Header list of 2cud.pdb file
Complete list - r 9 2 Bytes
HEADER SIGNALING PROTEIN 26-MAY-05 2CUD
TITLE SOLUTION STRUCTURE OF THE SH3 DOMAIN OF THE HUMAN SRC-LIKE ADOPTER
TITLE 2 PROTEIN (SLAP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SRC-LIKE-ADAPTER;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN;
COMPND 5 SYNONYM: SRC-LIKE-ADAPTER PROTEIN 1, HSLAP, SLAP;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SLA;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040921-09;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS SH3 DOMAIN, SRC-LIKE ADAPTER PROTEIN (SLAP), NEGATIVE MITOGENESIS
KEYWDS 2 REGULATOR, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 3 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.OHNISHI,T.KIGAWA,N.TOCHIO,M.SATO,N.NAMEKI,S.KOSHIBA,M.INOUE,
AUTHOR 2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CUD 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CUD 1 VERSN
REVDAT 1 26-NOV-05 2CUD 0
JRNL AUTH S.OHNISHI,T.KIGAWA,N.TOCHIO,M.SATO,N.NAMEKI,S.KOSHIBA,
JRNL AUTH 2 M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SH3 DOMAIN OF THE HUMAN SRC-LIKE
JRNL TITL 2 ADOPTER PROTEIN (SLAP)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CUD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000024628.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.28MM PROTEIN U-15N,13C; 20MM D
REMARK 210 -TRISHCL(PH7.0); 100MM NACL; 1MM
REMARK 210 D-DTT; 0.02% NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0,4,
REMARK 210 KUJIRA 0.9295, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LEAST RESTRAINT VIOLATIONS
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: 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 ASN A 11 144.84 -38.31
REMARK 500 1 GLU A 13 41.28 35.48
REMARK 500 1 ASP A 25 140.07 -35.97
REMARK 500 1 PRO A 27 -173.57 -69.75
REMARK 500 1 PRO A 29 3.33 -69.74
REMARK 500 1 PRO A 76 -175.66 -69.67
REMARK 500 2 PRO A 8 -176.65 -69.70
REMARK 500 2 ASN A 11 148.42 -175.02
REMARK 500 2 PRO A 29 5.24 -69.70
REMARK 500 2 ILE A 31 -53.57 -125.56
REMARK 500 2 PRO A 76 2.78 -69.76
REMARK 500 2 SER A 77 134.88 -34.90
REMARK 500 3 PRO A 8 -174.51 -69.75
REMARK 500 3 PRO A 10 1.95 -69.77
REMARK 500 3 ASN A 11 135.56 -34.64
REMARK 500 3 PRO A 12 1.67 -69.85
REMARK 500 3 GLU A 13 101.63 -47.14
REMARK 500 3 VAL A 22 106.98 -55.68
REMARK 500 3 PRO A 27 -175.48 -69.76
REMARK 500 3 PRO A 29 2.92 -69.73
REMARK 500 3 PRO A 76 1.27 -69.79
REMARK 500 3 SER A 78 124.91 -37.06
REMARK 500 4 SER A 2 41.86 38.36
REMARK 500 4 SER A 6 -38.91 -37.79
REMARK 500 4 GLU A 13 49.35 -87.96
REMARK 500 4 ASP A 25 148.34 -35.37
REMARK 500 4 PRO A 27 -174.27 -69.80
REMARK 500 4 PRO A 29 3.04 -69.78
REMARK 500 5 PRO A 10 80.02 -69.82
REMARK 500 5 ASN A 11 109.99 -49.07
REMARK 500 5 GLU A 13 33.84 -85.25
REMARK 500 5 VAL A 22 99.21 -61.63
REMARK 500 5 PRO A 27 -175.09 -69.76
