Header list of 1b50.pdb file
Complete list - v 3 2 Bytes
HEADER CHEMOKINE 11-JAN-99 1B50
TITLE NMR STRUCTURE OF HUMAN MIP-1A D26A, 10 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MIP-1A;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS CHEMOKINE, CYTOKINE, CHEMOTAXIS
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR J.P.WALTHO,L.D.HIGGINS,C.J.CRAVEN,P.TAN,T.DUDGEON
REVDAT 5 03-NOV-21 1B50 1 SEQADV
REVDAT 4 22-FEB-12 1B50 1 JRNL VERSN
REVDAT 3 24-FEB-09 1B50 1 VERSN
REVDAT 2 01-APR-03 1B50 1 JRNL
REVDAT 1 22-JUL-99 1B50 0
JRNL AUTH L.G.CZAPLEWSKI,J.MCKEATING,C.J.CRAVEN,L.D.HIGGINS,V.APPAY,
JRNL AUTH 2 A.BROWN,T.DUDGEON,L.A.HOWARD,T.MEYERS,J.OWEN,S.R.PALAN,
JRNL AUTH 3 P.TAN,G.WILSON,N.R.WOODS,C.M.HEYWORTH,B.I.LORD,D.BROTHERTON,
JRNL AUTH 4 R.CHRISTISON,S.CRAIG,S.CRIBBES,R.M.EDWARDS,S.J.EVANS,
JRNL AUTH 5 R.GILBERT,P.MORGAN,E.RANDLE,N.SCHOFIELD,P.G.VARLEY,J.FISHER,
JRNL AUTH 6 J.P.WALTHO,M.G.HUNTER
JRNL TITL IDENTIFICATION OF AMINO ACID RESIDUES CRITICAL FOR
JRNL TITL 2 AGGREGATION OF HUMAN CC CHEMOKINES MACROPHAGE INFLAMMATORY
JRNL TITL 3 PROTEIN (MIP)-1ALPHA, MIP-1BETA, AND RANTES.
JRNL TITL 4 CHARACTERIZATION OF ACTIVE DISAGGREGATED CHEMOKINE VARIANTS.
JRNL REF J.BIOL.CHEM. V. 274 16077 1999
JRNL REFN ISSN 0021-9258
JRNL PMID 10347159
JRNL DOI 10.1074/JBC.274.23.16077
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE
REMARK 4
REMARK 4 1B50 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171481.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 318
REMARK 210 PH : 3.5
REMARK 210 IONIC STRENGTH : NO ADDED SALT
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 10% H2O/90% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : ST; ARD HETERONUCLEAR TECHNIQUES
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING STARTING
REMARK 210 FROM RANDOM ATOM POSITIONS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : CONVERGED LOW ENERGY 'PLATEAU'
REMARK 210 OF ENERGY DISTRIBUTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELLED MIP-1A. ADDITIONAL
REMARK 210 INTERMONOMER CONSTRAINTS WERE ACQUIRED USING A MIXED 13C/ 15N-
REMARK 210 12C/14N SAMPLE.
