Header list of 1wrt.pdb file
Complete list - r 2 2 Bytes
HEADER OPERON REPRESSOR 12-MAY-95 1WRT
TITLE NMR STUDY OF APO TRP REPRESSOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APO TRP REPRESSOR;
COMPND 3 CHAIN: R, S
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: CY15070 AND CY17071
KEYWDS OPERON REPRESSOR, TRANSCRIPTION REGULATION, DNA-BINDING
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR D.ZHAO,Z.ZHENG
REVDAT 3 02-MAR-22 1WRT 1 REMARK
REVDAT 2 24-FEB-09 1WRT 1 VERSN
REVDAT 1 20-JUN-96 1WRT 0
JRNL AUTH D.ZHAO,C.H.ARROWSMITH,X.JIA,O.JARDETZKY
JRNL TITL REFINED SOLUTION STRUCTURES OF THE ESCHERICHIA COLI TRP
JRNL TITL 2 HOLO- AND APOREPRESSOR.
JRNL REF J.MOL.BIOL. V. 229 735 1993
JRNL REFN ISSN 0022-2836
JRNL PMID 8433368
JRNL DOI 10.1006/JMBI.1993.1076
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.ZHANG,D.ZHAO,M.REVINGTON,W.LEE,X.JIA,C.ARROWSMITH,
REMARK 1 AUTH 2 O.JARDETZKY
REMARK 1 TITL THE SOLUTION STRUCTURES OF THE TRP REPRESSOR-OPERATOR DNA
REMARK 1 TITL 2 COMPLEX
REMARK 1 REF J.MOL.BIOL. V. 238 592 1994
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.ZHAO,O.JARDETZKY
REMARK 1 TITL SEQUENTIAL SIMULATED ANNEALING: AN EFFICIENT PROCEDURE FOR
REMARK 1 TITL 2 STRUCTURAL REFINEMENT BASED ON NMR CONSTRAINTS
REMARK 1 REF J.PHYS.CHEM. V. 97 3007 1993
REMARK 1 REFN ISSN 0022-3654
REMARK 1 REFERENCE 3
REMARK 1 AUTH C.ARROWSMITH,R.PACHTER,R.ALTMAN,O.JARDETZKY
REMARK 1 TITL THE SOLUTION STRUCTURES OF ESCHERICHIA COLI TRP REPRESSOR
REMARK 1 TITL 2 AND TRP APOREPRESSOR AT AN INTERMEDIATE RESOLUTION
REMARK 1 REF EUR.J.BIOCHEM. V. 202 53 1991
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 4
REMARK 1 AUTH C.H.ARROWSMITH,R.PACHTER,R.B.ALTMAN,S.B.IYER,O.JARDETZKY
REMARK 1 TITL SEQUENCE-SPECIFIC 1H NMR ASSIGNMENTS AND SECONDARY STRUCTURE
REMARK 1 TITL 2 IN SOLUTION OF ESCHERICHIA COLI TRP REPRESSOR
REMARK 1 REF BIOCHEMISTRY V. 29 6332 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 5
REMARK 1 AUTH C.H.ARROWSMITH,J.CAREY,L.TREAT-CLEMONS,O.JARDETZKY
REMARK 1 TITL NMR ASSIGNMENTS FOR THE AMINO-TERMINAL RESIDUES OF TRP
REMARK 1 TITL 2 REPRESSOR AND THEIR ROLE IN DNA BINDING
REMARK 1 REF BIOCHEMISTRY V. 28 3875 1989
REMARK 1 REFN ISSN 0006-2960
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: NULL
REMARK 4
REMARK 4 1WRT 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_1000177228.
