Header list of 1bc9.pdb file
Complete list - 16 20 Bytes
HEADER EXCHANGE FACTOR 06-MAY-98 1BC9
TITLE CYTOHESIN-1/B2-1 SEC7 DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOHESIN-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEC7 DOMAIN,;
COMPND 5 SYNONYM: B2-1, SEC7 HOMOLOG B2-1;
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 CELL_LINE: BL21;
SOURCE 6 ORGAN: SPLEEN;
SOURCE 7 GENE: B2-1;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET-20B;
SOURCE 13 EXPRESSION_SYSTEM_GENE: B2-1
KEYWDS EXCHANGE FACTOR, INTEGRIN BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR S.F.BETZ,A.SCHNUCHEL,H.WANG,E.T.OLEJNICZAK,R.P.MEADOWS,S.W.FESIK
REVDAT 4 16-FEB-22 1BC9 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1BC9 1 VERSN
REVDAT 2 01-APR-03 1BC9 1 JRNL
REVDAT 1 11-MAY-99 1BC9 0
JRNL AUTH S.F.BETZ,A.SCHNUCHEL,H.WANG,E.T.OLEJNICZAK,R.P.MEADOWS,
JRNL AUTH 2 B.P.LIPSKY,E.A.HARRIS,D.E.STAUNTON,S.W.FESIK
JRNL TITL SOLUTION STRUCTURE OF THE CYTOHESIN-1 (B2-1) SEC7 DOMAIN AND
JRNL TITL 2 ITS INTERACTION WITH THE GTPASE ADP RIBOSYLATION FACTOR 1.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 95 7909 1998
JRNL REFN ISSN 0027-8424
JRNL PMID 9653114
JRNL DOI 10.1073/PNAS.95.14.7909
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION.
REMARK 4
REMARK 4 1BC9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171582.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 305
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 0.47 M
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 20 MM NAPI, 150 MM (NH4)2SO4,
REMARK 210 3MM DTT, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA; HN(CO)CA; HN(CA)CB; HN
REMARK 210 (COCA)CB; HNCO; HN(CA)CO; HCCH-
REMARK 210 TOCSY; 13C-NOESY; 15N-NOESY;
REMARK 210 HNHA-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ; 800
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : DRX500; DRX600; AMX750; DRX800
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY/ SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 287
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMIZED AVERAGE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED CYTOHESIN-1 SEC7 DOMAIN.
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 ILE A 194 HG1 THR A 198 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 LYS A 58 97.15 -48.69
REMARK 500 ASP A 76 140.77 -170.27
REMARK 500 LYS A 78 -4.13 79.46
REMARK 500 ASN A 92 -165.35 -71.66
REMARK 500 GLU A 95 -74.69 -74.23
REMARK 500 PHE A 100 -71.64 -105.42
REMARK 500 LYS A 103 -68.35 -144.73
REMARK 500 GLU A 105 50.41 -108.95
REMARK 500 GLU A 118 -81.59 -140.97
REMARK 500 ARG A 119 -71.28 177.79
REMARK 500 ASP A 120 -166.58 45.44
REMARK 500 VAL A 131 57.52 -114.39
REMARK 500 GLU A 132 28.54 -154.52
REMARK 500 GLU A 135 73.26 42.66
REMARK 500 PHE A 136 28.55 -163.16
REMARK 500 LEU A 139 -75.13 -88.71
