Header list of 1adr.pdb file
Complete list - b 16 2 Bytes
HEADER TRANSCRIPTION REGULATION 19-JUL-93 1ADR
TITLE DETERMINATION OF THE NUCLEAR MAGNETIC RESONANCE STRUCTURE OF THE DNA-
TITLE 2 BINDING DOMAIN OF THE P22 C2 REPRESSOR (1-76) IN SOLUTION AND
TITLE 3 COMPARISON WITH THE DNA-BINDING DOMAIN OF THE 434 REPRESSOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: P22 C2 REPRESSOR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE P22;
SOURCE 3 ORGANISM_TAXID: 10754
KEYWDS TRANSCRIPTION REGULATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.SEVILLASIERRA,G.OTTING,K.WUTHRICH
REVDAT 3 16-FEB-22 1ADR 1 REMARK
REVDAT 2 24-FEB-09 1ADR 1 VERSN
REVDAT 1 31-JAN-94 1ADR 0
JRNL AUTH P.SEVILLA-SIERRA,G.OTTING,K.WUTHRICH
JRNL TITL DETERMINATION OF THE NUCLEAR MAGNETIC RESONANCE STRUCTURE OF
JRNL TITL 2 THE DNA-BINDING DOMAIN OF THE P22 C2 REPRESSOR (1 TO 76) IN
JRNL TITL 3 SOLUTION AND COMPARISON WITH THE DNA-BINDING DOMAIN OF THE
JRNL TITL 4 434 REPRESSOR.
JRNL REF J.MOL.BIOL. V. 235 1003 1994
JRNL REFN ISSN 0022-2836
JRNL PMID 8289306
JRNL DOI 10.1006/JMBI.1994.1053
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : OPAL
REMARK 3 AUTHORS : P.LUGINBUHL,P.GUNTERT,M.BILLETER,K.WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ADR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170692.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 3 TYR A 63 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 8 ARG A 13 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 12 TYR A 63 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 13 ARG A 40 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 18 ARG A 11 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 20 ARG A 9 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
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 ASN A 2 161.80 68.65
REMARK 500 1 GLN A 4 146.80 62.66
REMARK 500 1 LYS A 18 39.81 77.00
REMARK 500 1 ASP A 68 50.55 -115.36
REMARK 500 1 SER A 70 -143.60 -147.64
REMARK 500 1 GLN A 71 46.11 -155.73
REMARK 500 1 ASN A 73 84.53 51.44
REMARK 500 2 ASN A 2 53.68 -159.73
REMARK 500 2 THR A 3 158.44 67.65
REMARK 500 2 GLN A 4 71.60 60.96
REMARK 500 2 PRO A 45 -177.29 -67.61
REMARK 500 2 LYS A 66 64.66 -167.64
REMARK 500 2 LEU A 69 9.85 -67.49
REMARK 500 2 SER A 70 96.07 -68.68
REMARK 500 2 ASN A 73 148.81 73.59
REMARK 500 2 VAL A 74 73.38 58.97
REMARK 500 3 ASN A 2 106.59 -51.39
REMARK 500 3 GLN A 4 -177.21 64.98
REMARK 500 3 LYS A 18 47.64 83.47
REMARK 500 3 ARG A 40 83.54 -161.98
REMARK 500 3 SER A 41 -95.36 -148.16
REMARK 500 3 GLU A 42 -42.13 -137.93
REMARK 500 3 LYS A 66 61.79 -169.14
REMARK 500 3 GLN A 71 30.79 -86.87
REMARK 500 3 THR A 72 96.52 -67.06
REMARK 500 3 ASN A 73 12.69 80.10
REMARK 500 4 ASN A 2 179.57 59.28
REMARK 500 4 THR A 3 37.85 -145.96
REMARK 500 4 LYS A 18 45.90 75.21
REMARK 500 4 ASP A 68 -163.17 90.29
REMARK 500 4 LEU A 69 -37.72 -178.35
REMARK 500 4 SER A 70 164.64 88.57
REMARK 500 4 GLN A 71 16.87 51.01
REMARK 500 5 THR A 3 88.81 -157.19
REMARK 500 5 LEU A 5 179.00 60.74
REMARK 500 5 SER A 41 29.57 106.04
REMARK 500 5 SER A 70 117.33 67.68
REMARK 500 5 ASN A 73 102.48 -45.54
REMARK 500 6 ASN A 2 159.29 70.63
REMARK 500 6 LEU A 5 117.66 64.83
REMARK 500 6 LYS A 18 38.84 75.71