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 : 15
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, S
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 1-15
REMARK 465 RES C SSSEQI
REMARK 465 ASP R 108
REMARK 465 ASP S 108
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 TYR S 30 N ASP S 33 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 HIS R 16 CG HIS R 16 ND1 -0.099
REMARK 500 1 HIS R 35 CG HIS R 35 ND1 -0.098
REMARK 500 1 TRP R 99 CG TRP R 99 CD2 -0.115
REMARK 500 1 HIS S 16 CG HIS S 16 ND1 -0.101
REMARK 500 1 HIS S 35 CG HIS S 35 ND1 -0.099
REMARK 500 1 TRP S 99 CG TRP S 99 CD2 -0.111
REMARK 500 2 HIS R 16 CG HIS R 16 ND1 -0.103
REMARK 500 2 TRP R 19 CG TRP R 19 CD2 -0.102
REMARK 500 2 HIS R 35 CG HIS R 35 ND1 -0.103
REMARK 500 2 TRP R 99 CG TRP R 99 CD2 -0.108
REMARK 500 2 HIS S 16 CG HIS S 16 ND1 -0.101
REMARK 500 2 HIS S 35 CG HIS S 35 ND1 -0.096
REMARK 500 2 TRP S 99 CG TRP S 99 CD2 -0.111
REMARK 500 3 HIS R 16 CG HIS R 16 ND1 -0.099
REMARK 500 3 HIS R 35 CG HIS R 35 ND1 -0.100
REMARK 500 3 TRP R 99 CG TRP R 99 CD2 -0.112
REMARK 500 3 HIS S 16 CG HIS S 16 ND1 -0.102
REMARK 500 3 HIS S 35 CG HIS S 35 ND1 -0.099
REMARK 500 3 TRP S 99 CG TRP S 99 CD2 -0.112
REMARK 500 4 HIS R 16 CG HIS R 16 ND1 -0.101
REMARK 500 4 HIS R 35 CG HIS R 35 ND1 -0.102
REMARK 500 4 TRP R 99 CG TRP R 99 CD2 -0.108
REMARK 500 4 HIS S 16 CG HIS S 16 ND1 -0.099
REMARK 500 4 HIS S 35 CG HIS S 35 ND1 -0.099
REMARK 500 4 TRP S 99 CG TRP S 99 CD2 -0.110
REMARK 500 5 HIS R 16 CG HIS R 16 ND1 -0.102
REMARK 500 5 HIS R 35 CG HIS R 35 ND1 -0.100
REMARK 500 5 TRP R 99 CG TRP R 99 CD2 -0.112
REMARK 500 5 HIS S 16 CG HIS S 16 ND1 -0.103
REMARK 500 5 HIS S 35 CG HIS S 35 ND1 -0.101
REMARK 500 5 TRP S 99 CG TRP S 99 CD2 -0.111
REMARK 500 6 HIS R 16 CG HIS R 16 ND1 -0.099
REMARK 500 6 TRP R 19 CG TRP R 19 CD2 -0.104
REMARK 500 6 HIS R 35 CG HIS R 35 ND1 -0.101
REMARK 500 6 TRP R 99 CG TRP R 99 CD2 -0.116
REMARK 500 6 HIS S 16 CG HIS S 16 ND1 -0.102
REMARK 500 6 HIS S 35 CG HIS S 35 ND1 -0.100
REMARK 500 6 TRP S 99 CG TRP S 99 CD2 -0.110
REMARK 500 7 HIS R 16 CG HIS R 16 ND1 -0.099
REMARK 500 7 HIS R 35 CG HIS R 35 ND1 -0.099
REMARK 500 7 TRP R 99 CG TRP R 99 CD2 -0.111
REMARK 500 7 HIS S 16 CG HIS S 16 ND1 -0.101
REMARK 500 7 HIS S 35 CG HIS S 35 ND1 -0.100
REMARK 500 7 TRP S 99 CG TRP S 99 CD2 -0.116
REMARK 500 8 HIS R 16 CG HIS R 16 ND1 -0.102
REMARK 500 8 HIS R 35 CG HIS R 35 ND1 -0.099
REMARK 500 8 TRP R 99 CG TRP R 99 CD2 -0.112
REMARK 500 8 HIS S 16 CG HIS S 16 ND1 -0.103
REMARK 500 8 HIS S 35 CG HIS S 35 ND1 -0.101
REMARK 500 8 TRP S 99 CG TRP S 99 CD2 -0.114
REMARK 500
REMARK 500 THIS ENTRY HAS 92 BOND DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
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 1 TRP R 19 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 1 TRP R 19 CD1 - NE1 - CE2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 1 TRP R 19 NE1 - CE2 - CZ2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 1 TRP R 19 NE1 - CE2 - CD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 1 TRP R 99 CG - CD1 - NE1 ANGL. DEV. = -7.1 DEGREES
