Header list of 2orc.pdb file
Complete list - r 16 2 Bytes
HEADER GENE REGULATING PROTEIN 20-JAN-98 2ORC
TITLE CRO REPRESSOR INSERTION MUTANT K56-[DGEVK], NMR, 32 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CRO REPRESSOR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: RESULTS IN A 71-RESIDUE STABLE MONOMER MUTANT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE LAMBDA;
SOURCE 3 ORGANISM_TAXID: 10710;
SOURCE 4 GENE: CRO MUTANT K56-[DGEVK];
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: X90;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PUCRO.MDG;
SOURCE 9 EXPRESSION_SYSTEM_GENE: CRO MUTANT K56-[DGEVK]
KEYWDS GENE REGULATING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 32
AUTHOR M.C.MOSSING
REVDAT 3 16-MAR-22 2ORC 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2ORC 1 VERSN
REVDAT 1 27-MAY-98 2ORC 0
JRNL AUTH M.C.MOSSING
JRNL TITL SOLUTION STRUCTURE AND DYNAMICS OF A DESIGNED MONOMERIC
JRNL TITL 2 VARIANT OF THE LAMBDA CRO REPRESSOR.
JRNL REF PROTEIN SCI. V. 7 983 1998
JRNL REFN ISSN 0961-8368
JRNL PMID 9568905
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.C.MOSSING,R.T.SAUER
REMARK 1 TITL STABLE, MONOMERIC VARIANTS OF LAMBDA CRO OBTAINED BY
REMARK 1 TITL 2 INSERTION OF A DESIGNED BETA-HAIRPIN SEQUENCE
REMARK 1 REF SCIENCE V. 250 1712 1990
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL REFERENCE.
REMARK 4
REMARK 4 2ORC 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_1000178426.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY; HSQC-NOESY;
REMARK 210 HSQC-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY/ SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 32
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO DISTANCE VIOLATION > 0.5A, NO
REMARK 210 DIHEDRAL VIOLATION > 5 DEGREES
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: 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
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 GLU A 2 -154.37 55.32
REMARK 500 1 GLN A 3 58.90 -95.72
REMARK 500 1 THR A 6 -174.78 -65.32
REMARK 500 1 PHE A 14 -77.36 -111.09
REMARK 500 1 ALA A 36 -88.13 -76.34
REMARK 500 1 ALA A 46 -19.59 91.01
REMARK 500 1 ASP A 56A 73.72 -4.38
REMARK 500 1 GLU A 56C 128.70 -178.92
REMARK 500 1 PHE A 58 109.99 56.35
REMARK 500 1 LYS A 62 64.43 178.99
REMARK 500 1 THR A 64 -77.27 -138.61
REMARK 500 2 GLU A 2 -156.42 57.84
REMARK 500 2 GLN A 3 65.16 -103.35
REMARK 500 2 THR A 6 -178.30 -51.06
REMARK 500 2 PHE A 14 -67.63 -98.52
REMARK 500 2 LYS A 39 66.83 71.29
REMARK 500 2 SER A 49 101.34 -48.86
REMARK 500 2 LYS A 56 110.41 -160.24
REMARK 500 2 GLU A 56C 98.20 -60.90
REMARK 500 2 VAL A 56D 61.01 -107.19
REMARK 500 2 LYS A 56E 174.90 -58.93
REMARK 500 2 PRO A 57 -79.72 -88.98
REMARK 500 2 PHE A 58 122.31 59.91
REMARK 500 2 LYS A 62 55.82 -168.75
REMARK 500 2 LYS A 63 -161.00 -58.82
REMARK 500 2 THR A 64 -165.06 -62.95
REMARK 500 3 GLU A 2 94.54 -47.14
REMARK 500 3 GLN A 3 -129.11 -139.60
REMARK 500 3 THR A 6 -176.36 -49.46
REMARK 500 3 PHE A 14 -77.52 -122.95
REMARK 500 3 ASN A 31 -7.76 -59.99
REMARK 500 3 LYS A 39 45.74 177.18
REMARK 500 3 ILE A 44 43.87 -89.29
REMARK 500 3 ASN A 45 -151.53 -105.45
REMARK 500 3 ASP A 47 -53.71 120.61
REMARK 500 3 ASP A 56A -90.10 50.98
REMARK 500 3 GLU A 56C 97.03 -162.19
REMARK 500 3 SER A 60 -167.50 -62.62
REMARK 500 3 ASN A 61 55.13 37.12
REMARK 500 3 LYS A 62 49.64 -175.07
REMARK 500 3 LYS A 63 -95.15 -136.38
REMARK 500 3 THR A 64 -92.28 -116.39
REMARK 500 4 GLU A 2 109.76 -166.71
REMARK 500 4 GLN A 3 58.85 -100.40
REMARK 500 4 LYS A 8 -63.79 -90.56
REMARK 500 4 PHE A 14 -75.94 -117.95
REMARK 500 4 ASN A 45 -123.78 -103.40
REMARK 500 4 ALA A 46 29.09 40.65
REMARK 500 4 ASP A 47 64.35 72.78
REMARK 500 4 ASP A 56A 93.82 -40.57
REMARK 500
REMARK 500 THIS ENTRY HAS 414 RAMACHANDRAN OUTLIERS.