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 1 THR A 6 145.94 66.28
REMARK 500 1 PRO A 20 -177.69 -64.59
REMARK 500 1 ALA A 25 -50.33 -160.01
REMARK 500 1 ALA A 26 -162.22 -105.26
REMARK 500 1 TYR A 27 175.11 175.62
REMARK 500 1 GLU A 29 55.87 -100.78
REMARK 500 1 THR A 30 -140.55 59.05
REMARK 500 1 SER A 32 -169.39 -76.43
REMARK 500 1 GLN A 33 19.42 54.89
REMARK 500 1 CYS A 34 52.73 177.79
REMARK 500 1 SER A 35 93.15 -34.67
REMARK 500 1 THR A 43 -163.89 -54.97
REMARK 500 1 CYS A 50 173.79 58.75
REMARK 500 1 ASP A 52 170.90 -47.94
REMARK 500 1 GLN A 59 -36.51 -32.50
REMARK 500 1 ASP A 64 -77.15 -43.26
REMARK 500 1 LEU A 67 -52.81 83.36
REMARK 500 1 THR B 6 145.93 66.32
REMARK 500 1 PRO B 20 -177.73 -64.58
REMARK 500 1 ALA B 25 -50.45 -160.06
REMARK 500 1 ALA B 26 -162.27 -105.24
REMARK 500 1 TYR B 27 175.05 175.65
REMARK 500 1 GLU B 29 55.89 -100.80
REMARK 500 1 THR B 30 -140.53 59.02
REMARK 500 1 SER B 32 -169.40 -76.40
REMARK 500 1 GLN B 33 19.49 54.82
REMARK 500 1 CYS B 34 52.67 177.76
REMARK 500 1 SER B 35 93.14 -34.64
REMARK 500 1 THR B 43 -163.88 -55.03
REMARK 500 1 CYS B 50 173.83 58.73
REMARK 500 1 ASP B 52 170.99 -47.94
REMARK 500 1 GLN B 59 -36.44 -32.58
REMARK 500 1 ASP B 64 -77.15 -43.29
REMARK 500 1 LEU B 67 -52.80 83.29
REMARK 500 2 ALA A 3 -173.25 -69.73
REMARK 500 2 THR A 6 150.68 68.87
REMARK 500 2 ALA A 25 -66.05 -125.76
REMARK 500 2 ALA A 26 -161.86 -104.23
REMARK 500 2 TYR A 27 -105.18 -145.81
REMARK 500 2 PHE A 28 116.25 90.37
REMARK 500 2 SER A 31 -76.93 169.73
REMARK 500 2 GLN A 33 75.73 45.93
REMARK 500 2 CYS A 34 -169.56 161.86
REMARK 500 2 SER A 35 -93.63 -43.37
REMARK 500 2 LYS A 36 -44.32 118.78
REMARK 500 2 PRO A 37 43.10 -80.92
REMARK 500 2 THR A 43 164.64 -40.97
REMARK 500 2 SER A 46 36.05 77.95
REMARK 500 2 ASP A 52 158.07 -41.47
REMARK 500 2 SER A 54 29.63 81.85
REMARK 500
REMARK 500 THIS ENTRY HAS 456 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 17 0.28 SIDE CHAIN
REMARK 500 1 ARG A 45 0.15 SIDE CHAIN
REMARK 500 1 ARG A 47 0.09 SIDE CHAIN
REMARK 500 1 ARG B 17 0.28 SIDE CHAIN
REMARK 500 1 ARG B 45 0.14 SIDE CHAIN
REMARK 500 1 ARG B 47 0.09 SIDE CHAIN
REMARK 500 2 ARG A 17 0.19 SIDE CHAIN
REMARK 500 2 ARG A 45 0.28 SIDE CHAIN
REMARK 500 2 ARG A 47 0.26 SIDE CHAIN
REMARK 500 2 ARG B 17 0.19 SIDE CHAIN
REMARK 500 2 ARG B 45 0.28 SIDE CHAIN
REMARK 500 2 ARG B 47 0.26 SIDE CHAIN
REMARK 500 3 ARG A 17 0.31 SIDE CHAIN
REMARK 500 3 ARG A 45 0.29 SIDE CHAIN
REMARK 500 3 ARG A 47 0.18 SIDE CHAIN
REMARK 500 3 ARG B 17 0.30 SIDE CHAIN
REMARK 500 3 ARG B 45 0.29 SIDE CHAIN
REMARK 500 3 ARG B 47 0.18 SIDE CHAIN
REMARK 500 4 ARG A 17 0.32 SIDE CHAIN
REMARK 500 4 ARG A 45 0.25 SIDE CHAIN
