Header list of 1vve.pdb file
Complete list - r 25 2 Bytes
HEADER COMPLEMENT INHIBITOR 25-JUN-97 1VVE
TITLE C-TERMINAL HALF OF VACCINIA VIRUS COMPLEMENT CONTROL PROTEIN, NMR, 21
TITLE 2 STRUCTURES
SPLIT 1VVD 1VVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VACCINIA VIRUS COMPLEMENT CONTROL PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MODULES 3 AND 4;
COMPND 5 SYNONYM: SP35, VCP, VACCINIA VIRUS SP35;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VACCINIA VIRUS;
SOURCE 3 ORGANISM_TAXID: 10245;
SOURCE 4 GENE: C21L;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: HIS4;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPIC9
KEYWDS COMPLEMENT INHIBITOR, COMPLEMENT MODULE, SCR, SUSHI DOMAIN, MODULE
KEYWDS 2 PAIR
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR A.WILES,I.D.CAMPBELL,P.N.BARLOW
REVDAT 3 24-NOV-10 1VVE 1 REMARK
REVDAT 2 24-FEB-09 1VVE 1 VERSN
REVDAT 1 03-DEC-97 1VVE 0
JRNL AUTH A.P.WILES,G.SHAW,J.BRIGHT,A.PERCZEL,I.D.CAMPBELL,P.N.BARLOW
JRNL TITL NMR STUDIES OF A VIRAL PROTEIN THAT MIMICS THE REGULATORS OF
JRNL TITL 2 COMPLEMENT ACTIVATION.
JRNL REF J.MOL.BIOL. V. 272 253 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9299352
JRNL DOI 10.1006/JMBI.1997.1241
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.84
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION.
REMARK 4
REMARK 4 1VVE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N; 1H-NOESY HSQC; 1H-TOCSY
REMARK 210 HSQC; DQF-COSY; HOHAHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : HOME BUILT
REMARK 210 SPECTROMETER MANUFACTURER : HOME BUILT/GE
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SIMULATE ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : < 2 NOE VIOLATIONS > 0.5 A; NO
REMARK 210 DIHEDRAL ANGLE VIOLATIONS > 5
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ASN A 68 H LYS A 90 1.51
REMARK 500 O LYS A 76 HH TYR A 79 1.53
REMARK 500 O LYS A 94 H VAL A 117 1.54
REMARK 500 O ILE A 38 H THR A 55 1.58
REMARK 500 O VAL A 27 H VAL A 43 1.60
REMARK 500
REMARK 500 REMARK: NULL
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 22 SER A 10 96.41 -52.56
REMARK 500 22 ASN A 15 136.15 66.52
REMARK 500 22 TYR A 17 35.85 -151.46
REMARK 500 22 ASP A 19 -38.69 -147.57
REMARK 500 22 TYR A 21 -16.67 171.89
REMARK 500 22 THR A 22 -95.44 47.73
REMARK 500 22 ASN A 32 160.60 -47.94
REMARK 500 22 SER A 33 105.16 -59.98
REMARK 500 22 VAL A 43 -175.91 -60.24
REMARK 500 22 ASP A 52 65.28 62.62
REMARK 500 22 PRO A 62 -91.67 -75.43
REMARK 500 22 ASN A 68 49.14 36.53
REMARK 500 22 TYR A 70 163.14 -36.41
REMARK 500 22 LEU A 71 -70.59 -49.14
REMARK 500 22 SER A 80 111.90 -163.06
REMARK 500 22 TYR A 81 38.33 30.97
REMARK 500 22 ASN A 82 -140.60 -176.48
REMARK 500 22 LYS A 90 -88.93 -44.61
