERSN
REVDAT 1 30-APR-94 1HUM 0
JRNL AUTH P.J.LODI,D.S.GARRETT,J.KUSZEWSKI,M.L.TSANG,J.A.WEATHERBEE,
JRNL AUTH 2 W.J.LEONARD,A.M.GRONENBORN,G.M.CLORE
JRNL TITL HIGH-RESOLUTION SOLUTION STRUCTURE OF THE BETA CHEMOKINE
JRNL TITL 2 HMIP-1 BETA BY MULTIDIMENSIONAL NMR.
JRNL REF SCIENCE V. 263 1762 1994
JRNL REFN ISSN 0036-8075
JRNL PMID 8134838
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 RESTRAINED MINIMIZED AVERAGE STRUCTURE OVER 35 FILES
REMARK 3 AVE.RMS DIFF. TO MEAN FOR BACKBONE
REMARK 3 (4-69)= 0.304637 ANGSTROMS
REMARK 3 AVE.RMS DIFF. TO MEAN FOR ALL ORDERED NON-H-ATOMS
REMARK 3 (4-69)= 0.45 ANGSTROMS
REMARK 3 AVE.RMS DIFF. TO MEAN FOR ALL NON-H-ATOMS
REMARK 3 (4-69)= 0.706906 ANGSTROMS
REMARK 3
REMARK 3 THE 3D STRUCTURE OF THE HMIP-1BETA DIMER IN SOLUTION BY NMR
REMARK 3 IS BASED ON 3586 EXPERIMENTAL RESTRAINTS COMPRISING: 3132
REMARK 3 STRUCTURE USEFUL INTERPROTON DISTANCE RESTRAINTS OF WHICH
REMARK 3 228 ARE INTERSUBUNIT; 24 RESTRAINTS FOR 12 H-BONDS
REMARK 3 INVOLVING TIGHTLY BOUND WATER MOLECULES; 108 RESTRAINTS FOR
REMARK 3 54 BACKBONE HYDROGEN BONDS INVOLVING SLOWLY EXCHANGING
REMARK 3 AMIDE PROTONS; 220 TORSION ANGLE RESTRAINTS (122 PHI, 10
REMARK 3 PSI, 80 CHI1 AND 8 CHI2); AND 102 HN-HALPHA THREE-BOND
REMARK 3 COUPLING CONSTANTS. A COMPLETE LIST OF EXPERIMENTAL
REMARK 3 RESTRAINTS AND 1H, 13C AND 15N ASSIGNMENTS ARE AVAILABLE
REMARK 3 FROM THE PROTEIN DATA BANK AS A SEPARATE ENTRY.
REMARK 3
REMARK 3 THE STRUCTURES ARE CALCULATED USING THE HYBRID METRIC
REMARK 3 MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING
REMARK 3 METHOD DESCRIBED BY: NILGES, M., CLORE, G.M. & GRONENBORN,
REMARK 3 A.M. (1988) FEBS LETT 229, 317-324. ALL STRUCTURAL
REMARK 3 STATISTICS ARE GIVEN IN THE REFERENCE.
REMARK 3
REMARK 3 THIS ENTRY CORRESPONDS TO THE RESTRAINED MINIMIZED
REMARK 3 AVERAGE STRUCTURE: (SA)R. THIS IS OBTAINED BY FIRST
REMARK 3 AVERAGING THE COORDINATES OF THE INDIVIDUAL 35 DYNAMICAL
REMARK 3 SIMULATED ANNEALING SA STRUCTURES BEST FITTED TO RESIDUES
REMARK 3 A 4 - A 69 (CHAIN A) AND B 4 - B 69 (CHAIN B), AND
REMARK 3 SUBJECTING THE RESULTING COORDINATES TO RESTRAINED
REMARK 3 MINIMIZATION.
REMARK 3
REMARK 3 THE FIELD THAT CONTAINS THE B VALUE IN X-RAY STRUCTURES
REMARK 3 (COLUMNS 61 - 66) GIVES THE AVERAGE RMS DIFFERENCE BETWEEN
REMARK 3 THE INDIVIDUAL SA STRUCTURES AND THE MEAN STRUCTURE.
