Header list of 1by1.pdb file
Complete list - b 16 2 Bytes
HEADER TRANSPORT PROTEIN 22-OCT-98 1BY1
TITLE DBL HOMOLOGY DOMAIN FROM BETA-PIX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (PIX);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DBL HOMOLOGY 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS RHO-GTPASE EXCHANGE FACTOR, TRANSPORT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.AGHAZADEH,K.ZHU,T.J.KUBISESKI,G.A.LIU,T.PAWSON,Y.ZHENG,M.K.ROSEN
REVDAT 4 16-FEB-22 1BY1 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1BY1 1 VERSN
REVDAT 2 29-MAR-05 1BY1 1 JRNL
REVDAT 1 24-OCT-99 1BY1 0
JRNL AUTH B.AGHAZADEH,K.ZHU,T.J.KUBISESKI,G.A.LIU,T.PAWSON,Y.ZHENG,
JRNL AUTH 2 M.K.ROSEN
JRNL TITL STRUCTURE AND MUTAGENESIS OF THE DBL HOMOLOGY DOMAIN
JRNL REF NAT.STRUCT.BIOL. V. 5 1098 1998
JRNL REFN ISSN 1072-8368
JRNL PMID 9846881
JRNL DOI 10.1038/4209
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.3, X-PLOR 3.851
REMARK 3 AUTHORS : A.BRUNGER, M.NILGES
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: X-PLOR 3.851 WAS USED IN COMBINATION
REMARK 3 WITH ARIA (REF. M. NILGES)
REMARK 4
REMARK 4 1BY1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1000007323.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 311
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 150MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY TOCSY 2D; NOESY TOCSY 3D
REMARK 210 THROUGH BOND TRANSFER EXPERIMENTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW, ARIA, X-PLOR,
REMARK 210 CNS
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING A COMBINATION OF TRIPLE
REMARK 210 - AND QUADRUPLE- RESONANCE NMR EXPERIMENTS ON 13C/ 15N AND
REMARK 210 PARTIALLY OR FULLY DEUTERATED SAMPLES WITH SELECTIVE METHYL
REMARK 210 LABELING AT VALINE,LEUCINE AND ISOLEUCINES.
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 PHE A 67 H LEU A 71 1.53
REMARK 500 O LEU A 22 H ASN A 26 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 ASP A 5 -33.00 173.97
REMARK 500 1 ASN A 10 111.58 166.20
REMARK 500 1 THR A 34 -71.36 -66.87
REMARK 500 1 LEU A 36 -71.56 -51.74
REMARK 500 1 GLU A 47 -73.25 -43.84
REMARK 500 1 LEU A 49 40.43 -104.65
REMARK 500 1 SER A 50 -82.58 -58.98
REMARK 500 1 ALA A 52 -65.47 68.85
REMARK 500 1 TYR A 56 -86.89 -85.99
REMARK 500 1 LEU A 57 -67.42 -90.68
REMARK 500 1 ASN A 60 -74.05 -89.96
REMARK 500 1 PRO A 82 84.95 -36.11
REMARK 500 1 ALA A 84 -64.06 68.99
REMARK 500 1 GLN A 85 41.09 -152.18
REMARK 500 1 GLN A 86 172.35 -48.17
REMARK 500 1 ARG A 87 99.48 -169.12
REMARK 500 1 PRO A 97 -34.64 -39.27
REMARK 500 1 LEU A 117 -73.10 -61.20
REMARK 500 1 GLU A 129 -90.28 -59.16
REMARK 500 1 THR A 130 26.08 46.10
