Header list of 2crr.pdb file
Complete list - r 9 2 Bytes
HEADER PROTEIN TRANSPORT 20-MAY-05 2CRR
TITLE SOLUTION STRUCTURE OF ARFGAP DOMAIN FROM HUMAN SMAP1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STROMAL MEMBRANE-ASSOCIATED PROTEIN SMAP1B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ARFGAP DOMAIN;
COMPND 5 SYNONYM: SMAP1, HYPOTHETICAL PROTEIN OTTHUMP00000039271;
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: OTTHUMP00000039271, GD:RP1-104A17.1-001, RP1-104A17.1-004;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040628-12;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS ARFGAP DOMAIN, SMAP1, ZINC FINGER, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, PROTEIN
KEYWDS 4 TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.SUETAKE,M.SATO,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CRR 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2CRR 1 VERSN
REVDAT 1 20-NOV-05 2CRR 0
JRNL AUTH T.SUETAKE,M.SATO,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF ARFGAP DOMAIN FROM HUMAN SMAP1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 2.0.17
REMARK 3 AUTHORS : VARIAN (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CRR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024551.
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 : 100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.27MM 13C, 15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS-HCL; 100MM NACL; 2MM
REMARK 210 D10-DTT; 0.02% NAN3; 0.01MM
REMARK 210 ZNCL2; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.927, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATION, TARGET
REMARK 210 FUNCTION
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 LYS A 8 43.40 -108.55
REMARK 500 1 LEU A 12 43.25 -80.96
REMARK 500 1 CYS A 32 159.38 -46.03
REMARK 500 1 ASP A 34 -68.19 -131.97
REMARK 500 1 ALA A 37 -179.16 -63.04
REMARK 500 1 PRO A 40 86.83 -69.78
REMARK 500 1 ARG A 41 -75.67 -62.71
REMARK 500 1 TRP A 42 163.00 -47.35
REMARK 500 1 ASN A 46 -37.07 -38.99
REMARK 500 1 MET A 88 -71.75 -96.81
REMARK 500 1 THR A 91 -71.54 -43.26
REMARK 500 1 GLU A 98 33.72 -84.53
REMARK 500 1 GLN A 112 -35.41 -34.73
REMARK 500 1 TYR A 127 38.66 -84.74
REMARK 500 2 SER A 3 42.14 -94.68
REMARK 500 2 LEU A 12 45.77 -80.22
REMARK 500 2 ASP A 34 -59.13 -134.12
REMARK 500 2 PRO A 40 81.50 -69.75
REMARK 500 2 ARG A 41 -70.57 -56.66
REMARK 500 2 TRP A 42 173.01 -55.07
REMARK 500 2 MET A 88 -73.09 -76.27
REMARK 500 2 ALA A 93 -38.69 -38.42
REMARK 500 2 LEU A 96 -68.25 -108.36
REMARK 500 2 GLU A 98 34.91 -83.70
REMARK 500 2 TYR A 127 38.58 -84.39
REMARK 500 3 SER A 2 147.39 -170.80
REMARK 500 3 SER A 6 92.79 -47.98
REMARK 500 3 LEU A 12 48.04 -80.67
REMARK 500 3 GLU A 14 44.15 -80.34
REMARK 500 3 CYS A 32 161.93 -41.88
REMARK 500 3 ASP A 34 -54.36 -131.47
REMARK 500 3 PRO A 40 81.57 -69.74
REMARK 500 3 ARG A 41 -76.74 -58.36
REMARK 500 3 TRP A 42 168.33 -46.83
REMARK 500 3 MET A 88 -73.79 -63.08