REMARK 4
REMARK 4 1HUM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174031.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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: 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 ASP A 6 71.59 -159.73
REMARK 500 PRO A 8 -158.72 -62.06
REMARK 500 ALA A 10 82.32 -68.93
REMARK 500 SER A 14 -154.04 -156.20
REMARK 500 THR A 16 -156.89 -60.47
REMARK 500 PHE A 24 28.64 -140.45
REMARK 500 THR A 31 -167.60 -72.35
REMARK 500 SER A 32 -146.88 -83.64
REMARK 500 SER A 33 -34.80 -140.92
REMARK 500 SER A 36 30.63 -65.94
REMARK 500 GLN A 37 66.79 -153.23
REMARK 500 THR A 44 -158.75 -98.21
REMARK 500 SER A 47 -121.20 -167.55
REMARK 500 LYS A 48 -94.17 -158.33
REMARK 500 LEU A 68 -81.16 -78.26
REMARK 500 ASP B 6 71.60 -159.75
REMARK 500 PRO B 8 -158.68 -62.02
REMARK 500 ALA B 10 82.26 -68.87
REMARK 500 SER B 14 -154.07 -156.12
REMARK 500 THR B 16 -156.96 -60.40
REMARK 500 PHE B 24 28.71 -140.48
REMARK 500 THR B 31 -167.64 -72.30
REMARK 500 SER B 32 -146.85 -83.62
REMARK 500 SER B 33 -34.87 -140.94
REMARK 500 SER B 36 30.72 -66.12
REMARK 500 GLN B 37 66.76 -153.36
REMARK 500 THR B 44 -158.64 -98.22
REMARK 500 SER B 47 -121.18 -167.59
REMARK 500 LYS B 48 -94.14 -158.34
REMARK 500 LEU B 68 -81.16 -78.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HUN RELATED DB: PDB
DBREF 1HUM A 1 69 UNP P13236 CCL4_HUMAN 24 92
DBREF 1HUM B 1 69 UNP P13236 CCL4_HUMAN 24 92
SEQRES 1 A 69 ALA PRO MET GLY SER ASP PRO PRO THR ALA CYS CYS PHE
SEQRES 2 A 69 SER TYR THR ALA ARG LYS LEU PRO ARG ASN PHE VAL VAL
SEQRES 3 A 69 ASP TYR TYR GLU THR SER SER LEU CYS SER GLN PRO ALA
SEQRES 4 A 69 VAL VAL PHE GLN THR LYS ARG SER LYS GLN VAL CYS ALA
SEQRES 5 A 69 ASP PRO SER GLU SER TRP VAL GLN GLU TYR VAL TYR ASP
SEQRES 6 A 69 LEU GLU LEU ASN
SEQRES 1 B 69 ALA PRO MET GLY SER ASP PRO PRO THR ALA CYS CYS PHE
SEQRES 2 B 69 SER TYR THR ALA ARG LYS LEU PRO ARG ASN PHE VAL VAL
SEQRES 3 B 69 ASP TYR TYR GLU THR SER SER LEU CYS SER GLN PRO ALA
SEQRES 4 B 69 VAL VAL PHE GLN THR LYS ARG SER LYS GLN VAL CYS ALA
SEQRES 5 B 69 ASP PRO SER GLU SER TRP VAL GLN GLU TYR VAL TYR ASP
SEQRES 6 B 69 LEU GLU LEU ASN
FORMUL 3 HOH *4(H2 O)
HELIX 1 1 PRO A 21 VAL A 25 5 5
HELIX 2 2 GLU A 56 ASN A 69 1 14
HELIX 3 3 PRO B 21 VAL B 25 5 5
HELIX 4 4 GLU B 56 ASN B 69 1 14
SHEET 1 A 3 ASP A 27 GLU A 30 0
SHEET 2 A 3 VAL A 40 GLN A 43 -1 O VAL A 41 N TYR A 29
SHEET 3 A 3 GLN A 49 ALA A 52 -1 O VAL A 50 N PHE A 42
SHEET 1 B 3 ASP B 27 GLU B 30 0
SHEET 2 B 3 VAL B 40 GLN B 43 -1 O VAL B 41 N TYR B 29
SHEET 3 B 3 GLN B 49 ALA B 52 -1 O VAL B 50 N PHE B 42
SSBOND 1 CYS A 11 CYS A 35 1555 1555 2.02
SSBOND 2 CYS A 12 CYS A 51 1555 1555 2.02
SSBOND 3 CYS B 11 CYS B 35 1555 1555 2.02
SSBOND 4 CYS B 12 CYS B 51 1555 1555 2.02
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 - 23 20 Bytes