REMARK 500 6 SER A 41 46.16 36.11
REMARK 500 6 GLN A 58 70.87 42.37
REMARK 500 6 ASP A 68 80.70 48.51
REMARK 500 6 SER A 70 158.12 178.28
REMARK 500 6 GLN A 71 20.17 -143.01
REMARK 500 6 ASN A 73 87.35 58.33
REMARK 500 6 VAL A 74 79.44 73.93
REMARK 500 7 GLN A 4 119.62 57.08
REMARK 500 7 LYS A 18 43.56 78.93
REMARK 500
REMARK 500 THIS ENTRY HAS 145 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 MET A 1 ASN A 2 4 -137.29
REMARK 500 MET A 1 ASN A 2 6 -140.83
REMARK 500 SER A 41 GLU A 42 8 -116.69
REMARK 500 ALA A 75 TYR A 76 11 -147.49
REMARK 500 VAL A 74 ALA A 75 15 -146.76
REMARK 500 MET A 1 ASN A 2 17 141.40
REMARK 500 MET A 1 ASN A 2 18 -148.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 13 0.10 SIDE CHAIN
REMARK 500 1 TYR A 63 0.07 SIDE CHAIN
REMARK 500 1 TYR A 76 0.08 SIDE CHAIN
REMARK 500 2 ARG A 9 0.08 SIDE CHAIN
REMARK 500 2 ARG A 13 0.08 SIDE CHAIN
REMARK 500 2 TYR A 63 0.21 SIDE CHAIN
REMARK 500 3 ARG A 9 0.08 SIDE CHAIN
REMARK 500 3 ARG A 40 0.09 SIDE CHAIN
REMARK 500 3 TYR A 63 0.08 SIDE CHAIN
REMARK 500 4 ARG A 9 0.10 SIDE CHAIN
REMARK 500 4 ARG A 13 0.14 SIDE CHAIN
REMARK 500 4 ARG A 14 0.08 SIDE CHAIN
REMARK 500 4 TYR A 63 0.09 SIDE CHAIN
REMARK 500 5 TYR A 63 0.15 SIDE CHAIN
REMARK 500 6 ARG A 13 0.10 SIDE CHAIN
REMARK 500 6 ARG A 40 0.10 SIDE CHAIN
REMARK 500 6 TYR A 63 0.08 SIDE CHAIN
REMARK 500 7 ARG A 40 0.11 SIDE CHAIN
REMARK 500 7 TYR A 63 0.12 SIDE CHAIN
REMARK 500 8 ARG A 9 0.29 SIDE CHAIN
REMARK 500 8 ARG A 13 0.08 SIDE CHAIN
REMARK 500 9 ARG A 9 0.14 SIDE CHAIN
REMARK 500 9 ARG A 40 0.08 SIDE CHAIN
REMARK 500 10 ARG A 9 0.11 SIDE CHAIN
REMARK 500 10 ARG A 13 0.09 SIDE CHAIN
REMARK 500 10 ARG A 40 0.11 SIDE CHAIN
REMARK 500 10 TYR A 76 0.12 SIDE CHAIN
REMARK 500 11 ARG A 9 0.11 SIDE CHAIN
REMARK 500 12 ARG A 14 0.08 SIDE CHAIN
REMARK 500 12 ARG A 20 0.11 SIDE CHAIN
REMARK 500 12 TYR A 63 0.14 SIDE CHAIN
REMARK 500 13 ARG A 9 0.11 SIDE CHAIN
REMARK 500 13 ARG A 14 0.12 SIDE CHAIN
REMARK 500 14 ARG A 9 0.11 SIDE CHAIN
REMARK 500 15 ARG A 14 0.08 SIDE CHAIN
REMARK 500 16 ARG A 14 0.08 SIDE CHAIN
REMARK 500 16 TYR A 63 0.09 SIDE CHAIN
REMARK 500 17 ARG A 9 0.24 SIDE CHAIN
REMARK 500 18 ARG A 9 0.10 SIDE CHAIN
REMARK 500 18 ARG A 11 0.10 SIDE CHAIN
REMARK 500 18 ARG A 13 0.12 SIDE CHAIN
REMARK 500 18 ARG A 14 0.11 SIDE CHAIN
REMARK 500 18 TYR A 63 0.11 SIDE CHAIN
REMARK 500 18 TYR A 76 0.07 SIDE CHAIN
REMARK 500 19 ARG A 13 0.12 SIDE CHAIN
REMARK 500 19 ARG A 14 0.12 SIDE CHAIN
REMARK 500 20 ARG A 9 0.14 SIDE CHAIN
REMARK 500 20 TYR A 63 0.12 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ADR A 1 76 UNP P69202 RPC2_BPP22 1 76
SEQRES 1 A 76 MET ASN THR GLN LEU MET GLY GLU ARG ILE ARG ALA ARG
SEQRES 2 A 76 ARG LYS LYS LEU LYS ILE ARG GLN ALA ALA LEU GLY LYS
SEQRES 3 A 76 MET VAL GLY VAL SER ASN VAL ALA ILE SER GLN TRP GLU
SEQRES 4 A 76 ARG SER GLU THR GLU PRO ASN GLY GLU ASN LEU LEU ALA
SEQRES 5 A 76 LEU SER LYS ALA LEU GLN CYS SER PRO ASP TYR LEU LEU
SEQRES 6 A 76 LYS GLY ASP LEU SER GLN THR ASN VAL ALA TYR
HELIX 1 A1 MET A 6 LEU A 17 1 12
HELIX 2 A2 GLN A 21 VAL A 28 1 8
HELIX 3 A3 ASN A 32 GLU A 39 1 8
HELIX 4 A4 GLY A 47 LEU A 57 1 11
HELIX 5 A5 PRO A 61 LEU A 65 1 5
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