Header list of 1esk.pdb file
Complete list - 16 20 Bytes
HEADER VIRAL PROTEIN 10-APR-00 1ESK
TITLE SOLUTION STRUCTURE OF NCP7 FROM HIV-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GAG POLYPROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 12-53;
COMPND 5 SYNONYM: NUCLEOCAPSID PROTEIN NCP7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PROTEIN WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 IS NATURALLY FOUND IN HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 (HIV-1).
KEYWDS (12-53)NCP7, HIV-1, PROTEIN, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 9
AUTHOR N.MORELLET,H.DEMENE,V.TEILLEUX,T.HUYNH-DINH,H.DE ROCQUIGNY,M.-
AUTHOR 2 C.FOURNIE-ZALUSKI,B.P.ROQUES
REVDAT 3 16-FEB-22 1ESK 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1ESK 1 VERSN
REVDAT 1 26-APR-00 1ESK 0
JRNL AUTH N.MORELLET,H.DEMENE,V.TEILLEUX,T.HUYNH-DINH,H.DE ROCQUIGNY,
JRNL AUTH 2 M.-C.FOURNIE-ZALUSKI,B.P.ROQUES
JRNL TITL SOLUTION STRUCTURE OF (12-53)NCP7 OF HIV-1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.MORELLET,H.DE ROQUIGNY,Y.MELY,N.JULLIAN,H.DEMENE,
REMARK 1 AUTH 2 M.OTTMANN,D.GERARD,J.L.DARLIX,M.C.FOURNIE-ZALUSKI,B.P.ROQUES
REMARK 1 TITL CONFORMATIONAL BEHAVIOUR OF THE ACTIVE AND INACTIVE FORMS OF
REMARK 1 TITL 2 THE NUCLEOCAPSID NCP7 OF HIV-1 STUDIED BY 1H NMR.
REMARK 1 REF J.MOL.BIOL. V. 235 287 1994
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH N.MORELLET,H.DEMENE,V.TEILLEUX,T.HUYNH-DINH,H.DE ROQUIGNY,
REMARK 1 AUTH 2 M.C.FOURNIE-ZALUSKI,B.P.ROQUES
REMARK 1 TITL STRUCTURE OF THE COMPLEX BETWEEN THE HIV-1 NUCLEOCAPSID
REMARK 1 TITL 2 PROTEIN AND THE SINGLE-STRANDED PENTANUCLEOTIDE D(ACGCC).
REMARK 1 REF J.MOL.BIOL. V. 283 419 1998
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1998.2098
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : UXNMR 940501, DISCOVER
REMARK 3 AUTHORS : BRUKER (UXNMR), MSI (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 444 NOE-DERIVED DISTANCE CONSTRAINTS
REMARK 4
REMARK 4 1ESK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010857.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : N.A.