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 4 0.15 SIDE CHAIN
REMARK 500 1 ARG A 13 0.23 SIDE CHAIN
REMARK 500 1 ARG A 38 0.18 SIDE CHAIN
REMARK 500 2 ARG A 4 0.14 SIDE CHAIN
REMARK 500 2 ARG A 13 0.31 SIDE CHAIN
REMARK 500 2 ARG A 38 0.10 SIDE CHAIN
REMARK 500 3 ARG A 4 0.22 SIDE CHAIN
REMARK 500 3 ARG A 13 0.32 SIDE CHAIN
REMARK 500 3 ARG A 38 0.18 SIDE CHAIN
REMARK 500 4 ARG A 4 0.29 SIDE CHAIN
REMARK 500 4 ARG A 13 0.28 SIDE CHAIN
REMARK 500 4 ARG A 38 0.30 SIDE CHAIN
REMARK 500 5 ARG A 4 0.32 SIDE CHAIN
REMARK 500 5 ARG A 13 0.25 SIDE CHAIN
REMARK 500 5 ARG A 38 0.27 SIDE CHAIN
REMARK 500 6 ARG A 38 0.32 SIDE CHAIN
REMARK 500 7 ARG A 4 0.26 SIDE CHAIN
REMARK 500 7 ARG A 13 0.32 SIDE CHAIN
REMARK 500 7 ARG A 38 0.32 SIDE CHAIN
REMARK 500 8 ARG A 4 0.26 SIDE CHAIN
REMARK 500 8 ARG A 13 0.32 SIDE CHAIN
REMARK 500 8 ARG A 38 0.12 SIDE CHAIN
REMARK 500 9 ARG A 4 0.32 SIDE CHAIN
REMARK 500 9 ARG A 13 0.30 SIDE CHAIN
REMARK 500 9 ARG A 38 0.32 SIDE CHAIN
REMARK 500 10 ARG A 4 0.30 SIDE CHAIN
REMARK 500 10 ARG A 13 0.08 SIDE CHAIN
REMARK 500 11 ARG A 4 0.29 SIDE CHAIN
REMARK 500 11 ARG A 13 0.28 SIDE CHAIN
REMARK 500 11 ARG A 38 0.24 SIDE CHAIN
REMARK 500 12 ARG A 4 0.23 SIDE CHAIN
REMARK 500 12 ARG A 13 0.31 SIDE CHAIN
REMARK 500 12 ARG A 38 0.32 SIDE CHAIN
REMARK 500 13 ARG A 4 0.32 SIDE CHAIN
REMARK 500 13 ARG A 13 0.24 SIDE CHAIN
REMARK 500 13 ARG A 38 0.22 SIDE CHAIN
REMARK 500 14 ARG A 4 0.31 SIDE CHAIN
REMARK 500 14 ARG A 13 0.30 SIDE CHAIN
REMARK 500 14 ARG A 38 0.23 SIDE CHAIN
REMARK 500 15 ARG A 4 0.29 SIDE CHAIN
REMARK 500 15 ARG A 13 0.29 SIDE CHAIN
REMARK 500 15 ARG A 38 0.26 SIDE CHAIN
REMARK 500 16 ARG A 13 0.28 SIDE CHAIN
REMARK 500 17 ARG A 4 0.31 SIDE CHAIN
REMARK 500 17 ARG A 13 0.12 SIDE CHAIN
REMARK 500 17 ARG A 38 0.26 SIDE CHAIN
REMARK 500 18 ARG A 4 0.31 SIDE CHAIN
REMARK 500 18 ARG A 13 0.31 SIDE CHAIN
REMARK 500 18 ARG A 38 0.25 SIDE CHAIN
REMARK 500 19 ARG A 4 0.24 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 88 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2ORC A 1 66 UNP P03040 RCRO_LAMBD 1 66
