Header list of 2sdf.pdb file
Complete list - r 16 2 Bytes
HEADER CYTOKINE 07-MAR-98 2SDF
TITLE SOLUTION NMR STRUCTURE OF STROMAL CELL-DERIVED FACTOR-1 (SDF-1), 30
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STROMAL CELL-DERIVED FACTOR-1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SDF;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS CYTOKINE, SDF-1, CHEMOKINES, STROMAL CELL-DERIVED FACTOR-1, G-COUPLED
KEYWDS 2 RECEPTORS, PROTEIN SYNTHESIS, SOLUTION STRUCTURE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR M.P.CRUMP,K.RAJARATHNAM,I.CLARK-LEWIS,B.D.SYKES
REVDAT 3 16-MAR-22 2SDF 1 REMARK
REVDAT 2 24-FEB-09 2SDF 1 VERSN
REVDAT 1 17-JUN-98 2SDF 0
JRNL AUTH M.P.CRUMP,J.H.GONG,P.LOETSCHER,K.RAJARATHNAM,A.AMARA,
JRNL AUTH 2 F.ARENZANA-SEISDEDOS,J.L.VIRELIZIER,M.BAGGIOLINI,B.D.SYKES,
JRNL AUTH 3 I.CLARK-LEWIS
JRNL TITL SOLUTION STRUCTURE AND BASIS FOR FUNCTIONAL ACTIVITY OF
JRNL TITL 2 STROMAL CELL-DERIVED FACTOR-1; DISSOCIATION OF CXCR4
JRNL TITL 3 ACTIVATION FROM BINDING AND INHIBITION OF HIV-1.
JRNL REF EMBO J. V. 16 6996 1997
JRNL REFN ISSN 0261-4189
JRNL PMID 9384579
JRNL DOI 10.1093/EMBOJ/16.23.6996
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: STRUCTURES WERE REFINED WITH MULTIPLE
REMARK 3 ROUNDS OF SIMULATED ANNEALING, WITH THE ADDITION OF NEW NOES AND
REMARK 3 CORRECTION OF AMBIGUOUS NOES. DETAILS OF THE NUMBER OF
REMARK 3 RESTRAINTS ETC. CAN BE FOUND IN THE JRNL CITATION ABOVE.
REMARK 4
REMARK 4 2SDF 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_1000178618.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 4.9
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; NOESY; TOCSY; 13C-HSQC;
REMARK 210 13C EDITED HMQC-NOESY; 15N-HSQC;
REMARK 210 3D 15N-EDITED NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : VARIAN INOVA; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : ENSEMBLE OF 30 STRUCTURES THAT
REMARK 210 SATISFIED THE NMR RESTRAINTS
REMARK 210 WITH NO NOE VIOLATIONS GREATER
REMARK 210 THAN 0.3 A AND NO DIHEDRAL ANGLE
REMARK 210 VIOLATIONS GREATER THAN 3
REMARK 210 DEGREES.
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: 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: 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 SER A 4 -176.75 -62.36
REMARK 500 1 LEU A 5 -174.69 -59.20
REMARK 500 1 SER A 6 -165.41 -58.21
REMARK 500 1 ARG A 8 -48.18 -152.97
REMARK 500 1 ARG A 12 -49.22 -140.41
REMARK 500 1 ASN A 30 53.21 -91.38
REMARK 500 1 LYS A 43 -74.27 -100.01
REMARK 500 1 ASN A 46 77.00 60.16
REMARK 500 1 ARG A 47 163.60 179.30
REMARK 500 1 LEU A 66 129.52 -177.87
REMARK 500 2 VAL A 3 -58.20 -128.90
REMARK 500 2 SER A 4 98.32 49.01
REMARK 500 2 ARG A 8 163.18 60.65
REMARK 500 2 ARG A 12 -48.19 -140.36
REMARK 500 2 ASN A 46 82.61 75.55
REMARK 500 2 ARG A 47 170.12 178.17
REMARK 500 3 SER A 6 154.31 61.31
REMARK 500 3 TYR A 7 170.42 179.82
REMARK 500 3 ARG A 8 -177.39 60.81
REMARK 500 3 ARG A 12 -49.32 -149.55
REMARK 500 3 GLU A 15 73.51 -100.08
REMARK 500 3 ASN A 46 83.33 70.76
REMARK 500 4 SER A 4 92.79 -179.37
REMARK 500 4 SER A 6 169.38 59.89
REMARK 500 4 ARG A 12 -50.11 -144.29
REMARK 500 4 ALA A 35 -74.72 -95.70
REMARK 500 4 LYS A 43 -64.96 -93.58
REMARK 500 4 ASN A 46 60.90 61.60
REMARK 500 5 SER A 4 -63.79 -132.03
REMARK 500 5 LEU A 5 76.02 -68.53
REMARK 500 5 SER A 6 164.02 60.32
REMARK 500 5 TYR A 7 -156.46 -74.72
REMARK 500 5 CYS A 9 161.43 -48.03