REMARK 500 1 TRP R 99 CD1 - NE1 - CE2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 1 TRP R 99 NE1 - CE2 - CZ2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 1 TRP S 19 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 1 TRP S 19 CD1 - NE1 - CE2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 1 TRP S 19 NE1 - CE2 - CZ2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 1 TRP S 99 CG - CD1 - NE1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 1 TRP S 99 CD1 - NE1 - CE2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 1 TRP S 99 NE1 - CE2 - CZ2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 2 TRP R 19 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 2 TRP R 19 CD1 - NE1 - CE2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 2 TRP R 19 NE1 - CE2 - CZ2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 2 TRP R 19 NE1 - CE2 - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 2 TRP R 99 CG - CD1 - NE1 ANGL. DEV. = -7.5 DEGREES
REMARK 500 2 TRP R 99 CD1 - NE1 - CE2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 2 TRP R 99 NE1 - CE2 - CZ2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 2 TRP S 19 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 2 TRP S 19 CD1 - NE1 - CE2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 2 TRP S 19 NE1 - CE2 - CZ2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 2 TRP S 99 CG - CD1 - NE1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 2 TRP S 99 CD1 - NE1 - CE2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 2 TRP S 99 NE1 - CE2 - CZ2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 3 TRP R 19 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 3 TRP R 19 CD1 - NE1 - CE2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 3 TRP R 19 NE1 - CE2 - CZ2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 3 TRP R 99 CG - CD1 - NE1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 3 TRP R 99 CD1 - NE1 - CE2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 3 TRP R 99 NE1 - CE2 - CZ2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 3 TRP S 19 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 3 TRP S 19 CD1 - NE1 - CE2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 3 TRP S 19 NE1 - CE2 - CZ2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 3 TRP S 99 CG - CD1 - NE1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 3 TRP S 99 CD1 - NE1 - CE2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 3 TRP S 99 NE1 - CE2 - CZ2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 4 TRP R 19 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 4 TRP R 19 CD1 - NE1 - CE2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 4 TRP R 19 NE1 - CE2 - CZ2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 4 TRP R 99 CG - CD1 - NE1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 4 TRP R 99 CD1 - NE1 - CE2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 4 TRP R 99 NE1 - CE2 - CZ2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 4 TRP S 19 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 4 TRP S 19 CD1 - NE1 - CE2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 4 TRP S 19 NE1 - CE2 - CZ2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 4 TRP S 19 NE1 - CE2 - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 4 TRP S 99 CG - CD1 - NE1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 4 TRP S 99 CD1 - NE1 - CE2 ANGL. DEV. = 5.9 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 191 ANGLE DEVIATIONS.
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 SER R 5 73.25 53.69
REMARK 500 1 TYR R 7 -2.06 -161.54
REMARK 500 1 ALA R 12 10.65 -152.33
REMARK 500 1 GLU R 13 -160.38 54.71
