Header list of 1kmx.pdb file
Complete list - b 23 2 Bytes
HEADER HORMONE/GROWTH FACTOR 17-DEC-01 1KMX
TITLE HEPARIN-BINDING DOMAIN FROM VASCULAR ENDOTHELIAL GROWTH FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VASCULAR ENDOTHELIAL GROWTH FACTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HEPARIN-BINDING DOMAIN;
COMPND 5 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 HEPARIN-BINDING, ANGIOGENESIS, GROWTH FACTOR, HORMONE-GROWTH FACTOR
KEYWDS 2 COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.E.STAUFFER,N.J.SKELTON,W.J.FAIRBROTHER
REVDAT 3 23-FEB-22 1KMX 1 REMARK
REVDAT 2 24-FEB-09 1KMX 1 VERSN
REVDAT 1 24-JUL-02 1KMX 0
JRNL AUTH M.E.STAUFFER,N.J.SKELTON,W.J.FAIRBROTHER
JRNL TITL REFINEMENT OF THE SOLUTION STRUCTURE OF THE HEPARIN-BINDING
JRNL TITL 2 DOMAIN OF VASCULAR ENDOTHELIAL GROWTH FACTOR USING RESIDUAL
JRNL TITL 3 DIPOLAR COUPLINGS
JRNL REF J.BIOMOL.NMR V. 23 57 2002
JRNL REFN ISSN 0925-2738
JRNL PMID 12061718
JRNL DOI 10.1023/A:1015346504499
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.J.FAIRBROTHER,M.A.CHAMPE,H.W.CHRISTINGER,B.A.KEYT,
REMARK 1 AUTH 2 M.A.STAROVASNIK
REMARK 1 TITL SOLUTION STRUCTURE OF THE HEPARIN-BINDING DOMAIN OF VASCULAR
REMARK 1 TITL 2 ENDOTHELIAL GROWTH FACTOR
REMARK 1 REF STRUCTURE V. 6 637 1998
REMARK 1 REFN ISSN 0969-2126
REMARK 1 DOI 10.1016/S0969-2126(98)00065-3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : UXNMR, CNX
REMARK 3 AUTHORS : MOLECULAR SIMULATIONS, INC. (CNX)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 459 NOE
REMARK 3 -DERIVED DISTANCE RESTRAINTS, 28 H-BOND RESTRAINTS, 66 DIHEDRAL
REMARK 3 ANGLE RESTRAINTS, AND 38 RESIDUAL DIPOLAR COUPLING RESTRAINTS
REMARK 4
REMARK 4 1KMX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-DEC-01.
REMARK 100 THE DEPOSITION ID IS D_1000015124.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 300; 300; 300
REMARK 210 PH : 5.5; 5.5; 5.5; 5.5
REMARK 210 IONIC STRENGTH : 25 MM SODIUM ACETATE; 50 MM
REMARK 210 SODIUM CHLORIDE; 25 MM SODIUM
REMARK 210 ACETATE; 50 MM SODIUM CHLORIDE;
REMARK 210 25 MM SODIUM ACETATE; 50 MM
REMARK 210 SODIUM CHLORIDE; 25 MM SODIUM
REMARK 210 ACETATE; 50 MM SODIUM CHLORIDE
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT;
REMARK 210 AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.0 MM VEGF HEPARIN-BINDING
REMARK 210 DOMAIN; 25 MM SODIUM ACETATE; 50
REMARK 210 MM SODIUM CHLORIDE, 0.02% SODIUM
REMARK 210 AZIDE; 2.0 MM VEGF HEPARIN-
REMARK 210 BINDING DOMAIN U-15N; 25 MM
REMARK 210 SODIUM ACETATE; 50 MM SODIUM
REMARK 210 CHLORIDE, 0.02% SODIUM AZIDE;
REMARK 210 2.0 MM VEGF HEPARIN-BINDING
REMARK 210 DOMAIN U-15N; 25 MM SODIUM
REMARK 210 ACETATE; 50 MM SODIUM CHLORIDE,
REMARK 210 0.02% SODIUM AZIDE; 0.6 MM VEGF
REMARK 210 HEPARIN-BINDING DOMAIN U-15N; 25
REMARK 210 MM SODIUM ACETATE; 50 MM SODIUM
REMARK 210 CHLORIDE; 0.02% SODIUM AZIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; 2D 15N
REMARK 210 IPAP-HSQC; 2D 15N IPAP HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR, FELIX, CNX
