Header list of 1kuz.pdb file
Complete list - b 23 2 Bytes
HEADER CELL ADHESION 22-JAN-02 1KUZ
TITLE SOLUTION STRUCTURE OF THE MEMBRANE PROXIMAL REGIONS OF ALPHA-IIB AND
TITLE 2 BETA-3 INTEGRINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRIN ALPHA-IIB;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MEMBRANE PROXIMAL REGION;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: INTEGRIN BETA-3;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: MEMBRANE PROXIMAL REGION;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS PROTEIN WAS CUSTOM SYNTHESIZED. IT IS NATURALLY
SOURCE 4 FOUND IN HOMO SAPIENS (HUMAN).;
SOURCE 5 MOL_ID: 2;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 OTHER_DETAILS: THIS PROTEIN WAS CUSTOM SYNTHESIZED. IT IS NATURALLY
SOURCE 8 FOUND IN HOMO SAPIENS (HUMAN).
KEYWDS COILED-COIL, CELL ADHESION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.M.WELJIE,P.M.HWANG,H.J.VOGEL
REVDAT 3 23-FEB-22 1KUZ 1 REMARK
REVDAT 2 24-FEB-09 1KUZ 1 VERSN
REVDAT 1 08-MAY-02 1KUZ 0
JRNL AUTH A.M.WELJIE,P.M.HWANG,H.J.VOGEL
JRNL TITL SOLUTION STRUCTURES OF THE CYTOPLASMIC TAIL COMPLEX FROM
JRNL TITL 2 PLATELET INTEGRIN ALPHA IIB- AND BETA 3-SUBUNITS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 99 5878 2002
JRNL REFN ISSN 0027-8424
JRNL PMID 11983888
JRNL DOI 10.1073/PNAS.092515799
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.1, ARIA 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER, A.T. ET AL. (CNS),
REMARK 3 NILGES, M. ET AL. (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KUZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1000015369.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM AIIB/B3 PEPTIDES; PH 5.2
REMARK 210 (UNBUFFERED), 90% H2O 10% D2O; 2
REMARK 210 MM AIIB/B3 PEPTIDES; PH 5.2
REMARK 210 (UNBUFFERED), 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE VERSION 1.8 REV
REMARK 210 2000.243.12.42, NMRVIEW 5.03
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS, MATRIX RELAXATION,
REMARK 210 TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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 : 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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
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 TRP A 2 -86.87 -119.95
REMARK 500 1 LYS A 8 -8.80 -59.26
REMARK 500 1 ASN A 10 -87.16 -91.57
REMARK 500 1 ALA B 24 47.57 -84.85
REMARK 500 2 TRP A 2 -88.38 -120.05
REMARK 500 2 ASN A 10 -86.03 -110.48
REMARK 500 2 ILE B 15 36.13 -87.38
REMARK 500 2 ALA B 24 41.99 -84.37
REMARK 500 2 ARG B 32 -62.33 -106.64
REMARK 500 3 TRP A 2 -90.41 -120.56
REMARK 500 3 LYS A 8 -9.42 -58.64
REMARK 500 3 ASN A 10 -74.65 -88.18
REMARK 500 4 TRP A 2 -90.02 -120.10
REMARK 500 4 ASN A 10 -77.74 -94.59
REMARK 500 4 ALA B 24 37.30 -79.48
REMARK 500 4 ARG B 32 -64.27 -93.00
REMARK 500 5 TRP A 2 -86.03 -120.22
REMARK 500 5 LYS A 8 -7.24 -59.74
REMARK 500 5 ASN A 10 -76.41 -90.88
REMARK 500 5 ALA B 24 47.06 -83.84
REMARK 500 5 ARG B 32 -60.15 -92.73
REMARK 500 6 TRP A 2 -89.57 -117.52
REMARK 500 6 ASN A 10 -95.57 -101.43
REMARK 500 6 ALA B 24 48.21 -83.86
REMARK 500 7 TRP A 2 -88.01 -120.52
REMARK 500 7 LYS A 8 -7.55 -59.51
REMARK 500 7 ASN A 10 -76.95 -86.65
REMARK 500 7 ILE B 15 33.66 -88.14
REMARK 500 8 TRP A 2 -92.71 -112.30
REMARK 500 8 LYS A 8 -9.34 -59.82
REMARK 500 8 ASN A 10 -77.33 -94.70
REMARK 500 8 ALA B 24 40.37 -83.58
REMARK 500 8 ARG B 32 -62.39 -108.24
REMARK 500 9 TRP A 2 -90.16 -120.35
REMARK 500 9 ASN A 10 -87.47 -120.82
REMARK 500 9 ALA B 24 48.83 -84.32
REMARK 500 9 ARG B 32 -63.58 -103.32
REMARK 500 10 TRP A 2 -91.68 -113.38
REMARK 500 10 ASN A 10 -78.65 -97.02
REMARK 500 10 ALA B 24 48.78 -84.58
REMARK 500 10 ARG B 32 -61.63 -93.56
REMARK 500 11 TRP A 2 -89.49 -113.61
REMARK 500 11 ASN A 10 -84.81 -96.70
REMARK 500 11 ALA B 24 45.03 -85.15
REMARK 500 11 ARG B 32 -66.62 -104.30
REMARK 500 12 TRP A 2 -97.43 -114.27
REMARK 500 12 ASN A 10 -76.10 -89.22
REMARK 500 13 TRP A 2 -88.28 -118.17
REMARK 500 13 ASN A 10 -89.45 -116.17
REMARK 500 13 ALA B 24 40.48 -78.75
REMARK 500
REMARK 500 THIS ENTRY HAS 79 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KUP RELATED DB: PDB
REMARK 900 1KUP IS THE SOLUTION STRUCTURE OF THE MEMBRANE PROXIMAL REGIONS OF
REMARK 900 ALPHA-IIB AND BETA-3 INTEGRINS; CONFORMER 1 OF 2 CONFORMATIONS
REMARK 900 DETERMINED.
DBREF 1KUZ A 1 11 UNP P08514 ITA2B_HUMAN 1018 1028
DBREF 1KUZ B 12 36 UNP P05106 ITB3_HUMAN 742 766
SEQRES 1 A 11 MET TRP LYS VAL GLY PHE PHE LYS ARG ASN ARG
SEQRES 1 B 25 LYS LEU LEU ILE THR ILE HIS ASP ARG LYS GLU PHE ALA
SEQRES 2 B 25 LYS PHE GLU GLU GLU ARG ALA ARG ALA LYS TRP ASP
HELIX 1 1 LYS A 3 LYS A 8 1 6
HELIX 2 2 ILE B 17 LYS B 21 5 5
HELIX 3 3 PHE B 26 ALA B 31 1 6
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 - b 23 2 Bytes