REMARK 500 5 PRO A 29 1.14 -69.74
REMARK 500 6 PRO A 10 3.00 -69.80
REMARK 500 6 ASN A 11 143.21 -33.32
REMARK 500 6 PRO A 12 2.50 -69.67
REMARK 500 6 GLU A 13 87.05 -50.65
REMARK 500 6 ASP A 25 144.55 -36.36
REMARK 500 6 PRO A 29 2.86 -69.78
REMARK 500 6 ARG A 72 99.01 -67.12
REMARK 500 6 PRO A 76 -178.16 -69.78
REMARK 500 7 PRO A 10 80.10 -69.68
REMARK 500 7 PRO A 12 0.24 -69.80
REMARK 500 7 ASP A 25 139.96 -34.99
REMARK 500 7 PRO A 27 -174.67 -69.74
REMARK 500 7 PRO A 29 5.15 -69.73
REMARK 500 7 ARG A 37 156.55 -49.77
REMARK 500 7 SER A 77 -55.66 -125.94
REMARK 500 8 ASP A 16 -179.47 -64.35
REMARK 500
REMARK 500 THIS ENTRY HAS 149 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002007132.1 RELATED DB: TARGETDB
DBREF 2CUD A 8 73 UNP Q13239 SLAP1_HUMAN 14 79
SEQADV 2CUD GLY A 1 UNP Q13239 CLONING ARTIFACT
SEQADV 2CUD SER A 2 UNP Q13239 CLONING ARTIFACT
SEQADV 2CUD SER A 3 UNP Q13239 CLONING ARTIFACT
SEQADV 2CUD GLY A 4 UNP Q13239 CLONING ARTIFACT
SEQADV 2CUD SER A 5 UNP Q13239 CLONING ARTIFACT
SEQADV 2CUD SER A 6 UNP Q13239 CLONING ARTIFACT
SEQADV 2CUD GLY A 7 UNP Q13239 CLONING ARTIFACT
SEQADV 2CUD SER A 74 UNP Q13239 CLONING ARTIFACT
SEQADV 2CUD GLY A 75 UNP Q13239 CLONING ARTIFACT
SEQADV 2CUD PRO A 76 UNP Q13239 CLONING ARTIFACT
SEQADV 2CUD SER A 77 UNP Q13239 CLONING ARTIFACT
SEQADV 2CUD SER A 78 UNP Q13239 CLONING ARTIFACT
SEQADV 2CUD GLY A 79 UNP Q13239 CLONING ARTIFACT
SEQRES 1 A 79 GLY SER SER GLY SER SER GLY PRO LEU PRO ASN PRO GLU
SEQRES 2 A 79 GLY LEU ASP SER ASP PHE LEU ALA VAL LEU SER ASP TYR
SEQRES 3 A 79 PRO SER PRO ASP ILE SER PRO PRO ILE PHE ARG ARG GLY
SEQRES 4 A 79 GLU LYS LEU ARG VAL ILE SER ASP GLU GLY GLY TRP TRP
SEQRES 5 A 79 LYS ALA ILE SER LEU SER THR GLY ARG GLU SER TYR ILE
SEQRES 6 A 79 PRO GLY ILE CYS VAL ALA ARG VAL SER GLY PRO SER SER
SEQRES 7 A 79 GLY
HELIX 1 1 GLY A 67 CYS A 69 5 3
SHEET 1 A 5 GLU A 62 PRO A 66 0
SHEET 2 A 5 TRP A 51 SER A 56 -1 N ALA A 54 O SER A 63
SHEET 3 A 5 LYS A 41 GLU A 48 -1 N ILE A 45 O LYS A 53
SHEET 4 A 5 PHE A 19 VAL A 22 -1 N LEU A 20 O LEU A 42
SHEET 5 A 5 VAL A 70 VAL A 73 -1 O ALA A 71 N ALA A 21
CISPEP 1 TYR A 26 PRO A 27 1 -0.06
CISPEP 2 TYR A 26 PRO A 27 2 -0.07
CISPEP 3 TYR A 26 PRO A 27 3 -0.05
CISPEP 4 TYR A 26 PRO A 27 4 0.02
CISPEP 5 TYR A 26 PRO A 27 5 0.00
CISPEP 6 TYR A 26 PRO A 27 6 -0.04
CISPEP 7 TYR A 26 PRO A 27 7 -0.07
CISPEP 8 TYR A 26 PRO A 27 8 -0.05
CISPEP 9 TYR A 26 PRO A 27 9 -0.05
CISPEP 10 TYR A 26 PRO A 27 10 0.02
CISPEP 11 TYR A 26 PRO A 27 11 -0.02
CISPEP 12 TYR A 26 PRO A 27 12 -0.06
CISPEP 13 TYR A 26 PRO A 27 13 -0.11
CISPEP 14 TYR A 26 PRO A 27 14 -0.06
CISPEP 15 TYR A 26 PRO A 27 15 -0.10
CISPEP 16 TYR A 26 PRO A 27 16 -0.05
CISPEP 17 TYR A 26 PRO A 27 17 -0.04
CISPEP 18 TYR A 26 PRO A 27 18 -0.01
CISPEP 19 TYR A 26 PRO A 27 19 -0.08
CISPEP 20 TYR A 26 PRO A 27 20 -0.03
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 - r 9 2 Bytes