Header list of 1ci5.pdb file
Complete list - r 14 2 Bytes
HEADER IMMUNE SYSTEM 07-APR-99 1CI5
TITLE GLYCAN-FREE MUTANT ADHESION DOMAIN OF HUMAN CD58 (LFA-3)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (LYMPHOCYTE FUNCTION-ASSOCIATED ANTIGEN 3(CD58));
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ADHESION DOMAIN;
COMPND 5 SYNONYM: 1DCD58-6M;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELLULAR_LOCATION: CELL SURFACE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET11A;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET11A-1DCD58X6;
SOURCE 12 EXPRESSION_SYSTEM_GENE: 1DCD58X6
KEYWDS ADHESION GLYCOPROTEIN, IMMUNOGLOBULIN SUPERFAMILY V-SET DOMAIN, CELL
KEYWDS 2 SURFACE RECEPTOR, IMMUNE SYSTEM
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Z.Y.J.SUN,V.DOTSCH,M.KIM,J.LI,E.L.REINHERZ,G.WAGNER
REVDAT 4 14-MAR-18 1CI5 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1CI5 1 VERSN
REVDAT 2 01-APR-03 1CI5 1 JRNL
REVDAT 1 22-JUN-99 1CI5 0
JRNL AUTH Z.Y.SUN,V.DOTSCH,M.KIM,J.LI,E.L.REINHERZ,G.WAGNER
JRNL TITL FUNCTIONAL GLYCAN-FREE ADHESION DOMAIN OF HUMAN CELL SURFACE
JRNL TITL 2 RECEPTOR CD58: DESIGN, PRODUCTION AND NMR STUDIES.
JRNL REF EMBO J. V. 18 2941 1999
JRNL REFN ISSN 0261-4189
JRNL PMID 10357807
JRNL DOI 10.1093/EMBOJ/18.11.2941
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NO NOE VIOLATION GREATER THAN 0.3 A, NO
REMARK 3 DIHEDRAL ANGLE VIOLATION GREATER THAN 5 DEGREE. AVERAGE BACKBONE
REMARK 3 ATOM (RESIDUE 3 - 95) RMSD TO MEAN STRUCTURE 0.37 A, AVERAGE
REMARK 3 HEAVY ATOM (RESIDUE 3 - 95) RMSD TO MEAN STRUCTURE 0.93 A.
REMARK 4
REMARK 4 1CI5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000891.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 10 MM NAPO4
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; NOESY-HSQC; HNCA;
REMARK 210 CBCA(CO)NH; HBHA(CBCACO)NH; HCCH-
REMARK 210 TOCSY; HNHA; HNHB
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500; INOVA500; INOVA750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY, X-PLOR, DIANA, DYANA
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 25
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST ENERGY FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED 1DCD58-6M.
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 O VAL A 26 H LEU A 38 1.57
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 GLN A 31 -133.02 67.30
REMARK 500 1 VAL A 35 -64.13 -103.02
REMARK 500 1 SER A 47 -97.21 51.53
REMARK 500 1 SER A 48 15.45 -140.69
REMARK 500 1 ARG A 52 28.75 -152.41
REMARK 500 1 LYS A 58 -74.74 -136.97
REMARK 500 1 ASN A 66 83.01 53.51
REMARK 500 1 ASP A 84 -74.32 -162.82
REMARK 500 1 SER A 85 139.74 -172.34
REMARK 500 2 PRO A 18 83.30 -59.35
REMARK 500 2 SER A 19 86.11 -150.36
REMARK 500 2 GLN A 31 -133.66 68.14
REMARK 500 2 VAL A 35 -67.81 -105.32
REMARK 500 2 GLU A 39 139.30 -177.55
