Header list of 1cv9.pdb file
Complete list - 16 202 Bytes
HEADER IMMUNE SYSTEM 23-AUG-99 1CV9
TITLE NMR STUDY OF ITAM PEPTIDE SUBSTRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IG-ALPHA ITAM PEPTIDE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 178-189;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SEQUENCE FROM HUMAN IG-ALPHA ITAM
KEYWDS LYN TYROSINE KINASE, ITAM, IMMUNORECEPTOR TYROSINE ACTIVATION MOTIF,
KEYWDS 2 PEPTIDE SUBSTATE, IMMUNE SYSTEM
EXPDTA SOLUTION NMR
AUTHOR B.S.GAUL,M.L.HARRISON,R.L.GEAHLEN,C.B.POST
REVDAT 6 16-FEB-22 1CV9 1 REMARK LINK
REVDAT 5 24-FEB-09 1CV9 1 VERSN
REVDAT 4 01-APR-03 1CV9 1 JRNL
REVDAT 3 31-MAY-00 1CV9 3 JRNL ATOM SEQRES
REVDAT 2 05-NOV-99 1CV9 3 ATOM SEQRES
REVDAT 1 31-AUG-99 1CV9 0
JRNL AUTH B.S.GAUL,M.L.HARRISON,R.L.GEAHLEN,R.A.BURTON,C.B.POST
JRNL TITL SUBSTRATE RECOGNITION BY THE LYN PROTEIN-TYROSINE KINASE.
JRNL TITL 2 NMR STRUCTURE OF THE IMMUNORECEPTOR TYROSINE-BASED
JRNL TITL 3 ACTIVATION MOTIF SIGNALING REGION OF THE B CELL ANTIGEN
JRNL TITL 4 RECEPTOR.
JRNL REF J.BIOL.CHEM. V. 275 16174 2000
JRNL REFN ISSN 0021-9258
JRNL PMID 10748115
JRNL DOI 10.1074/JBC.M909044199
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1, CHARMM 23.2
REMARK 3 AUTHORS : BRUNGER, A.T. (X-PLOR), BROOKS, B.R. ET AL.
REMARK 3 (CHARMM)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CV9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY NDB.
REMARK 100 THE DEPOSITION ID IS D_1000009563.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 278
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM ITP WITH 0.2 MM KLYN, PH
REMARK 210 7.0 PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 2D ROESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : THE SIMULATED ANNEALING PROTOCOL
REMARK 210 IN THE X-PLOR 3.1 MANUAL WAS
REMARK 210 USED FOR STRUCTURE CALCULATION.
REMARK 210 RESTRAINED POWELL MINIMIZATION
REMARK 210 INCOPORATED THE CHARMM FORCE
REMARK 210 FIELD USING THE TOP_ALL22 AND
REMARK 210 PAR_ALL22 FILES IN THE X-PLOR
REMARK 210 3.1 LIBRARY. 107 NOE DERIVED
REMARK 210 DISTANCE RESTRAINTS WERE USED
REMARK 210 THROUGH OUT THE STRUCTURE
REMARK 210 CALCULATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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 ASN A 3 -77.53 -90.35
REMARK 500 LEU A 4 -13.58 47.22
REMARK 500 GLU A 6 -158.76 -133.81
REMARK 500 LEU A 8 33.42 -87.67
REMARK 500 ASN A 9 94.01 73.47
REMARK 500 LEU A 10 -129.17 -104.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 6 GLY A 7 -144.37
REMARK 500 GLY A 7 LEU A 8 -110.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 13
DBREF 1CV9 A 0 13 PDB 1CV9 1CV9 0 13
SEQRES 1 A 14 ACE ASP GLU ASN LEU TYR GLU GLY LEU ASN LEU ASP ASP
SEQRES 2 A 14 NH2
HET ACE A 0 6
HET NH2 A 13 3
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
FORMUL 1 ACE C2 H4 O
FORMUL 1 NH2 H2 N
LINK C ACE A 0 N ASP A 1 1555 1555 1.34
LINK C ASP A 12 N NH2 A 13 1555 1555 1.35
SITE 1 AC2 1 ASP A 12
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
Complete list - 16 202 Bytes