REMARK 500 3 THR A 91 -72.00 -49.65
REMARK 500 3 GLU A 98 35.55 -84.85
REMARK 500 3 ASN A 104 35.78 -96.51
REMARK 500 3 TYR A 122 -61.22 -103.95
REMARK 500 3 TYR A 127 38.24 -82.23
REMARK 500 4 LYS A 8 41.84 -81.33
REMARK 500 4 ALA A 9 41.59 -103.47
REMARK 500 4 GLU A 14 46.94 -89.95
REMARK 500 4 CYS A 32 162.90 -46.64
REMARK 500 4 ASP A 34 -55.76 -134.30
REMARK 500 4 ALA A 37 177.28 -55.41
REMARK 500 4 PRO A 40 86.84 -69.71
REMARK 500 4 ARG A 41 -75.31 -65.35
REMARK 500 4 TRP A 42 171.28 -50.73
REMARK 500 4 MET A 88 -74.40 -74.52
REMARK 500
REMARK 500 THIS ENTRY HAS 273 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 32 SG
REMARK 620 2 CYS A 35 SG 110.5
REMARK 620 3 CYS A 52 SG 119.5 95.3
REMARK 620 4 CYS A 55 SG 116.9 112.9 99.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001000987.1 RELATED DB: TARGETDB
DBREF 2CRR A 8 135 UNP Q6PK24 Q6PK24_HUMAN 9 136
SEQADV 2CRR GLY A 1 UNP Q6PK24 CLONING ARTIFACT
SEQADV 2CRR SER A 2 UNP Q6PK24 CLONING ARTIFACT
SEQADV 2CRR SER A 3 UNP Q6PK24 CLONING ARTIFACT
SEQADV 2CRR GLY A 4 UNP Q6PK24 CLONING ARTIFACT
SEQADV 2CRR SER A 5 UNP Q6PK24 CLONING ARTIFACT
SEQADV 2CRR SER A 6 UNP Q6PK24 CLONING ARTIFACT
SEQADV 2CRR GLY A 7 UNP Q6PK24 CLONING ARTIFACT
SEQADV 2CRR SER A 136 UNP Q6PK24 CLONING ARTIFACT
SEQADV 2CRR GLY A 137 UNP Q6PK24 CLONING ARTIFACT
SEQADV 2CRR PRO A 138 UNP Q6PK24 CLONING ARTIFACT
SEQADV 2CRR SER A 139 UNP Q6PK24 CLONING ARTIFACT
SEQADV 2CRR SER A 140 UNP Q6PK24 CLONING ARTIFACT
SEQADV 2CRR GLY A 141 UNP Q6PK24 CLONING ARTIFACT
SEQRES 1 A 141 GLY SER SER GLY SER SER GLY LYS ALA GLN LYS LEU ASN
SEQRES 2 A 141 GLU GLN HIS GLN LEU ILE LEU SER LYS LEU LEU ARG GLU
SEQRES 3 A 141 GLU ASP ASN LYS TYR CYS ALA ASP CYS GLU ALA LYS GLY
SEQRES 4 A 141 PRO ARG TRP ALA SER TRP ASN ILE GLY VAL PHE ILE CYS
SEQRES 5 A 141 ILE ARG CYS ALA GLY ILE HIS ARG ASN LEU GLY VAL HIS
SEQRES 6 A 141 ILE SER ARG VAL LYS SER VAL ASN LEU ASP GLN TRP THR
SEQRES 7 A 141 ALA GLU GLN ILE GLN CYS MET GLN ASP MET GLY ASN THR
SEQRES 8 A 141 LYS ALA ARG LEU LEU TYR GLU ALA ASN LEU PRO GLU ASN
SEQRES 9 A 141 PHE ARG ARG PRO GLN THR ASP GLN ALA VAL GLU PHE PHE
SEQRES 10 A 141 ILE ARG ASP LYS TYR GLU LYS LYS LYS TYR TYR ASP LYS
SEQRES 11 A 141 ASN ALA ILE ALA ILE SER GLY PRO SER SER GLY
HET ZN A 401 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 GLN A 15 GLU A 26 1 12
HELIX 2 2 GLU A 27 LYS A 30 5 4
HELIX 3 3 CYS A 52 GLY A 63 1 12
HELIX 4 4 THR A 78 MET A 88 1 11
HELIX 5 5 MET A 88 TYR A 97 1 10
HELIX 6 6 GLU A 98 ASN A 100 5 3
HELIX 7 7 THR A 110 GLU A 123 1 14
HELIX 8 8 LYS A 130 ALA A 134 5 5
SHEET 1 A 2 ALA A 43 SER A 44 0
SHEET 2 A 2 VAL A 49 PHE A 50 -1 O VAL A 49 N SER A 44
LINK SG CYS A 32 ZN ZN A 401 1555 1555 2.34
LINK SG CYS A 35 ZN ZN A 401 1555 1555 2.37
LINK SG CYS A 52 ZN ZN A 401 1555 1555 2.31
LINK SG CYS A 55 ZN ZN A 401 1555 1555 2.36
SITE 1 AC1 4 CYS A 32 CYS A 35 CYS A 52 CYS A 55
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