REMARK 500 5 ARG A 12 -49.33 -153.73
REMARK 500 5 SER A 16 84.74 -63.22
REMARK 500 5 HIS A 17 -34.33 178.79
REMARK 500 5 VAL A 18 152.93 -42.50
REMARK 500 5 LYS A 43 -60.31 -90.84
REMARK 500 5 LEU A 66 167.76 60.65
REMARK 500 6 VAL A 3 -64.71 -141.26
REMARK 500 6 SER A 4 101.38 -173.57
REMARK 500 6 SER A 6 -171.02 60.66
REMARK 500 6 ARG A 8 24.65 -145.72
REMARK 500 6 ALA A 35 -158.42 -75.91
REMARK 500 6 LEU A 66 130.17 66.76
REMARK 500 7 SER A 6 50.26 -91.62
REMARK 500 7 TYR A 7 175.57 56.56
REMARK 500 7 ARG A 8 138.78 63.40
REMARK 500 7 ARG A 12 -47.32 -139.56
REMARK 500 7 GLU A 15 72.25 -103.11
REMARK 500
REMARK 500 THIS ENTRY HAS 208 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 8 0.30 SIDE CHAIN
REMARK 500 1 ARG A 12 0.23 SIDE CHAIN
REMARK 500 1 ARG A 20 0.23 SIDE CHAIN
REMARK 500 1 ARG A 41 0.31 SIDE CHAIN
REMARK 500 1 ARG A 47 0.21 SIDE CHAIN
REMARK 500 2 ARG A 8 0.20 SIDE CHAIN
REMARK 500 2 ARG A 12 0.28 SIDE CHAIN
REMARK 500 2 ARG A 20 0.30 SIDE CHAIN
REMARK 500 2 ARG A 41 0.30 SIDE CHAIN
REMARK 500 2 ARG A 47 0.23 SIDE CHAIN
REMARK 500 3 ARG A 8 0.30 SIDE CHAIN
REMARK 500 3 ARG A 12 0.22 SIDE CHAIN
REMARK 500 3 ARG A 20 0.31 SIDE CHAIN
REMARK 500 3 ARG A 41 0.20 SIDE CHAIN
REMARK 500 3 ARG A 47 0.30 SIDE CHAIN
REMARK 500 4 ARG A 8 0.31 SIDE CHAIN
REMARK 500 4 ARG A 12 0.21 SIDE CHAIN
REMARK 500 4 ARG A 20 0.23 SIDE CHAIN
REMARK 500 4 ARG A 41 0.26 SIDE CHAIN
REMARK 500 4 ARG A 47 0.19 SIDE CHAIN
REMARK 500 5 ARG A 8 0.21 SIDE CHAIN
REMARK 500 5 ARG A 12 0.31 SIDE CHAIN
REMARK 500 5 ARG A 20 0.26 SIDE CHAIN
REMARK 500 5 ARG A 41 0.31 SIDE CHAIN
REMARK 500 5 ARG A 47 0.28 SIDE CHAIN
REMARK 500 6 ARG A 8 0.31 SIDE CHAIN
REMARK 500 6 ARG A 12 0.31 SIDE CHAIN
REMARK 500 6 ARG A 20 0.30 SIDE CHAIN
REMARK 500 6 ARG A 41 0.27 SIDE CHAIN
REMARK 500 6 ARG A 47 0.30 SIDE CHAIN
REMARK 500 7 ARG A 8 0.30 SIDE CHAIN
REMARK 500 7 ARG A 12 0.22 SIDE CHAIN
REMARK 500 7 ARG A 20 0.19 SIDE CHAIN
REMARK 500 7 ARG A 41 0.28 SIDE CHAIN
REMARK 500 7 ARG A 47 0.30 SIDE CHAIN
REMARK 500 8 ARG A 8 0.21 SIDE CHAIN
REMARK 500 8 ARG A 12 0.30 SIDE CHAIN
REMARK 500 8 ARG A 20 0.29 SIDE CHAIN
REMARK 500 8 ARG A 41 0.30 SIDE CHAIN
REMARK 500 8 ARG A 47 0.21 SIDE CHAIN
REMARK 500 9 ARG A 8 0.27 SIDE CHAIN
REMARK 500 9 ARG A 12 0.27 SIDE CHAIN
REMARK 500 9 ARG A 20 0.22 SIDE CHAIN
REMARK 500 9 ARG A 41 0.21 SIDE CHAIN
REMARK 500 9 ARG A 47 0.23 SIDE CHAIN
REMARK 500 10 ARG A 8 0.29 SIDE CHAIN
REMARK 500 10 ARG A 12 0.26 SIDE CHAIN
REMARK 500 10 ARG A 20 0.27 SIDE CHAIN
REMARK 500 10 ARG A 41 0.29 SIDE CHAIN
REMARK 500 10 ARG A 47 0.29 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 150 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2SDF A 1 67 UNP P48061 SDF1_HUMAN 22 88
SEQRES 1 A 67 LYS PRO VAL SER LEU SER TYR ARG CYS PRO CYS ARG PHE
SEQRES 2 A 67 PHE GLU SER HIS VAL ALA ARG ALA ASN VAL LYS HIS LEU
SEQRES 3 A 67 LYS ILE LEU ASN THR PRO ASN CYS ALA LEU GLN ILE VAL
SEQRES 4 A 67 ALA ARG LEU LYS ASN ASN ASN ARG GLN VAL CYS ILE ASP
SEQRES 5 A 67 PRO LYS LEU LYS TRP ILE GLN GLU TYR LEU GLU LYS ALA
SEQRES 6 A 67 LEU ASN
HELIX 1 1 ILE A 58 ALA A 65 1 8
SHEET 1 A 3 ARG A 47 CYS A 50 0
SHEET 2 A 3 GLN A 37 LEU A 42 -1 N LEU A 42 O ARG A 47
SHEET 3 A 3 VAL A 23 LEU A 29 -1 N LEU A 29 O GLN A 37
SSBOND 1 CYS A 9 CYS A 34 1555 1555 2.02
SSBOND 2 CYS A 11 CYS A 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 - r 16 2 Bytes