Header list of 1cs9.pdb file
Complete list - 16 202 Bytes
HEADER DNA BINDING PROTEIN 18-AUG-99 1CS9
TITLE SOLUTION STRUCTURE OF CGGIRGERA IN CONTACT WITH THE MONOCLONAL
TITLE 2 ANTIBODY MAB 4X11, NMR, 7 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H3 PEPTIDE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL REGION 130-135;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE PEPTIDE
SOURCE 4 CORRESPONDS TO THE IRGERA SEQUENCE PRESENT IN THE C-TERMINAL REGION
SOURCE 5 130-135 OF HISTONE H3 BOUND TO THE MAB 4X11 MONOCLONAL ANTIBODY
SOURCE 6 (IGG1). THE SEQUENCE CGG WAS ADDED TO THE N- TERMINUS OF THE IRGERA
SOURCE 7 SEQUENCE AS A LINKER TO THE DEXTRAN MATRIX IN BIACORE EXPERIMENTS
SOURCE 8 VIA THE CYS THIOL GROUP.
KEYWDS SYNTHETIC PEPTIDE, TR-NOE, ANTIGEN-ANTIBODY COMPLEX, DNA BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 7
AUTHOR A.PHAN CHAN DU,M.C.PETIT,G.GUICHARD,J.P.BRIAND,S.MULLER,M.T.CUNG
REVDAT 6 16-FEB-22 1CS9 1 REMARK
REVDAT 5 24-FEB-09 1CS9 1 VERSN
REVDAT 4 01-APR-03 1CS9 1 JRNL
REVDAT 3 13-JUN-01 1CS9 1 JRNL
REVDAT 2 03-NOV-99 1CS9 3 ATOM JRNL REMARK
REVDAT 1 02-SEP-99 1CS9 0
JRNL AUTH A.PHAN-CHAN-DU,M.C.PETIT,G.GUICHARD,J.P.BRIAND,S.MULLER,
JRNL AUTH 2 M.T.CUNG
JRNL TITL STRUCTURE OF ANTIBODY-BOUND PEPTIDES AND RETRO-INVERSO
JRNL TITL 2 ANALOGUES. A TRANSFERRED NUCLEAR OVERHAUSER EFFECT
JRNL TITL 3 SPECTROSCOPY AND MOLECULAR DYNAMICS APPROACH.
JRNL REF BIOCHEMISTRY V. 40 5720 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11341837
JRNL DOI 10.1021/BI001151H
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.4, DISCOVER 3
REMARK 3 AUTHORS : GUNTERT, WUTHRICH (DYANA), MOLECULAR SIMULATIONS
REMARK 3 INC. (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 ENERGY MINIMISATION. A DISTANT DEPENDENT DIELECTRIC CONSTANT
REMARK 3 EQUAL TO 4R WAS APPLIED. THE NET
REMARK 3 ELECTRIC CHARGES WERE DECREASED, WHILE THOSE OF THE N AND C
REMARK 3 TERMINAL CHARGED
REMARK 3 GROUPS WERE NEGLECTED. IN THE PDB, NH3+ IS INCLUDED IN THE RESIDUE
REMARK 3 CYS, AND
REMARK 3 COO- IS INCLUDED IN THE RESIDUE ALA. THE RESIDUE GLU HAS MISSING
REMARK 3 ATOMS HE2 IN ALL STRUCTURES
REMARK 3 BECAUSE IN DISCOVER, THIS RESIDUE IS MODELLED AS A CHARGED
REMARK 3 GROUP(WE HAVE COO- AND NOT COOH).
REMARK 4
REMARK 4 1CS9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-AUG-99.
REMARK 100 THE DEPOSITION ID IS D_1000009525.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 277
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 0.1M PHOSPHATE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 5 MM PEPTIDE, 0.1MM MAB; 100 MM
REMARK 210 PHOSPHATE BUFFER CONTAINING 0.02%
REMARK 210 SODIUM AZIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TOCSY, NOESY, COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DISCOVER 3
REMARK 210 METHOD USED : ENERGY MINIMIZATION MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 7
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 7
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE PEPTIDE/MAB MOLAR RATIO WAS ADJUSTED TO 50/1 (I.E. 5MM OF
REMARK 210 PEPTIDE AND
REMARK 210 0.1MM OF MAB)
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 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 3 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 3 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 4 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 4 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 5 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 5 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 6 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 6 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 7 ARG A 5 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 7 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 3.5 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 2 ARG A 5 -97.81 -154.01
REMARK 500 3 GLU A 7 -96.90 -158.65
REMARK 500 3 ARG A 8 65.11 -160.87
REMARK 500 4 ARG A 5 85.41 -158.30
REMARK 500 4 GLU A 7 119.21 -163.13
REMARK 500 4 ARG A 8 89.73 -156.61
REMARK 500 5 ARG A 5 -81.59 -157.65
REMARK 500 5 GLU A 7 -84.79 -157.47
REMARK 500 5 ARG A 8 -66.04 -157.62
REMARK 500 6 GLU A 7 83.01 -155.53
REMARK 500 7 GLU A 7 111.28 -160.49
REMARK 500 7 ARG A 8 85.82 -151.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CT6 RELATED DB: PDB
DBREF 1CS9 A 4 9 UNP P16106 H31_HUMAN 130 135
SEQRES 1 A 9 CYS GLY GLY ILE ARG GLY GLU ARG ALA
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 - 16 202 Bytes