REMARK 500 1 LYS A 131 -63.71 164.65
REMARK 500 1 ALA A 133 -174.82 -62.15
REMARK 500 1 SER A 134 -156.08 -62.13
REMARK 500 1 PRO A 136 49.58 -72.45
REMARK 500 1 LEU A 141 -81.26 -49.05
REMARK 500 1 HIS A 165 -67.34 68.84
REMARK 500 1 GLU A 167 -82.85 65.86
REMARK 500 1 ASP A 168 178.90 64.98
REMARK 500 1 TYR A 169 -38.97 -179.24
REMARK 500 1 THR A 171 -163.19 -170.56
REMARK 500 1 ASP A 172 -67.23 69.10
REMARK 500 1 ARG A 196 102.74 -43.98
REMARK 500 1 LEU A 201 59.31 38.34
REMARK 500 1 GLN A 202 -56.81 -121.23
REMARK 500 1 THR A 205 57.69 -160.29
REMARK 500 1 ALA A 207 43.35 -106.94
REMARK 500 2 LYS A 2 -69.78 67.31
REMARK 500 2 ASP A 5 36.07 -173.18
REMARK 500 2 ILE A 9 132.74 54.60
REMARK 500 2 LYS A 11 -48.75 -161.61
REMARK 500 2 THR A 34 -73.31 -64.53
REMARK 500 2 GLU A 47 -80.29 -46.64
REMARK 500 2 SER A 50 -157.73 -57.39
REMARK 500 2 SER A 51 159.64 -43.31
REMARK 500 2 ALA A 52 -57.99 75.07
REMARK 500 2 TYR A 56 -90.09 -88.22
REMARK 500 2 LEU A 57 -77.45 -90.12
REMARK 500 2 ASN A 60 -71.91 -91.50
REMARK 500 2 LEU A 81 -174.00 -57.41
REMARK 500 2 PRO A 82 61.72 -66.71
REMARK 500
REMARK 500 THIS ENTRY HAS 709 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BY1 A 1 209 UNP Q14155 ARHG7_HUMAN 81 289
SEQADV 1BY1 MET A 1 UNP Q14155 PRO 81 CLONING ARTIFACT
SEQRES 1 A 209 MET LYS GLY PHE ASP THR THR ALA ILE ASN LYS SER TYR
SEQRES 2 A 209 TYR ASN VAL VAL LEU GLN ASN ILE LEU GLU THR GLU ASN
SEQRES 3 A 209 GLU TYR SER LYS GLU LEU GLN THR VAL LEU SER THR TYR
SEQRES 4 A 209 LEU ARG PRO LEU GLN THR SER GLU LYS LEU SER SER ALA
SEQRES 5 A 209 ASN ILE SER TYR LEU MET GLY ASN LEU GLU GLU ILE CYS
SEQRES 6 A 209 SER PHE GLN GLN MET LEU VAL GLN SER LEU GLU GLU CYS
SEQRES 7 A 209 THR LYS LEU PRO GLU ALA GLN GLN ARG VAL GLY GLY CYS
SEQRES 8 A 209 PHE LEU ASN LEU MET PRO GLN MET LYS THR LEU TYR LEU
SEQRES 9 A 209 THR TYR CYS ALA ASN HIS PRO SER ALA VAL ASN VAL LEU
SEQRES 10 A 209 THR GLU HIS SER GLU GLU LEU GLY GLU PHE MET GLU THR
SEQRES 11 A 209 LYS GLY ALA SER SER PRO GLY ILE LEU VAL LEU THR THR
SEQRES 12 A 209 GLY LEU SER LYS PRO PHE MET ARG LEU ASP LYS TYR PRO
SEQRES 13 A 209 THR LEU LEU LYS GLU LEU GLU ARG HIS MET GLU ASP TYR
SEQRES 14 A 209 HIS THR ASP ARG GLN ASP ILE GLN LYS SER MET ALA ALA
SEQRES 15 A 209 PHE LYS ASN LEU SER ALA GLN CYS GLN GLU VAL ARG LYS
SEQRES 16 A 209 ARG LYS GLU LEU GLU LEU GLN ILE LEU THR GLU ALA ILE
SEQRES 17 A 209 ARG
HELIX 1 1 TYR A 13 THR A 45 1 33
HELIX 2 2 ASN A 53 TYR A 56 1 4
HELIX 3 3 MET A 58 LYS A 80 1 23
HELIX 4 4 VAL A 88 HIS A 120 1 33
HELIX 5 5 LEU A 124 PHE A 127 1 4
HELIX 6 6 VAL A 140 LYS A 147 1 8
HELIX 7 7 ARG A 151 ARG A 164 5 14
HELIX 8 8 ARG A 173 LYS A 195 5 23
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