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS REFINED USING 1H-15N DIPOLAR COUPLING
REMARK 210 RESTRAINTS
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-20
REMARK 470 RES CSSEQI ATOMS
REMARK 470 ARG A 55 O
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 GLN A 3 -71.95 -160.20
REMARK 500 1 GLU A 4 79.42 68.09
REMARK 500 1 CYS A 10 -71.97 -91.73
REMARK 500 1 SER A 11 -159.16 -90.55
REMARK 500 1 GLU A 12 -70.82 -125.04
REMARK 500 1 ARG A 14 58.72 -94.96
REMARK 500 1 ARG A 54 -69.29 -163.65
REMARK 500 2 ARG A 2 176.17 61.61
REMARK 500 2 PRO A 9 172.32 -45.43
REMARK 500 2 CYS A 10 -82.83 -90.31
REMARK 500 2 ARG A 13 -59.40 -127.76
REMARK 500 2 ARG A 14 59.22 -90.60
REMARK 500 2 ARG A 54 -48.35 -159.83
REMARK 500 3 PRO A 9 174.85 -56.61
REMARK 500 3 CYS A 10 -79.70 -90.10
REMARK 500 3 ARG A 13 -71.49 -141.76
REMARK 500 3 ARG A 14 45.22 -158.46
REMARK 500 3 HIS A 16 -46.36 -161.16
REMARK 500 3 PRO A 22 39.40 -89.68
REMARK 500 3 GLN A 23 -49.24 -148.82
REMARK 500 3 PRO A 53 -75.09 -85.48
REMARK 500 3 ARG A 54 -140.42 -154.53
REMARK 500 4 ARG A 2 -166.23 60.72
REMARK 500 4 GLN A 3 73.61 58.72
REMARK 500 4 GLU A 4 33.98 -141.21
REMARK 500 4 ARG A 14 83.51 -67.84
REMARK 500 4 LYS A 15 176.55 -41.52
REMARK 500 4 HIS A 16 -48.14 -153.68
REMARK 500 4 ARG A 54 -92.12 -159.14
REMARK 500 5 ARG A 2 -159.57 -89.56
REMARK 500 5 GLU A 4 112.39 64.98
REMARK 500 5 ASN A 5 85.63 -150.21
REMARK 500 5 PRO A 9 178.84 -47.97
REMARK 500 5 CYS A 10 -93.65 -90.08
REMARK 500 5 GLU A 12 32.17 -141.82
REMARK 500 5 ARG A 13 -43.69 -150.49
REMARK 500 5 ARG A 14 60.58 -152.61
REMARK 500 5 LEU A 17 44.70 -97.08
REMARK 500 5 ARG A 54 -54.54 -139.16
REMARK 500 6 CYS A 10 -64.83 -90.37
REMARK 500 6 ARG A 13 -46.90 -138.71
REMARK 500 6 ARG A 14 59.07 -93.47
REMARK 500 6 ARG A 54 -69.51 -142.42
REMARK 500 7 ARG A 2 -45.58 -159.28
REMARK 500 7 PRO A 6 -156.45 -58.15
REMARK 500 7 PRO A 9 -169.45 -72.45
REMARK 500 7 CYS A 10 -76.16 -88.67
REMARK 500 7 SER A 11 -76.80 -88.48
REMARK 500 7 GLU A 12 -67.21 -156.97
REMARK 500 7 ARG A 13 -48.44 -142.36
REMARK 500
REMARK 500 THIS ENTRY HAS 152 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VGH RELATED DB: PDB
REMARK 900 1VGH IS THE SAME PROTEIN BUT REFINED WITHOUT USING RESIDUAL DIPOLAR
REMARK 900 COUPLING RESTRAINTS
REMARK 900 RELATED ID: 2VGH RELATED DB: PDB
REMARK 900 2VGH IS THE MINIMIZED MEAN CORRESPONDING THE THE SAME PROTEIN
REMARK 900 REFINED WITHOUT RESIDUAL DIPOLAR COUPLING RESTRAINTS
DBREF 1KMX A 1 55 UNP P15692 VEGFA_HUMAN 137 191
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 THR A 32 ALA A 38 1 7
SHEET 1 A 2 PHE A 18 GLN A 20 0
SHEET 2 A 2 CYS A 27 CYS A 29 -1 O SER A 28 N 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 O ARG A 49 N ASN A 44
SSBOND 1 CYS A 7 CYS A 25 1555 1555 2.03
SSBOND 2 CYS A 10 CYS A 27 1555 1555 2.03
SSBOND 3 CYS A 29 CYS A 48 1555 1555 2.03
SSBOND 4 CYS A 36 CYS A 50 1555 1555 2.03
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 - b 23 2 Bytes