Header list of 1kwd.pdb file
Complete list - 23 20 Bytes
HEADER VIRAL PROTEIN 29-JAN-02 1KWD
TITLE SOLUTION STRUCTURE OF THE CENTRAL CONSERVED REGION OF HUMAN
TITLE 2 RESPIRATORY SYNCYTIAL VIRUS ATTACHMENT GLYCOPROTEIN G 187
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR SURFACE GLYCOPROTEIN G;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 172-187;
COMPND 5 SYNONYM: ATTACHMENT GLYCOPROTEIN G;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SYNTHESIS OF THE PEPTIDE WAS PERFORMED BY A SOLID
SOURCE 4 PHASE METHOD USING FMOC/TBU CHEMISTRY.
KEYWDS CYSTEINE NOSE, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR M.SUGAWARA,J.CZAPLICKI,J.FERRAGE,J.F.HAEUW,U.F.POWER,N.CORVAIA,
AUTHOR 2 T.NGUYEN,A.BECK,A.MILON
REVDAT 3 23-FEB-22 1KWD 1 REMARK
REVDAT 2 24-FEB-09 1KWD 1 VERSN
REVDAT 1 17-JUN-03 1KWD 0
JRNL AUTH M.SUGAWARA,J.CZAPLICKI,J.FERRAGE,J.F.HAEUW,U.F.POWER,
JRNL AUTH 2 N.CORVAIA,T.NGUYEN,A.BECK,A.MILTON
JRNL TITL STRUCTURE-ANTIGENICITY RELATIONSHIP STUDIES OF THE CENTRAL
JRNL TITL 2 CONSERVED REGION OF HUMAN RESPIRATORY SYNCYTIAL VIRUS
JRNL TITL 3 PROTEIN G.
JRNL REF J.PEPT.RES. V. 60 271 2002
JRNL REFN ISSN 1397-002X
JRNL PMID 12383117
JRNL DOI 10.1034/J.1399-3011.2002.21027.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 98, DISCOVER 98
REMARK 3 AUTHORS : MSI (FELIX), MSI (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 76 NOE
REMARK 3 -DERIVED DISTANCE RESTRAINS AND 5 DIHEDRAL ANGLE RESTRAINS.
REMARK 4
REMARK 4 1KWD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-02.
REMARK 100 THE DEPOSITION ID IS D_1000015403.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 285
REMARK 210 PH : 4.6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM G4A(1-4/2-3), 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DISCOVER 98, XWINNMR 2.5
REMARK 210 METHOD USED : SIMULATED ANNEALING COUPLED WITH
REMARK 210 RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS, STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 7
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 16 CYS A 182 CB - CA - C ANGL. DEV. = 7.2 DEGREES
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 1 ASN A 178 76.16 54.41
REMARK 500 3 ASN A 178 72.11 50.85
REMARK 500 5 ASN A 178 81.10 55.21
REMARK 500 9 THR A 181 -69.06 -157.46
REMARK 500 10 THR A 181 -63.20 -157.21
REMARK 500 11 ASN A 178 72.07 49.19
REMARK 500 11 ALA A 184 -8.70 -59.98
REMARK 500 14 ASN A 178 83.67 65.93
REMARK 500 15 THR A 181 -60.82 -155.72
REMARK 500 16 ASN A 178 81.74 61.40
REMARK 500 16 ASN A 179 111.04 -160.10
REMARK 500 16 CYS A 182 -73.48 -75.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KWE RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE CENTRAL CONSERVED REGION OF HUMAN
REMARK 900 RESPIRATORY SYNCYTIAL VIRUS ATTACHMENT GLYCOPROTEIN G
DBREF 1KWD A 172 187 UNP P20895 VGLG_HRSVL 172 187
SEQRES 1 A 16 PRO CYS SER ILE CYS SER ASN ASN PRO THR CYS TRP ALA
SEQRES 2 A 16 ILE CYS LYS
SSBOND 1 CYS A 173 CYS A 186 1555 1555 2.00
SSBOND 2 CYS A 176 CYS A 182 1555 1555 2.00
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 - 23 20 Bytes