Header list of 1f5x.pdb file
Complete list - b 16 2 Bytes
HEADER SIGNALING PROTEIN 18-JUN-00 1F5X TITLE NMR STRUCTURE OF THE Y174 AUTOINHIBITED DBL HOMOLOGY DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: RHO-GEF VAV; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: DBL HOMOLOGY DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET11A KEYWDS 11 ALPHA-HELICES, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR B.AGHAZADEH,M.K.ROSEN,W.E.LOWRY,X.Y.HUANG REVDAT 4 16-FEB-22 1F5X 1 REMARK SEQADV REVDAT 3 24-FEB-09 1F5X 1 VERSN REVDAT 2 01-APR-03 1F5X 1 JRNL REVDAT 1 15-SEP-00 1F5X 0 JRNL AUTH B.AGHAZADEH,W.E.LOWRY,X.Y.HUANG,M.K.ROSEN JRNL TITL STRUCTURAL BASIS FOR RELIEF OF AUTOINHIBITION OF THE DBL JRNL TITL 2 HOMOLOGY DOMAIN OF PROTO-ONCOGENE VAV BY TYROSINE JRNL TITL 3 PHOSPHORYLATION. JRNL REF CELL(CAMBRIDGE,MASS.) V. 102 625 2000 JRNL REFN ISSN 0092-8674 JRNL PMID 11007481 JRNL DOI 10.1016/S0092-8674(00)00085-4 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 2.0, ARIA 1 REMARK 3 AUTHORS : VARIAN (VNMR), NILGES (ARIA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 CNS WAS USED IN THE INITIAL GLOBAL FOLD DETERMINATION. REMARK 3 HIGH-RESOLUTION STRUCTURES WERE OBTAINED USING ARIA. REMARK 3 FINAL STRUCTURES ARE BASED ON A TOTAL OF 3966 RESTRAINTS, REMARK 3 3523 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 443 DIHEDRAL REMARK 3 ANGLE RESTRAINTS, 96 DISTANCE RESTRAINTS REMARK 4 REMARK 4 1F5X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-00. REMARK 100 THE DEPOSITION ID IS D_1000011282. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7 REMARK 210 IONIC STRENGTH : 70 MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.4 MM 15N,13C,2H; 20 MM REMARK 210 PHOSPHATE BUFFER; 50 MM NACL; 90% REMARK 210 H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D_13C-SEPARATED_NOESY; REMARK 210 4D_13C/15N-SEPARATED_NOESY; 3D_ REMARK 210 15N-SEPARATED_NOESY; 3D_13C- REMARK 210 SEPARATED_NOESY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.0, NMRVIEW 2.1.2, CNS REMARK 210 0.3 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES REMARK 210 SUBMITTED REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 16 REMARK 210 REMARK 210 REMARK: REMARK 210 THIS STRUCTURE WAS DETERMINED USING 3D AND 4D HETERONUCLEAR REMARK 210 TECHNIQUES REMARK 210 ON DEUTERATED SAMPLES IN CONJUNCTION WITH SELECTIVE METHYL AND REMARK 210 AROMATIC LABELING 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 LEU A 199 H VAL A 203 1.56 REMARK 500 O LYS A 168 H LEU A 172 1.56 REMARK 500 O LEU A 87 H LEU A 91 1.57 REMARK 500 O ASP A 26 H CYS A 29 1.58 REMARK 500 O GLU A 24 H LYS A 27 1.60 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 ARG A 12 88.19 -54.55 REMARK 500 1 LEU A 13 -54.15 -143.39 REMARK 500 1 PRO A 20 94.38 -54.65 REMARK 500 1 LYS A 21 143.43 68.90 REMARK 500 1 MET A 22 122.97 72.73 REMARK 500 1 CYS A 31 -55.06 -25.06 REMARK 500 1 GLU A 40 -76.31 -46.08 REMARK 500 1 HIS A 52 63.88 -67.63 REMARK 500 1 PHE A 53 -71.29 169.91 REMARK 500 1 PHE A 60 -54.36 -132.22 REMARK 500 1 LYS A 62 153.20 -44.95 REMARK 500 1 VAL A 71 -115.64 83.84 REMARK 500 1 ASN A 149 104.59 -168.50 REMARK 500 1 ASN A 150 