REMARK 500 22 SER A 100 106.37 -169.89
REMARK 500 22 CYS A 103 94.40 -49.52
REMARK 500 22 GLU A 112 142.34 -38.38
REMARK 500 22 CYS A 116 103.19 -54.66
REMARK 500 23 CYS A 3 97.90 -160.08
REMARK 500 23 SER A 10 92.48 -38.32
REMARK 500 23 TYR A 17 29.43 -157.09
REMARK 500 23 THR A 22 -99.01 51.14
REMARK 500 23 SER A 33 109.06 -45.51
REMARK 500 23 SER A 41 58.17 -68.45
REMARK 500 23 VAL A 43 -175.82 -61.52
REMARK 500 23 GLU A 49 73.42 -153.56
REMARK 500 23 THR A 55 -169.42 -112.10
REMARK 500 23 CYS A 56 86.72 -152.03
REMARK 500 23 GLN A 57 -143.39 -117.80
REMARK 500 23 VAL A 59 70.03 -101.19
REMARK 500 23 LYS A 60 -170.86 -65.52
REMARK 500 23 PRO A 62 -79.23 -85.31
REMARK 500 23 HIS A 63 128.60 171.63
REMARK 500 23 ILE A 66 170.15 172.44
REMARK 500 23 ASN A 68 65.92 38.56
REMARK 500 23 TYR A 70 -155.78 35.14
REMARK 500 23 SER A 73 -92.30 -80.66
REMARK 500 23 TYR A 79 -140.77 -114.51
REMARK 500 23 SER A 80 -123.24 -162.70
REMARK 500 23 ASN A 82 -110.87 -164.98
REMARK 500 23 ASP A 83 71.82 48.86
REMARK 500 23 TYR A 91 -176.63 52.49
REMARK 500 23 SER A 98 -166.91 -178.41
REMARK 500 23 SER A 99 -39.14 -159.23
REMARK 500 23 CYS A 103 92.06 -65.73
REMARK 500 23 ASN A 107 94.01 80.75
REMARK 500
REMARK 500 THIS ENTRY HAS 560 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 22 ARG A 13 0.31 SIDE CHAIN
REMARK 500 22 ARG A 77 0.27 SIDE CHAIN
REMARK 500 23 ARG A 13 0.27 SIDE CHAIN
REMARK 500 23 ARG A 77 0.27 SIDE CHAIN
REMARK 500 23 ARG A 118 0.19 SIDE CHAIN
REMARK 500 24 ARG A 13 0.18 SIDE CHAIN
REMARK 500 24 ARG A 77 0.21 SIDE CHAIN
REMARK 500 24 ARG A 118 0.32 SIDE CHAIN
REMARK 500 25 ARG A 13 0.14 SIDE CHAIN
REMARK 500 25 ARG A 77 0.31 SIDE CHAIN
REMARK 500 25 ARG A 118 0.32 SIDE CHAIN
REMARK 500 26 ARG A 13 0.20 SIDE CHAIN
REMARK 500 26 ARG A 77 0.16 SIDE CHAIN
REMARK 500 26 ARG A 118 0.20 SIDE CHAIN
REMARK 500 27 ARG A 13 0.29 SIDE CHAIN
REMARK 500 27 ARG A 77 0.32 SIDE CHAIN
REMARK 500 28 ARG A 13 0.29 SIDE CHAIN
REMARK 500 28 ARG A 77 0.19 SIDE CHAIN
REMARK 500 28 ARG A 118 0.09 SIDE CHAIN
REMARK 500 29 ARG A 13 0.32 SIDE CHAIN
REMARK 500 29 ARG A 77 0.12 SIDE CHAIN
REMARK 500 29 ARG A 118 0.27 SIDE CHAIN
REMARK 500 30 ARG A 13 0.15 SIDE CHAIN
REMARK 500 30 ARG A 77 0.14 SIDE CHAIN
REMARK 500 30 ARG A 118 0.14 SIDE CHAIN
REMARK 500 31 ARG A 13 0.32 SIDE CHAIN
REMARK 500 31 ARG A 77 0.26 SIDE CHAIN
REMARK 500 31 ARG A 118 0.27 SIDE CHAIN
REMARK 500 32 ARG A 77 0.32 SIDE CHAIN
REMARK 500 32 ARG A 118 0.30 SIDE CHAIN
REMARK 500 33 ARG A 13 0.14 SIDE CHAIN
REMARK 500 33 ARG A 77 0.19 SIDE CHAIN
REMARK 500 33 ARG A 118 0.32 SIDE CHAIN
REMARK 500 34 ARG A 13 0.17 SIDE CHAIN
REMARK 500 34 ARG A 77 0.28 SIDE CHAIN
REMARK 500 34 ARG A 118 0.31 SIDE CHAIN
REMARK 500 35 ARG A 13 0.20 SIDE CHAIN
