Header list of 2vgh.pdb file
Complete list - 16 202 Bytes
HEADER GROWTH FACTOR 17-DEC-97 2VGH
TITLE HEPARIN-BINDING DOMAIN FROM VASCULAR ENDOTHELIAL GROWTH FACTOR, NMR,
TITLE 2 MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VASCULAR ENDOTHELIAL GROWTH FACTOR-165;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HEPARIN-BINDING DOMAIN;
COMPND 5 SYNONYM: VEGF-165;
COMPND 6 ENGINEERED: 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: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GROWTH FACTOR, HEPARIN-BINDING, ANGIOGENESIS
EXPDTA SOLUTION NMR
AUTHOR W.J.FAIRBROTHER,M.A.CHAMPE,H.W.CHRISTINGER,B.A.KEYT,M.A.STAROVASNIK
REVDAT 3 16-MAR-22 2VGH 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2VGH 1 VERSN
REVDAT 1 08-APR-98 2VGH 0
JRNL AUTH W.J.FAIRBROTHER,M.A.CHAMPE,H.W.CHRISTINGER,B.A.KEYT,
JRNL AUTH 2 M.A.STAROVASNIK
JRNL TITL SOLUTION STRUCTURE OF THE HEPARIN-BINDING DOMAIN OF VASCULAR
JRNL TITL 2 ENDOTHELIAL GROWTH FACTOR.
JRNL REF STRUCTURE V. 6 637 1998
JRNL REFN ISSN 0969-2126
JRNL PMID 9634701
JRNL DOI 10.1016/S0969-2126(98)00065-3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISCOVER
REMARK 3 AUTHORS : MOLECULAR SIMULATIONS INC.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 2VGH 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_1000178731.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2QF-COSY; TOCSY (70 AND 100 MS);
REMARK 210 NOESY(50; AND 200 MS); 15N-HSQC;
REMARK 210 15N-TOCSY-HSQC(30 AND 70 MS);
REMARK 210 15N-NOESY-HSQC(120 MS); 15N-
REMARK 210 ROESY-HSQC(40 MS); HNHA; HNHB
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 : DGII, DISCOVER
REMARK 210 METHOD USED : DISTANCE GEOMETRY/ SIMULATED
REMARK 210 ANNEALING/RESTRAINED MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMIZED MEAN STRUCTURE
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 ARG A 2 141.98 76.01
REMARK 500 GLU A 4 178.51 64.55
REMARK 500 ASN A 5 84.58 -150.50
REMARK 500 GLU A 12 -78.01 -61.24
REMARK 500 ARG A 13 -59.87 -137.08
REMARK 500 LYS A 15 41.80 -84.08
REMARK 500 LEU A 17 40.98 -94.91
REMARK 500 PRO A 22 44.80 -83.35
REMARK 500 GLN A 23 -54.66 -143.19
REMARK 500 PRO A 53 -73.45 -67.77
REMARK 500 ARG A 54 67.38 -154.04
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2VGH A 1 55 UNP P15692 VEGFA_HUMAN 137 215
SEQADV 2VGH A UNP P15692 LYS 141 DELETION
SEQADV 2VGH A UNP P15692 LYS 142 DELETION
SEQADV 2VGH A UNP P15692 SER 143 DELETION
SEQADV 2VGH A UNP P15692 VAL 144 DELETION
SEQADV 2VGH A UNP P15692 ARG 145 DELETION
SEQADV 2VGH A UNP P15692 GLY 146 DELETION
SEQADV 2VGH A UNP P15692 LYS 147 DELETION
SEQADV 2VGH A UNP P15692 GLY 148 DELETION
SEQADV 2VGH A UNP P15692 LYS 149 DELETION
SEQADV 2VGH A UNP P15692 GLY 150 DELETION
SEQADV 2VGH A UNP P15692 GLN 151 DELETION
SEQADV 2VGH A UNP P15692 LYS 152 DELETION
SEQADV 2VGH A UNP P15692 ARG 153 DELETION
SEQADV 2VGH A UNP P15692 LYS 154 DELETION
SEQADV 2VGH A UNP P15692 ARG 155 DELETION
SEQADV 2VGH A UNP P15692 LYS 156 DELETION
SEQADV 2VGH A UNP P15692 LYS 157 DELETION
SEQADV 2VGH A UNP P15692 SER 158 DELETION
SEQADV 2VGH A UNP P15692 ARG 159 DELETION
SEQADV 2VGH A UNP P15692 TYR 160 DELETION
SEQADV 2VGH A UNP P15692 LYS 161 DELETION
SEQADV 2VGH A UNP P15692 SER 162 DELETION
SEQADV 2VGH A UNP P15692 TRP 163 DELETION
SEQADV 2VGH A UNP P15692 SER 164 DELETION
SEQADV 2VGH ASN A 5 UNP P15692 VAL 165 VARIANT
SEQRES 1 A 55 ALA ARG GLN GLU ASN PRO CYS GLY PRO CYS SER GLU ARG
SEQRES 2 A 55 ARG LYS HIS LEU PHE VAL GLN ASP PRO GLN THR CYS LYS
SEQRES 3 A 55 CYS SER CYS LYS ASN THR ASP SER ARG CYS LYS ALA ARG
SEQRES 4 A 55 GLN LEU GLU LEU ASN GLU ARG THR CYS ARG CYS ASP LYS
SEQRES 5 A 55 PRO ARG ARG
HELIX 1 1 ASP A 33 ALA A 38 1 6
SHEET 1 A 2 PHE A 18 GLN A 20 0
SHEET 2 A 2 CYS A 27 CYS A 29 -1 N SER A 28 O VAL A 19
SHEET 1 B 2 GLU A 42 ASN A 44 0
SHEET 2 B 2 ARG A 49 ASP A 51 -1 N ASP A 51 O GLU A 42
SSBOND 1 CYS A 7 CYS A 25 1555 1555 2.05
SSBOND 2 CYS A 10 CYS A 27 1555 1555 2.05
SSBOND 3 CYS A 29 CYS A 48 1555 1555 2.04
SSBOND 4 CYS A 36 CYS A 50 1555 1555 2.05
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 - 16 202 Bytes