91.42 -44.47 REMARK 500 1 PHE A 153 19.91 -140.13 REMARK 500 1 THR A 154 148.53 -38.88 REMARK 500 1 LEU A 155 -74.82 11.06 REMARK 500 1 ARG A 156 -38.15 -38.62 REMARK 500 1 LEU A 158 -70.94 -72.06 REMARK 500 1 ARG A 165 -72.95 -51.61 REMARK 500 1 TYR A 169 -76.82 -49.29 REMARK 500 1 GLU A 187 -71.87 -93.92 REMARK 500 1 ASN A 204 32.98 -94.99 REMARK 500 1 GLU A 205 71.46 -153.26 REMARK 500 1 LYS A 207 -63.18 70.05 REMARK 500 2 GLU A 8 -70.42 -52.35 REMARK 500 2 PRO A 20 76.61 -60.47 REMARK 500 2 LYS A 21 -72.11 -163.43 REMARK 500 2 GLN A 50 -71.90 -66.06 REMARK 500 2 HIS A 52 62.04 -68.47 REMARK 500 2 PHE A 53 -75.21 167.35 REMARK 500 2 PHE A 60 -66.01 -127.89 REMARK 500 2 PHE A 70 56.72 -107.32 REMARK 500 2 VAL A 71 -94.85 -34.98 REMARK 500 2 ALA A 123 -71.04 -58.04 REMARK 500 2 GLU A 135 -63.68 -127.11 REMARK 500 2 ASN A 150 84.35 -56.17 REMARK 500 2 THR A 154 152.97 -39.63 REMARK 500 2 LEU A 155 -71.34 6.32 REMARK 500 2 ARG A 156 -32.27 -39.96 REMARK 500 2 LEU A 158 -70.29 -58.38 REMARK 500 2 TYR A 169 -76.92 -50.60 REMARK 500 2 ASP A 182 -160.70 -125.24 REMARK 500 2 ALA A 183 -70.78 -91.71 REMARK 500 2 ASN A 204 32.72 -98.99 REMARK 500 2 GLU A 205 41.40 -142.96 REMARK 500 2 LYS A 207 -64.47 66.66 REMARK 500 3 LEU A 13 28.81 -146.85 REMARK 500 3 PRO A 17 101.62 -52.07 REMARK 500 3 LYS A 21 170.69 -53.71 REMARK 500 REMARK 500 THIS ENTRY HAS 403 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1F5X A 1 208 UNP P27870 VAV_MOUSE 168 375 SEQADV 1F5X MET A 1 UNP P27870 ALA 168 CONFLICT SEQADV 1F5X LYS A 2 UNP P27870 GLU 169 CONFLICT SEQRES 1 A 208 MET LYS GLY ASP GLU ILE TYR GLU ASP LEU MET ARG LEU SEQRES 2 A 208 GLU SER VAL PRO THR PRO PRO LYS MET THR GLU TYR ASP SEQRES 3 A 208 LYS ARG CYS CYS CYS LEU ARG GLU ILE GLN GLN THR GLU SEQRES 4 A 208 GLU LYS TYR THR ASP THR LEU GLY SER ILE GLN GLN HIS SEQRES 5 A 208 PHE MET LYS PRO LEU GLN ARG PHE LEU LYS PRO GLN ASP SEQRES 6 A 208 MET GLU THR ILE PHE VAL ASN ILE GLU GLU LEU PHE SER SEQRES 7 A 208 VAL HIS THR HIS PHE LEU LYS GLU LEU LYS ASP ALA LEU SEQRES 8 A 208 ALA GLY PRO GLY ALA THR THR LEU TYR GLN VAL PHE ILE SEQRES 9 A 208 LYS TYR LYS GLU ARG PHE LEU VAL TYR GLY ARG TYR CYS SEQRES 10 A 208 SER GLN VAL GLU SER ALA SER LYS HIS LEU ASP GLN VAL SEQRES 11 A 208 ALA THR ALA ARG GLU ASP VAL GLN MET LYS LEU GLU GLU SEQRES 12 A 208 CYS SER GLN ARG ALA ASN ASN GLY ARG PHE THR LEU ARG SEQRES 13 A 208 ASP LEU LEU MET VAL PRO MET GLN ARG VAL LEU LYS TYR SEQRES 14 A 208 HIS LEU LEU LEU GLN GLU LEU VAL LYS HIS THR GLN ASP SEQRES 15 A 208 ALA THR GLU LYS GLU ASN LEU ARG LEU ALA LEU ASP ALA SEQRES 16 A 208 MET ARG ASP LEU ALA GLN CYS VAL ASN GLU VAL LYS ARG HELIX 1 1 LYS A 2 MET A 11 1 10 HELIX 2 2 THR A 23 TYR A 25 5 3 HELIX 3 3 ASP A 26 CYS A 31 1 6 HELIX 4 4 CYS A 30 GLY A 47 1 18 HELIX 5 5 PHE A 53 GLN A 58 1 6 HELIX 6 6 LYS A 62 PHE A 70 1 9 HELIX 7 7 ASN A 72 GLY A 93 1 22 HELIX 8 8 GLY A 95 THR A 97 5 3 HELIX 9 9 THR A 98 LYS A 105 1 8 HELIX 10 10 TYR A 106 LEU A 111 1 6 HELIX 11 11 LEU A 111 ARG A 134 1 24 HELIX 12 12 ARG A 134 GLN A 146 1 13 HELIX 13 13 VAL A 161 LYS A 178 1 18 HELIX 14 14 THR A 184 ASN A 204 1 21 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 16 2 Bytes