SEQADV 2ORC GLU A 54 UNP P03040 INSERTION
SEQADV 2ORC VAL A 55 UNP P03040 INSERTION
SEQADV 2ORC LYS A 56 UNP P03040 INSERTION
SEQADV 2ORC ASP A 56A UNP P03040 INSERTION
SEQADV 2ORC GLY A 56B UNP P03040 INSERTION
SEQRES 1 A 71 MET GLU GLN ARG ILE THR LEU LYS ASP TYR ALA MET ARG
SEQRES 2 A 71 PHE GLY GLN THR LYS THR ALA LYS ASP LEU GLY VAL TYR
SEQRES 3 A 71 GLN SER ALA ILE ASN LYS ALA ILE HIS ALA GLY ARG LYS
SEQRES 4 A 71 ILE PHE LEU THR ILE ASN ALA ASP GLY SER VAL TYR ALA
SEQRES 5 A 71 GLU GLU VAL LYS ASP GLY GLU VAL LYS PRO PHE PRO SER
SEQRES 6 A 71 ASN LYS LYS THR THR ALA
HELIX 1 1 LYS A 8 ARG A 13 1 6
HELIX 2 2 GLN A 16 LEU A 23 1 8
HELIX 3 3 GLN A 27 HIS A 35 1 9
SHEET 1 A 2 GLN A 3 THR A 6 0
SHEET 2 A 2 PHE A 41 ILE A 44 -1 N ILE A 44 O GLN A 3
CISPEP 1 PHE A 58 PRO A 59 1 0.11
CISPEP 2 PHE A 58 PRO A 59 2 -0.03
CISPEP 3 PHE A 58 PRO A 59 3 0.15
CISPEP 4 PHE A 58 PRO A 59 4 0.16
CISPEP 5 PHE A 58 PRO A 59 5 0.11
CISPEP 6 PHE A 58 PRO A 59 6 -0.07
CISPEP 7 PHE A 58 PRO A 59 7 -0.44
CISPEP 8 PHE A 58 PRO A 59 8 -0.03
CISPEP 9 PHE A 58 PRO A 59 9 -0.68
CISPEP 10 PHE A 58 PRO A 59 10 0.10
CISPEP 11 PHE A 58 PRO A 59 11 -0.04
CISPEP 12 PHE A 58 PRO A 59 12 0.35
CISPEP 13 PHE A 58 PRO A 59 13 -0.17
CISPEP 14 PHE A 58 PRO A 59 14 -0.19
CISPEP 15 PHE A 58 PRO A 59 15 -0.32
CISPEP 16 PHE A 58 PRO A 59 16 0.12
CISPEP 17 PHE A 58 PRO A 59 17 0.08
CISPEP 18 PHE A 58 PRO A 59 18 0.09
CISPEP 19 PHE A 58 PRO A 59 19 -0.05
CISPEP 20 PHE A 58 PRO A 59 20 -0.31
CISPEP 21 PHE A 58 PRO A 59 21 0.07
CISPEP 22 PHE A 58 PRO A 59 22 0.10
CISPEP 23 PHE A 58 PRO A 59 23 -0.03
CISPEP 24 PHE A 58 PRO A 59 24 0.20
CISPEP 25 PHE A 58 PRO A 59 25 -0.13
CISPEP 26 PHE A 58 PRO A 59 26 0.09
CISPEP 27 PHE A 58 PRO A 59 27 0.16
CISPEP 28 PHE A 58 PRO A 59 28 0.04
CISPEP 29 PHE A 58 PRO A 59 29 0.20
CISPEP 30 PHE A 58 PRO A 59 30 -0.05
CISPEP 31 PHE A 58 PRO A 59 31 -0.06
CISPEP 32 PHE A 58 PRO A 59 32 0.06
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 16 2 Bytes