REMARK 500 2 SER A 47 -141.26 48.30
REMARK 500 2 ARG A 52 17.75 -144.38
REMARK 500 2 THR A 57 40.64 -97.14
REMARK 500 2 LYS A 58 -71.65 -132.80
REMARK 500 2 TYR A 65 -91.19 -114.64
REMARK 500 2 ASN A 66 94.49 -57.55
REMARK 500 2 ASP A 84 -82.53 -139.57
REMARK 500 3 GLN A 31 -133.79 67.68
REMARK 500 3 VAL A 35 -69.33 -101.90
REMARK 500 3 SER A 47 -149.24 58.74
REMARK 500 3 SER A 48 30.73 -92.56
REMARK 500 3 THR A 57 47.04 -109.69
REMARK 500 3 LYS A 58 -71.69 -141.45
REMARK 500 3 ASN A 66 82.16 53.02
REMARK 500 3 ASP A 84 -85.33 -136.39
REMARK 500 4 GLN A 31 -133.32 66.11
REMARK 500 4 VAL A 35 -67.01 -104.97
REMARK 500 4 GLU A 39 128.72 -173.10
REMARK 500 4 SER A 47 28.53 47.12
REMARK 500 4 THR A 57 38.53 -97.68
REMARK 500 4 LYS A 58 -74.05 -127.79
REMARK 500 4 ASN A 66 100.42 55.88
REMARK 500 4 ASP A 84 -78.57 -159.75
REMARK 500 4 SER A 85 118.52 -171.09
REMARK 500 5 PRO A 18 64.22 -69.59
REMARK 500 5 GLN A 31 -133.49 68.14
REMARK 500 5 VAL A 35 -69.88 -101.12
REMARK 500 5 PHE A 46 -167.03 -111.85
REMARK 500 5 ARG A 52 23.98 -147.73
REMARK 500 5 LYS A 58 -72.64 -149.68
REMARK 500 5 ASN A 66 84.74 52.04
REMARK 500 5 ASP A 84 -79.76 -147.69
REMARK 500 5 SER A 85 142.27 -174.86
REMARK 500 6 SER A 2 -82.42 62.26
REMARK 500 6 SER A 19 -57.58 -129.87
REMARK 500 6 GLN A 21 142.47 -171.13
REMARK 500
REMARK 500 THIS ENTRY HAS 208 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CI5 A 1 95 UNP P19256 LFA3_HUMAN 29 123
SEQADV 1CI5 SER A 1 UNP P19256 PHE 29 ENGINEERED MUTATION
SEQADV 1CI5 LYS A 9 UNP P19256 VAL 37 ENGINEERED MUTATION
SEQADV 1CI5 GLN A 21 UNP P19256 VAL 49 ENGINEERED MUTATION
SEQADV 1CI5 LYS A 58 UNP P19256 VAL 86 ENGINEERED MUTATION
SEQADV 1CI5 SER A 85 UNP P19256 THR 113 ENGINEERED MUTATION
SEQADV 1CI5 GLY A 93 UNP P19256 LEU 121 ENGINEERED MUTATION
SEQRES 1 A 95 SER SER GLN GLN ILE TYR GLY VAL LYS TYR GLY ASN VAL
SEQRES 2 A 95 THR PHE HIS VAL PRO SER ASN GLN PRO LEU LYS GLU VAL
SEQRES 3 A 95 LEU TRP LYS LYS GLN LYS ASP LYS VAL ALA GLU LEU GLU
SEQRES 4 A 95 ASN SER GLU PHE ARG ALA PHE SER SER PHE LYS ASN ARG
SEQRES 5 A 95 VAL TYR LEU ASP THR LYS SER GLY SER LEU THR ILE TYR
SEQRES 6 A 95 ASN LEU THR SER SER ASP GLU ASP GLU TYR GLU MET GLU
SEQRES 7 A 95 SER PRO ASN ILE THR ASP SER MET LYS PHE PHE LEU TYR
SEQRES 8 A 95 VAL GLY GLU SER
HELIX 1 1 PHE A 49 ARG A 52 5 4
SHEET 1 A 6 GLN A 3 VAL A 8 0
SHEET 2 A 6 SER A 85 GLY A 93 1 N PHE A 89 O GLN A 3
SHEET 3 A 6 GLU A 74 SER A 79 -1 N MET A 77 O MET A 86
SHEET 4 A 6 VAL A 26 LYS A 30 -1 N LYS A 29 O GLU A 76
SHEET 5 A 6 ASP A 33 GLU A 39 -1 N LEU A 38 O VAL A 26
SHEET 6 A 6 GLU A 42 ALA A 45 -1 N ARG A 44 O GLU A 37
SHEET 1 B 3 ASN A 12 PHE A 15 0
SHEET 2 B 3 LEU A 62 TYR A 65 -1 N ILE A 64 O VAL A 13
SHEET 3 B 3 VAL A 53 LEU A 55 -1 N TYR A 54 O THR A 63
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 - r 14 2 Bytes