Header list of 1l3y.pdb file
Complete list - 23 20 Bytes
HEADER CELL ADHESION 03-MAR-02 1L3Y
TITLE INTEGRIN EGF-LIKE MODULE 3 FROM THE BETA-2 SUBUNIT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRIN BETA-2:CYSTEINE-RICH MODULE 3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 535-574;
COMPND 5 SYNONYM: CELL SURFACE ADHESION GLYCOPROTEINS LFA-1/CR3/P150,95, CD18,
COMPND 6 BETA-SUBUNIT, COMPLEMENT RECEPTOR C3 BETA-SUBUNIT;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS INTEGRIN, BETA-2 SUBUNIT, CELL ADHESION, CYSTEINE-RICH MODULE, EGF-
KEYWDS 2 LIKE MODULE
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR N.BEGLOVA,S.C.BLACKLOW,J.TAKAGI,T.A.SPRINGER
REVDAT 3 23-FEB-22 1L3Y 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1L3Y 1 VERSN
REVDAT 1 01-APR-02 1L3Y 0
JRNL AUTH N.BEGLOVA,S.C.BLACKLOW,J.TAKAGI,T.A.SPRINGER
JRNL TITL CYSTEINE-RICH MODULE STRUCTURE REVEALS A FULCRUM FOR
JRNL TITL 2 INTEGRIN REARRANGEMENT UPON ACTIVATION.
JRNL REF NAT.STRUCT.BIOL. V. 9 282 2002
JRNL REFN ISSN 1072-8368
JRNL PMID 11896403
JRNL DOI 10.1038/NSB779
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : GIFA 4.3, CNS 1.0
REMARK 3 AUTHORS : DELSUC, M.A. (GIFA), BRUNGER, A (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1L3Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015624.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.2
REMARK 210 IONIC STRENGTH : 5MM NAPO4
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM I-EGF3 U-15N, 5 MM NAPO4; 1
REMARK 210 MM I-EGF3, 5 MM NAPO4
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_TOCSY; HMQC-J; 1H-
REMARK 210 NOESY; 1H-TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, CNS 1.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
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: 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 HE1 TYR A 10 HB2 GLN A 13 1.28
REMARK 500 H PHE A 24 O LYS A 27 1.46
REMARK 500 O PHE A 24 H LYS A 27 1.54
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 CYS A 7 133.25 -29.20
REMARK 500 1 ASN A 11 -86.14 -155.45
REMARK 500 1 GLN A 13 -116.11 -106.58
REMARK 500 1 VAL A 14 111.50 -168.65
REMARK 500 1 CYS A 15 40.08 71.70
REMARK 500 1 CYS A 25 90.53 -32.27
REMARK 500 1 GLU A 35 -83.11 -155.07
REMARK 500 1 ALA A 38 -80.46 -143.71
REMARK 500 1 CYS A 39 41.37 -155.96
REMARK 500 2 ASP A 3 -124.79 -175.28
REMARK 500 2 ILE A 5 80.39 -156.30
REMARK 500 2 ASN A 11 49.76 -156.05
REMARK 500 2 GLN A 13 -165.05 -105.05
REMARK 500 2 CYS A 15 46.15 74.70
REMARK 500 2 PHE A 24 -97.43 -156.06
REMARK 500 2 GLU A 35 -83.53 -155.14
REMARK 500 2 ALA A 38 -80.35 -145.18
REMARK 500 2 CYS A 39 40.67 -155.99
REMARK 500 3 CYS A 2 -164.53 43.93
REMARK 500 3 ASP A 3 -118.72 80.02
REMARK 500 3 TYR A 10 -149.26 -88.37
REMARK 500 3 CYS A 15 43.69 84.36
REMARK 500 3 CYS A 25 102.51 -37.46
REMARK 500 3 GLU A 35 -152.98 -155.40
REMARK 500 3 ALA A 38 -81.39 -140.84
REMARK 500 3 CYS A 39 39.33 -157.10
REMARK 500 4 CYS A 2 -36.34 -177.10
REMARK 500 4 CYS A 7 136.61 -18.85
REMARK 500 4 ASN A 11 -79.96 -156.14
REMARK 500 4 VAL A 14 106.16 43.59
REMARK 500 4 CYS A 15 40.13 80.28
REMARK 500 4 LEU A 22 -150.08 -104.10
REMARK 500 4 PHE A 24 -102.72 -156.45
REMARK 500 4 CYS A 25 77.31 -56.08
REMARK 500 4 GLU A 35 -90.28 -154.33
REMARK 500 4 ALA A 38 -81.96 -136.84
REMARK 500 4 CYS A 39 42.40 -156.13
REMARK 500 5 ASP A 3 -148.81 178.72
REMARK 500 5 ILE A 5 67.22 -155.45
REMARK 500 5 TYR A 10 -146.19 -92.16
REMARK 500 5 GLN A 13 -156.81 -149.57
REMARK 500 5 ARG A 20 -42.45 -155.13
REMARK 500 5 CYS A 25 72.76 -55.04
REMARK 500 5 GLU A 35 -102.65 -155.44
REMARK 500 5 ALA A 38 -73.62 -138.56
REMARK 500 5 CYS A 39 20.21 -157.35
REMARK 500 6 CYS A 2 -32.04 -177.48
REMARK 500 6 ASP A 3 -155.61 -167.56
REMARK 500 6 ASN A 6 53.52 -93.89
REMARK 500 6 CYS A 7 135.16 -7.77
REMARK 500
REMARK 500 THIS ENTRY HAS 142 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1L3Y A 1 40 UNP P05107 ITB2_HUMAN 535 574
SEQADV 1L3Y ALA A 41 UNP P05107 CLONING ARTIFACT
SEQRES 1 A 41 GLU CYS ASP THR ILE ASN CYS GLU ARG TYR ASN GLY GLN
SEQRES 2 A 41 VAL CYS GLY GLY PRO GLY ARG GLY LEU CYS PHE CYS GLY
SEQRES 3 A 41 LYS CYS ARG CYS HIS PRO GLY PHE GLU GLY SER ALA CYS
SEQRES 4 A 41 GLN ALA
HELIX 1 1 GLY A 16 ARG A 20 1 5
SHEET 1 A 2 GLY A 21 PHE A 24 0
SHEET 2 A 2 LYS A 27 CYS A 30 -1 O LYS A 27 N PHE A 24
SSBOND 1 CYS A 2 CYS A 25 1555 1555 2.03
SSBOND 2 CYS A 7 CYS A 23 1555 1555 2.03
SSBOND 3 CYS A 15 CYS A 28 1555 1555 2.03
SSBOND 4 CYS A 30 CYS A 39 1555 1555 2.03
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