Header list of 1gyf.pdb file
Complete list - b 23 2 Bytes
HEADER IMMUNE SYSTEM 30-APR-99 1GYF
TITLE GYF DOMAIN FROM HUMAN CD2BP2 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (CYTOPLASMIC DOMAIN BINDING PROTEIN (CD2BP2));
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CD2-BINDING DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL: T-LYMPHOCYTE;
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_PLASMID: PTFT74
KEYWDS T CELL SIGNALING, PROLINE-RICH SEQUENCE RECOGNITION, ADAPTER DOMAIN,
KEYWDS 2 IMMUNE SYSTEM
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR C.FREUND,V.DOETSCH,K.NISHIZAWA,E.L.REINHERZ,G.WAGNER
REVDAT 4 23-FEB-22 1GYF 1 REMARK
REVDAT 3 24-FEB-09 1GYF 1 VERSN
REVDAT 2 01-APR-03 1GYF 1 JRNL
REVDAT 1 05-JAN-00 1GYF 0
JRNL AUTH C.FREUND,V.DOTSCH,K.NISHIZAWA,E.L.REINHERZ,G.WAGNER
JRNL TITL THE GYF DOMAIN IS A NOVEL STRUCTURAL FOLD THAT IS INVOLVED
JRNL TITL 2 IN LYMPHOID SIGNALING THROUGH PROLINE-RICH SEQUENCES.
JRNL REF NAT.STRUCT.BIOL. V. 6 656 1999
JRNL REFN ISSN 1072-8368
JRNL PMID 10404223
JRNL DOI 10.1038/10712
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: NULL
REMARK 4
REMARK 4 1GYF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAY-99.
REMARK 100 THE DEPOSITION ID IS D_1000000983.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : 50 MM NAPO4
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 90% WATER/10%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 15N-NOESY; 13C-NOESY;
REMARK 210 15N-TOCSY; HCCH-TOCSY; HNCA;
REMARK 210 CBCACONH; HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500; VXR500; UNITY500;
REMARK 210 UNITYPLUS750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY, DYANA, X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATIONS,
REMARK 210 LEAST ENERGY FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 6
REMARK 210
REMARK 210 REMARK: LOWEST ENERGY. 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 O THR A 51 H GLU A 55 1.55
REMARK 500 H TYR A 30 O TYR A 41 1.56
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 TYR A 41 -156.50 -141.80
REMARK 500 1 PHE A 82 30.39 -98.59
REMARK 500 1 LEU A 84 30.56 -147.02
REMARK 500 1 TYR A 85 -52.04 -138.54
REMARK 500 2 GLU A 39 -174.58 -58.56
REMARK 500 2 TYR A 41 -162.55 -114.05
REMARK 500 2 GLN A 73 66.36 -115.03
REMARK 500 2 PHE A 74 -172.67 45.09
REMARK 500 2 TYR A 75 113.39 179.63
REMARK 500 2 PHE A 82 35.53 -96.70
REMARK 500 2 LEU A 84 30.00 -146.51
REMARK 500 2 TYR A 85 -53.05 -133.53
REMARK 500 3 GLU A 39 -177.50 -60.46
REMARK 500 3 GLN A 73 65.42 64.74
REMARK 500 3 PHE A 74 -178.09 -55.64
REMARK 500 3 PHE A 82 38.44 -97.47
REMARK 500 3 ASP A 83 30.73 -143.60
REMARK 500 3 LEU A 84 30.95 -147.50
REMARK 500 3 TYR A 85 -49.98 -136.33
REMARK 500 4 GLU A 39 -177.64 -61.96
REMARK 500 4 TYR A 41 -158.04 -121.00
REMARK 500 4 GLN A 73 70.37 -114.11
REMARK 500 4 PHE A 74 166.71 56.48
REMARK 500 4 TYR A 75 114.97 -174.05
REMARK 500 4 LEU A 84 30.05 -144.88
REMARK 500 4 TYR A 85 -52.96 -138.10
REMARK 500 5 VAL A 26 97.36 -64.47
REMARK 500 5 ASN A 34 51.46 -90.46
REMARK 500 5 GLU A 39 -177.46 -56.34
REMARK 500 5 TYR A 41 -162.98 -111.33
REMARK 500 5 LEU A 84 29.27 -144.92
REMARK 500 5 TYR A 85 -46.58 -140.54
REMARK 500 6 TYR A 41 -164.39 -113.36
REMARK 500 6 PHE A 58 75.81 -117.27
REMARK 500 6 GLN A 73 65.93 -112.22
REMARK 500 6 PHE A 74 104.30 48.61
REMARK 500 6 LEU A 84 29.42 -145.82
REMARK 500 6 TYR A 85 -56.94 -143.65
REMARK 500 7 ALA A 38 159.20 -43.33
REMARK 500 7 GLU A 39 -177.07 -57.22
REMARK 500 7 LEU A 40 84.33 -157.13
REMARK 500 7 TYR A 41 -162.57 -114.81
REMARK 500 7 PHE A 58 78.73 -114.00
REMARK 500 7 GLN A 73 71.19 -109.29
REMARK 500 7 PHE A 74 155.16 59.22
REMARK 500 7 TYR A 75 107.62 -161.37
REMARK 500 7 LEU A 84 30.51 -145.28
REMARK 500 7 TYR A 85 -49.50 -133.34
REMARK 500 8 THR A 35 -166.85 -101.95
REMARK 500 8 ALA A 38 154.81 -44.14
REMARK 500
REMARK 500 THIS ENTRY HAS 124 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1GYF A 25 86 UNP O95400 CD2B2_HUMAN 280 341
SEQRES 1 A 62 ASP VAL MET TRP GLU TYR LYS TRP GLU ASN THR GLY ASP
SEQRES 2 A 62 ALA GLU LEU TYR GLY PRO PHE THR SER ALA GLN MET GLN
SEQRES 3 A 62 THR TRP VAL SER GLU GLY TYR PHE PRO ASP GLY VAL TYR
SEQRES 4 A 62 CYS ARG LYS LEU ASP PRO PRO GLY GLY GLN PHE TYR ASN
SEQRES 5 A 62 SER LYS ARG ILE ASP PHE ASP LEU TYR THR
HELIX 1 1 SER A 46 GLU A 55 1 10
HELIX 2 2 SER A 77 ARG A 79 5 3
SHEET 1 A 2 TRP A 28 LYS A 31 0
SHEET 2 A 2 TYR A 63 LYS A 66 -1 N ARG A 65 O GLU A 29
CISPEP 1 ASP A 68 PRO A 69 1 0.08
CISPEP 2 ASP A 68 PRO A 69 2 0.01
CISPEP 3 ASP A 68 PRO A 69 3 0.08
CISPEP 4 ASP A 68 PRO A 69 4 -0.01
CISPEP 5 ASP A 68 PRO A 69 5 0.01
CISPEP 6 ASP A 68 PRO A 69 6 0.02
CISPEP 7 ASP A 68 PRO A 69 7 -0.06
CISPEP 8 ASP A 68 PRO A 69 8 0.10
CISPEP 9 ASP A 68 PRO A 69 9 0.06
CISPEP 10 ASP A 68 PRO A 69 10 0.03
CISPEP 11 ASP A 68 PRO A 69 11 0.09
CISPEP 12 ASP A 68 PRO A 69 12 0.02
CISPEP 13 ASP A 68 PRO A 69 13 -0.03
CISPEP 14 ASP A 68 PRO A 69 14 -0.09
CISPEP 15 ASP A 68 PRO A 69 15 -0.09
CISPEP 16 ASP A 68 PRO A 69 16 0.09
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