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM (12-53)NCP7, 90%H2O, 10%
REMARK 210 D2O, PH 6.0
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 9
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 1 PRO A 31 C - N - CD ANGL. DEV. = -15.2 DEGREES
REMARK 500 3 PRO A 31 C - N - CD ANGL. DEV. = -14.5 DEGREES
REMARK 500 7 CYS A 15 CB - CA - C ANGL. DEV. = 7.3 DEGREES
REMARK 500 8 PRO A 31 C - N - CD ANGL. DEV. = -15.0 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 17 -83.58 -54.39
REMARK 500 1 ARG A 29 56.40 -111.20
REMARK 500 1 PRO A 31 164.95 40.77
REMARK 500 1 LYS A 38 -60.13 -121.43
REMARK 500 1 HIS A 44 168.23 151.89
REMARK 500 2 PRO A 31 178.63 32.76
REMARK 500 3 VAL A 13 135.04 -35.98
REMARK 500 3 ASN A 17 -84.46 -57.68
REMARK 500 3 ARG A 29 55.76 -114.28
REMARK 500 3 PRO A 31 173.00 40.37
REMARK 500 3 HIS A 44 163.97 149.81
REMARK 500 4 GLU A 21 171.33 55.52
REMARK 500 4 PRO A 31 176.03 31.76
REMARK 500 5 CYS A 18 -43.39 -131.63
REMARK 500 5 GLU A 21 171.55 74.91
REMARK 500 5 PRO A 31 170.47 34.41
REMARK 500 5 LYS A 38 -60.93 -101.42
REMARK 500 5 HIS A 44 165.22 146.95
REMARK 500 6 PRO A 31 174.59 33.84
REMARK 500 6 LYS A 38 -62.59 -103.17
REMARK 500 6 HIS A 44 162.22 153.75
REMARK 500 6 ARG A 52 46.08 -88.07
REMARK 500 7 VAL A 13 135.03 -35.72
REMARK 500 7 PRO A 31 176.58 32.99
REMARK 500 7 LYS A 38 -63.87 -106.46
REMARK 500 7 HIS A 44 160.19 151.29
REMARK 500 7 ARG A 52 36.86 -154.15
REMARK 500 8 ASN A 17 -80.27 -52.26
REMARK 500 8 ARG A 29 58.43 -110.25
REMARK 500 8 PRO A 31 165.49 40.18
REMARK 500 8 THR A 50 -75.69 -96.15
REMARK 500 8 GLU A 51 32.86 -167.65
REMARK 500 9 VAL A 13 135.28 -36.94
REMARK 500 9 CYS A 18 -35.63 -136.26
REMARK 500 9 GLU A 21 167.65 64.55
REMARK 500 9 PRO A 31 169.80 36.47
REMARK 500 9 GLU A 42 -4.14 -145.97
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 4 ARG A 52 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 54 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 15 SG
REMARK 620 2 CYS A 18 SG 112.7
REMARK 620 3 HIS A 23 NE2 105.2 109.4
REMARK 620 4 CYS A 28 SG 109.0 110.5 109.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 55 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 36 SG
REMARK 620 2 CYS A 39 SG 112.4
REMARK 620 3 HIS A 44 NE2 108.6 109.9
REMARK 620 4 CYS A 49 SG 106.5 113.3 105.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 54
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 55
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BJ6 RELATED DB: PDB
DBREF 1ESK A 12 53 UNP P04585 POL_HV1H2 388 429
SEQADV 1ESK ASN A 12 UNP P04585 ILE 388 CONFLICT
SEQRES 1 A 42 ASN VAL LYS CYS PHE ASN CYS GLY LYS GLU GLY HIS THR
SEQRES 2 A 42 ALA ARG ASN CYS ARG ALA PRO ARG LYS LYS GLY CYS TRP
SEQRES 3 A 42 LYS CYS GLY LYS GLU GLY HIS GLN MET LYS ASP CYS THR
SEQRES 4 A 42 GLU ARG GLN
HET ZN A 54 1
HET ZN A 55 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
LINK SG CYS A 15 ZN ZN A 54 1555 1555 2.25
LINK SG CYS A 18 ZN ZN A 54 1555 1555 2.22
LINK NE2 HIS A 23 ZN ZN A 54 1555 1555 2.00
LINK SG CYS A 28 ZN ZN A 54 1555 1555 2.24
LINK SG CYS A 36 ZN ZN A 55 1555 1555 2.25
LINK SG CYS A 39 ZN ZN A 55 1555 1555 2.23
LINK NE2 HIS A 44 ZN ZN A 55 1555 1555 2.03
LINK SG CYS A 49 ZN ZN A 55 1555 1555 2.19
SITE 1 AC1 4 CYS A 15 CYS A 18 HIS A 23 CYS A 28
SITE 1 AC2 5 CYS A 36 CYS A 39 HIS A 44 CYS A 49
SITE 2 AC2 5 GLU A 51
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 - 16 20 Bytes