REMARK 500 35 ARG A 77 0.31 SIDE CHAIN
REMARK 500 35 ARG A 118 0.28 SIDE CHAIN
REMARK 500 36 ARG A 13 0.16 SIDE CHAIN
REMARK 500 36 ARG A 77 0.23 SIDE CHAIN
REMARK 500 36 ARG A 118 0.30 SIDE CHAIN
REMARK 500 37 ARG A 13 0.24 SIDE CHAIN
REMARK 500 37 ARG A 77 0.25 SIDE CHAIN
REMARK 500 37 ARG A 118 0.20 SIDE CHAIN
REMARK 500 38 ARG A 13 0.30 SIDE CHAIN
REMARK 500 38 ARG A 77 0.19 SIDE CHAIN
REMARK 500 38 ARG A 118 0.23 SIDE CHAIN
REMARK 500 39 ARG A 77 0.28 SIDE CHAIN
REMARK 500 39 ARG A 118 0.21 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 59 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VVC RELATED DB: PDB
REMARK 900 RELATED ID: 1VVD RELATED DB: PDB
DBREF 1VVE A 1 118 UNP P68638 VCP_VACCV 146 263
SEQRES 1 A 118 VAL LYS CYS GLN SER PRO PRO SER ILE SER ASN GLY ARG
SEQRES 2 A 118 HIS ASN GLY TYR GLU ASP PHE TYR THR ASP GLY SER VAL
SEQRES 3 A 118 VAL THR TYR SER CYS ASN SER GLY TYR SER LEU ILE GLY
SEQRES 4 A 118 ASN SER GLY VAL LEU CYS SER GLY GLY GLU TRP SER ASP
SEQRES 5 A 118 PRO PRO THR CYS GLN ILE VAL LYS CYS PRO HIS PRO THR
SEQRES 6 A 118 ILE SER ASN GLY TYR LEU SER SER GLY PHE LYS ARG SER
SEQRES 7 A 118 TYR SER TYR ASN ASP ASN VAL ASP PHE LYS CYS LYS TYR
SEQRES 8 A 118 GLY TYR LYS LEU SER GLY SER SER SER SER THR CYS SER
SEQRES 9 A 118 PRO GLY ASN THR TRP LYS PRO GLU LEU PRO LYS CYS VAL
SEQRES 10 A 118 ARG
SHEET 1 A 2 GLY A 12 HIS A 14 0
SHEET 2 A 2 TYR A 29 CYS A 31 -1 N SER A 30 O ARG A 13
SHEET 1 B 2 SER A 36 ILE A 38 0
SHEET 2 B 2 THR A 55 GLN A 57 -1 N GLN A 57 O SER A 36
SHEET 1 C 3 THR A 108 LYS A 110 0
SHEET 2 C 3 SER A 100 SER A 104 -1 N SER A 104 O THR A 108
SHEET 3 C 3 ASN A 82 ASP A 86 -1 N VAL A 85 O SER A 101
SSBOND 1 CYS A 3 CYS A 45 1555 1555 2.02
SSBOND 2 CYS A 31 CYS A 56 1555 1555 2.02
SSBOND 3 CYS A 61 CYS A 103 1555 1555 2.02
SSBOND 4 CYS A 89 CYS A 116 1555 1555 2.02
CISPEP 1 LYS A 110 PRO A 111 22 -0.49
CISPEP 2 LYS A 110 PRO A 111 23 -0.49
CISPEP 3 LYS A 110 PRO A 111 24 -0.16
CISPEP 4 LYS A 110 PRO A 111 25 -0.29
CISPEP 5 LYS A 110 PRO A 111 26 -0.79
CISPEP 6 LYS A 110 PRO A 111 27 -0.04
CISPEP 7 LYS A 110 PRO A 111 28 0.69
CISPEP 8 LYS A 110 PRO A 111 29 0.16
CISPEP 9 LYS A 110 PRO A 111 30 -0.62
CISPEP 10 LYS A 110 PRO A 111 31 -0.48
CISPEP 11 LYS A 110 PRO A 111 32 0.40
CISPEP 12 LYS A 110 PRO A 111 33 -0.48
CISPEP 13 LYS A 110 PRO A 111 34 0.38
CISPEP 14 LYS A 110 PRO A 111 35 -0.85
CISPEP 15 LYS A 110 PRO A 111 36 -0.13
CISPEP 16 LYS A 110 PRO A 111 37 0.26
CISPEP 17 LYS A 110 PRO A 111 38 0.38
CISPEP 18 LYS A 110 PRO A 111 39 -0.23
CISPEP 19 LYS A 110 PRO A 111 40 -0.37
CISPEP 20 LYS A 110 PRO A 111 41 -0.63
CISPEP 21 LYS A 110 PRO A 111 42 -0.14
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 22
Complete list - r 25 2 Bytes