REMARK 500 ASN A 140 157.35 155.99
REMARK 500 PHE A 148 26.37 -161.21
REMARK 500 PHE A 152 -37.70 -175.88
REMARK 500 ARG A 153 127.53 74.49
REMARK 500 GLU A 157 -165.37 72.85
REMARK 500 ALA A 158 106.35 -47.63
REMARK 500 GLN A 159 -41.94 -178.33
REMARK 500 ASN A 176 -68.69 -128.11
REMARK 500 ASN A 177 82.46 71.76
REMARK 500 PHE A 180 41.83 -96.42
REMARK 500 GLN A 181 -72.62 73.16
REMARK 500 SER A 182 -78.22 -150.32
REMARK 500 THR A 183 -45.76 -152.87
REMARK 500 THR A 198 -71.03 -49.13
REMARK 500 HIS A 201 78.79 -115.20
REMARK 500 LYS A 206 99.59 -48.99
REMARK 500 ASP A 207 -56.02 -136.17
REMARK 500 LYS A 208 64.45 71.58
REMARK 500 ASP A 226 -58.77 76.93
REMARK 500 LEU A 227 122.03 63.27
REMARK 500 PRO A 243 -154.40 -55.01
REMARK 500 PHE A 244 152.71 70.01
REMARK 500 LYS A 245 -137.54 -172.69
REMARK 500 ILE A 246 155.47 -36.23
REMARK 500 PRO A 247 176.05 -47.63
REMARK 500 HIS A 252 71.43 52.59
REMARK 500 HIS A 255 98.43 -44.41
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BC9 A 58 256 UNP Q15438 CYH1_HUMAN 58 256
SEQADV 1BC9 LEU A 249 UNP Q15438 ASP 249 CONFLICT
SEQADV 1BC9 GLU A 250 UNP Q15438 ASP 250 CONFLICT
SEQADV 1BC9 HIS A 251 UNP Q15438 GLY 251 CONFLICT
SEQADV 1BC9 HIS A 252 UNP Q15438 ASN 252 CONFLICT
SEQADV 1BC9 HIS A 253 UNP Q15438 ASP 253 CONFLICT
SEQADV 1BC9 HIS A 254 UNP Q15438 LEU 254 CONFLICT
SEQADV 1BC9 HIS A 255 UNP Q15438 THR 255 CONFLICT
SEQRES 1 A 200 MET LYS ASN MET GLN ARG ASN LYS GLN VAL ALA MET GLY
SEQRES 2 A 200 ARG LYS LYS PHE ASN MET ASP PRO LYS LYS GLY ILE GLN
SEQRES 3 A 200 PHE LEU ILE GLU ASN ASP LEU LEU LYS ASN THR CYS GLU
SEQRES 4 A 200 ASP ILE ALA GLN PHE LEU TYR LYS GLY GLU GLY LEU ASN
SEQRES 5 A 200 LYS THR ALA ILE GLY ASP TYR LEU GLY GLU ARG ASP GLU
SEQRES 6 A 200 PHE ASN ILE GLN VAL LEU HIS ALA PHE VAL GLU LEU HIS
SEQRES 7 A 200 GLU PHE THR ASP LEU ASN LEU VAL GLN ALA LEU ARG GLN
SEQRES 8 A 200 PHE LEU TRP SER PHE ARG LEU PRO GLY GLU ALA GLN LYS
SEQRES 9 A 200 ILE ASP ARG MET MET GLU ALA PHE ALA GLN ARG TYR CYS
SEQRES 10 A 200 GLN CYS ASN ASN GLY VAL PHE GLN SER THR ASP THR CYS
SEQRES 11 A 200 TYR VAL LEU SER PHE ALA ILE ILE MET LEU ASN THR SER
SEQRES 12 A 200 LEU HIS ASN PRO ASN VAL LYS ASP LYS PRO THR VAL GLU
SEQRES 13 A 200 ARG PHE ILE ALA MET ASN ARG GLY ILE ASN ASP GLY GLY
SEQRES 14 A 200 ASP LEU PRO GLU GLU LEU LEU ARG ASN LEU TYR GLU SER
SEQRES 15 A 200 ILE LYS ASN GLU PRO PHE LYS ILE PRO GLU LEU GLU HIS
SEQRES 16 A 200 HIS HIS HIS HIS HIS
HELIX 1 1 GLN A 61 MET A 75 1 15
HELIX 2 2 LYS A 78 GLU A 86 1 9
HELIX 3 3 CYS A 94 TYR A 102 1 9
HELIX 4 4 LYS A 109 TYR A 115 1 7
HELIX 5 5 GLU A 121 ALA A 129 1 9
HELIX 6 6 LEU A 141 ARG A 146 1 6
HELIX 7 7 LYS A 160 TYR A 172 1 13
HELIX 8 8 ASP A 184 LEU A 200 1 17
HELIX 9 9 VAL A 211 ILE A 221 1 11
HELIX 10 10 GLU A 229 ASN A 241 1 13
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
Complete list - 16 20 Bytes