Header list of 1v4r.pdb file
Complete list - r 2 2 Bytes
HEADER GENE REGULATION 17-NOV-03 1V4R
TITLE SOLUTION STRUCTURE OF STREPTMYCAL REPRESSOR TRAR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTIONAL REPRESSOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES;
SOURCE 3 ORGANISM_TAXID: 1883;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET24A, PSN22
KEYWDS HELIX-TURN-HELIX, WINGED-HELIX, GENE REGULATION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR T.TANAKA,C.KOMATSU,K.KOBAYASHI,M.SUGAI,M.KATAOKA,T.KOHNO
REVDAT 3 02-MAR-22 1V4R 1 REMARK
REVDAT 2 24-FEB-09 1V4R 1 VERSN
REVDAT 1 01-MAR-05 1V4R 0
JRNL AUTH T.TANAKA,C.KOMATSU,K.KOBAYASHI,M.SUGAI,M.KATAOKA,T.KOHNO
JRNL TITL SOLUTION STRUCTURE OF STREPTMYCAL REPRESSOR TRAR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ANSIG 3.3, X-PLOR 3.1
REMARK 3 AUTHORS : KRAULIS, P (ANSIG), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1V4R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000006204.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2MM TRAR U-15N,13C; 50MM
REMARK 210 PHOSPHATE BUFFER NA, 100MM NACL;
REMARK 210 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AZARA 2.7, X-PLOR 3.1, XWINNMR
REMARK 210 2.6
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 MATRIX RELAXATION, TORSION ANGLE
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 120
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 4
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-10
REMARK 465 RES C SSSEQI
REMARK 465 GLY A -1
REMARK 465 PRO A 0
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 HA LEU A 57 H GLY A 61 1.25
REMARK 500 HA ARG A 40 HE1 PHE A 43 1.27
REMARK 500 O ILE A 39 H PHE A 43 1.56
REMARK 500 HH11 ARG A 19 OE2 GLU A 60 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 LYS A 23 -75.93 -75.88
REMARK 500 1 GLU A 26 -15.20 111.79
REMARK 500 1 LEU A 27 58.50 -112.79
REMARK 500 1 LEU A 62 37.27 73.20
REMARK 500 1 ALA A 68 -63.89 -142.23
REMARK 500 1 LYS A 75 -85.59 -98.85
REMARK 500 1 VAL A 79 79.28 -55.30
REMARK 500 1 ARG A 88 111.23 66.53
REMARK 500 2 LEU A 62 66.70 63.04
REMARK 500 2 ALA A 68 -60.73 -160.87
REMARK 500 2 LYS A 75 88.55 -68.51
REMARK 500 2 ILE A 78 105.52 -55.70
REMARK 500 2 VAL A 79 72.00 65.85
REMARK 500 3 GLU A 7 -74.41 -99.66
REMARK 500 3 LEU A 33 109.69 -57.52
REMARK 500 3 ALA A 68 -16.69 -160.71
REMARK 500 3 LYS A 75 49.01 -84.87
REMARK 500 3 VAL A 79 43.50 33.90
REMARK 500 3 ARG A 88 -164.71 -76.98
REMARK 500 4 LEU A 62 80.33 69.74
REMARK 500 4 VAL A 79 91.60 -52.49
REMARK 500 4 LEU A 86 -89.88 57.18
REMARK 500 4 MET A 89 -55.51 70.23
REMARK 500 5 GLU A 7 -157.61 -86.95
REMARK 500 5 LEU A 27 72.77 -109.16
REMARK 500 5 LEU A 69 -62.10 -92.05
REMARK 500 5 LYS A 75 78.67 -69.18
REMARK 500 5 THR A 81 -54.88 -158.87
REMARK 500 5 LEU A 86 -81.65 59.45
REMARK 500 5 MET A 89 108.65 -58.13
REMARK 500 5 LYS A 91 79.38 -118.31
REMARK 500 5 MET A 94 52.83 -106.19
REMARK 500 6 LYS A 23 -81.04 -61.09
REMARK 500 6 LEU A 62 80.05 75.16
REMARK 500 6 ALA A 68 -68.30 -149.25
REMARK 500 6 LYS A 75 38.53 -79.22
REMARK 500 6 VAL A 79 74.82 -65.24
REMARK 500 6 LEU A 86 93.96 -68.98
REMARK 500 6 LYS A 87 -44.39 -161.99
REMARK 500 7 GLU A 7 -77.44 -69.33
REMARK 500 7 LYS A 23 -79.64 -66.06
REMARK 500 7 GLU A 26 9.79 59.53
REMARK 500 7 ALA A 68 -47.26 -160.23
REMARK 500 7 LYS A 75 92.73 -66.63
REMARK 500 8 PRO A 2 36.39 -86.22
REMARK 500 8 GLU A 7 -89.45 -93.23
REMARK 500 8 LEU A 62 78.28 63.29
REMARK 500 8 SER A 64 77.21 147.90
REMARK 500 8 THR A 81 -28.00 -142.53
REMARK 500 8 LYS A 87 -10.46 -157.91
REMARK 500
REMARK 500 THIS ENTRY HAS 71 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 35 VAL A 36 7 142.48
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1V4R A -1 100 PDB 1V4R 1V4R -1 100
SEQRES 1 A 102 GLY PRO MET PRO TYR LYS ALA PRO GLU GLY LYS GLY TYR
SEQRES 2 A 102 ALA ASP VAL ALA THR HIS PHE ARG THR LEU ILE LYS SER
SEQRES 3 A 102 GLY GLU LEU ALA PRO GLY ASP THR LEU PRO SER VAL ALA
SEQRES 4 A 102 ASP ILE ARG ALA GLN PHE GLY VAL ALA ALA LYS THR VAL
SEQRES 5 A 102 SER ARG ALA LEU ALA VAL LEU LYS SER GLU GLY LEU VAL
SEQRES 6 A 102 SER SER ARG GLY ALA LEU GLY THR VAL VAL GLU LYS ASN
SEQRES 7 A 102 PRO ILE VAL ILE THR GLY ALA ASP ARG LEU LYS ARG MET
SEQRES 8 A 102 GLU LYS ASN GLY MET ARG TYR ALA PRO GLY GLU
HELIX 1 1 GLY A 10 ILE A 22 1 13
HELIX 2 2 SER A 35 PHE A 43 1 9
HELIX 3 3 LYS A 48 LEU A 54 1 7
HELIX 4 4 GLY A 82 ARG A 88 1 7
SHEET 1 A 2 SER A 64 ARG A 66 0
SHEET 2 A 2 GLY A 70 VAL A 72 -1 N GLY A 70 O ARG A 66
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 2 2 Bytes