REMARK 500 4 ARG A 47 0.30 SIDE CHAIN
REMARK 500 4 ARG B 17 0.32 SIDE CHAIN
REMARK 500 4 ARG B 45 0.25 SIDE CHAIN
REMARK 500 4 ARG B 47 0.30 SIDE CHAIN
REMARK 500 5 ARG A 17 0.28 SIDE CHAIN
REMARK 500 5 ARG A 45 0.30 SIDE CHAIN
REMARK 500 5 ARG A 47 0.27 SIDE CHAIN
REMARK 500 5 ARG B 17 0.28 SIDE CHAIN
REMARK 500 5 ARG B 45 0.30 SIDE CHAIN
REMARK 500 5 ARG B 47 0.27 SIDE CHAIN
REMARK 500 6 ARG A 17 0.20 SIDE CHAIN
REMARK 500 6 ARG A 45 0.28 SIDE CHAIN
REMARK 500 6 ARG A 47 0.26 SIDE CHAIN
REMARK 500 6 ARG B 17 0.20 SIDE CHAIN
REMARK 500 6 ARG B 45 0.28 SIDE CHAIN
REMARK 500 6 ARG B 47 0.26 SIDE CHAIN
REMARK 500 7 ARG A 17 0.25 SIDE CHAIN
REMARK 500 7 ARG A 45 0.32 SIDE CHAIN
REMARK 500 7 ARG A 47 0.18 SIDE CHAIN
REMARK 500 7 ARG B 17 0.25 SIDE CHAIN
REMARK 500 7 ARG B 45 0.32 SIDE CHAIN
REMARK 500 7 ARG B 47 0.18 SIDE CHAIN
REMARK 500 8 ARG A 17 0.13 SIDE CHAIN
REMARK 500 8 ARG A 45 0.11 SIDE CHAIN
REMARK 500 8 ARG A 47 0.31 SIDE CHAIN
REMARK 500 8 ARG B 17 0.13 SIDE CHAIN
REMARK 500 8 ARG B 45 0.11 SIDE CHAIN
REMARK 500 8 ARG B 47 0.31 SIDE CHAIN
REMARK 500 9 ARG A 17 0.23 SIDE CHAIN
REMARK 500 9 ARG A 45 0.20 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 60 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1B50 A 1 69 UNP P10147 CCL3_HUMAN 24 92
DBREF 1B50 B 1 69 UNP P10147 CCL3_HUMAN 24 92
SEQADV 1B50 ALA A 26 UNP P10147 ASP 49 ENGINEERED MUTATION
SEQADV 1B50 ALA B 26 UNP P10147 ASP 49 ENGINEERED MUTATION
SEQRES 1 A 69 SER LEU ALA ALA ASP THR PRO THR ALA CYS CYS PHE SER
SEQRES 2 A 69 TYR THR SER ARG GLN ILE PRO GLN ASN PHE ILE ALA ALA
SEQRES 3 A 69 TYR PHE GLU THR SER SER GLN CYS SER LYS PRO GLY VAL
SEQRES 4 A 69 ILE PHE LEU THR LYS ARG SER ARG GLN VAL CYS ALA ASP
SEQRES 5 A 69 PRO SER GLU GLU TRP VAL GLN LYS TYR VAL SER ASP LEU
SEQRES 6 A 69 GLU LEU SER ALA
SEQRES 1 B 69 SER LEU ALA ALA ASP THR PRO THR ALA CYS CYS PHE SER
SEQRES 2 B 69 TYR THR SER ARG GLN ILE PRO GLN ASN PHE ILE ALA ALA
SEQRES 3 B 69 TYR PHE GLU THR SER SER GLN CYS SER LYS PRO GLY VAL
SEQRES 4 B 69 ILE PHE LEU THR LYS ARG SER ARG GLN VAL CYS ALA ASP
SEQRES 5 B 69 PRO SER GLU GLU TRP VAL GLN LYS TYR VAL SER ASP LEU
SEQRES 6 B 69 GLU LEU SER ALA
HELIX 1 1 GLU A 56 TYR A 61 1 6
HELIX 2 2 GLU B 56 TYR B 61 1 6
SHEET 1 A 2 ALA A 26 PHE A 28 0
SHEET 2 A 2 ILE A 40 LEU A 42 -1 N LEU A 42 O ALA A 26
SHEET 1 B 2 ALA B 26 PHE B 28 0
SHEET 2 B 2 ILE B 40 LEU B 42 -1 N LEU B 42 O ALA B 26
SSBOND 1 CYS A 10 CYS A 34 1555 1555 2.02
SSBOND 2 CYS A 11 CYS A 50 1555 1555 2.02
SSBOND 3 CYS B 10 CYS B 34 1555 1555 2.02
SSBOND 4 CYS B 11 CYS B 50 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
MODEL 1
Complete list - v 3 2 Bytes