REMARK 500 1 GLN R 14 177.80 50.15
REMARK 500 1 ARG R 15 -14.28 -153.14
REMARK 500 1 GLU R 18 -74.41 -49.13
REMARK 500 1 TRP R 19 -31.03 -32.77
REMARK 500 1 TYR R 30 -70.14 -47.37
REMARK 500 1 GLN R 31 -70.09 11.70
REMARK 500 1 ASN R 32 -95.97 -94.74
REMARK 500 1 ASP R 33 22.41 -151.58
REMARK 500 1 THR R 44 151.89 -45.69
REMARK 500 1 LEU R 51 -72.42 -69.39
REMARK 500 1 ILE R 57 -76.33 -59.38
REMARK 500 1 ARG R 63 -11.61 -43.96
REMARK 500 1 GLU R 65 35.80 -81.62
REMARK 500 1 ALA R 77 114.79 178.09
REMARK 500 1 ILE R 82 -67.60 -106.87
REMARK 500 1 THR R 83 6.50 -68.18
REMARK 500 1 ARG R 84 -74.84 -41.43
REMARK 500 1 ALA R 92 68.39 -151.91
REMARK 500 1 ARG R 97 -19.01 -47.28
REMARK 500 1 LYS R 106 118.46 59.79
REMARK 500 1 SER S 5 167.15 54.34
REMARK 500 1 TYR S 7 18.91 51.47
REMARK 500 1 SER S 8 137.96 62.41
REMARK 500 1 GLN S 14 -154.53 -146.58
REMARK 500 1 HIS S 16 73.48 -179.39
REMARK 500 1 TRP S 19 -13.36 -42.75
REMARK 500 1 LEU S 20 -81.22 -115.52
REMARK 500 1 ARG S 21 -39.61 -39.27
REMARK 500 1 TYR S 30 -79.84 -48.56
REMARK 500 1 GLN S 31 -66.30 -13.72
REMARK 500 1 ASN S 32 35.24 -77.32
REMARK 500 1 ASP S 33 28.36 31.78
REMARK 500 1 PRO S 37 -72.25 -59.17
REMARK 500 1 LEU S 39 -70.19 -43.36
REMARK 500 1 MET S 42 47.17 -95.07
REMARK 500 1 LEU S 43 -71.76 -61.13
REMARK 500 1 THR S 44 137.26 73.07
REMARK 500 1 ARG S 54 -65.68 -90.68
REMARK 500 1 GLU S 70 85.69 55.82
REMARK 500 1 GLU S 74 79.73 -152.63
REMARK 500 1 ILE S 79 28.04 -73.73
REMARK 500 1 ALA S 80 -102.55 -58.88
REMARK 500 1 SER S 86 -56.78 -139.82
REMARK 500 1 SER S 88 106.77 -160.92
REMARK 500 1 LEU S 89 -98.65 -94.71
REMARK 500 1 LEU S 100 -35.85 -33.94
REMARK 500
REMARK 500 THIS ENTRY HAS 790 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 R 21 0.26 SIDE CHAIN
REMARK 500 1 ARG R 54 0.18 SIDE CHAIN
REMARK 500 1 ARG R 56 0.30 SIDE CHAIN
REMARK 500 1 ARG R 63 0.25 SIDE CHAIN
REMARK 500 1 ARG R 69 0.28 SIDE CHAIN
REMARK 500 1 ARG R 84 0.20 SIDE CHAIN
REMARK 500 1 ARG R 97 0.30 SIDE CHAIN
REMARK 500 1 ARG S 15 0.18 SIDE CHAIN
REMARK 500 1 ARG S 21 0.24 SIDE CHAIN
REMARK 500 1 ARG S 48 0.24 SIDE CHAIN
REMARK 500 1 ARG S 54 0.32 SIDE CHAIN
REMARK 500 1 ARG S 56 0.23 SIDE CHAIN
REMARK 500 1 ARG S 63 0.28 SIDE CHAIN
REMARK 500 1 ARG S 69 0.21 SIDE CHAIN
REMARK 500 1 ARG S 84 0.32 SIDE CHAIN
REMARK 500 2 ARG R 21 0.31 SIDE CHAIN
REMARK 500 2 ARG R 48 0.24 SIDE CHAIN
REMARK 500 2 ARG R 54 0.09 SIDE CHAIN
REMARK 500 2 ARG R 56 0.32 SIDE CHAIN
REMARK 500 2 ARG R 63 0.31 SIDE CHAIN
REMARK 500 2 ARG R 69 0.32 SIDE CHAIN
REMARK 500 2 ARG R 84 0.26 SIDE CHAIN
REMARK 500 2 ARG S 15 0.28 SIDE CHAIN
REMARK 500 2 ARG S 21 0.09 SIDE CHAIN
REMARK 500 2 ARG S 48 0.28 SIDE CHAIN
REMARK 500 2 ARG S 54 0.24 SIDE CHAIN
REMARK 500 2 ARG S 56 0.31 SIDE CHAIN
REMARK 500 2 ARG S 63 0.27 SIDE CHAIN
REMARK 500 2 ARG S 69 0.32 SIDE CHAIN
REMARK 500 2 ARG S 84 0.31 SIDE CHAIN
REMARK 500 2 ARG S 97 0.27 SIDE CHAIN
REMARK 500 3 ARG R 15 0.28 SIDE CHAIN
REMARK 500 3 ARG R 21 0.31 SIDE CHAIN
REMARK 500 3 ARG R 48 0.30 SIDE CHAIN
REMARK 500 3 ARG R 54 0.15 SIDE CHAIN
REMARK 500 3 ARG R 56 0.31 SIDE CHAIN
REMARK 500 3 ARG R 63 0.27 SIDE CHAIN
REMARK 500 3 ARG R 69 0.30 SIDE CHAIN
REMARK 500 3 ARG R 84 0.24 SIDE CHAIN
REMARK 500 3 ARG R 97 0.18 SIDE CHAIN
REMARK 500 3 ARG S 15 0.30 SIDE CHAIN
REMARK 500 3 ARG S 21 0.30 SIDE CHAIN
REMARK 500 3 ARG S 48 0.24 SIDE CHAIN
REMARK 500 3 ARG S 54 0.31 SIDE CHAIN
REMARK 500 3 ARG S 56 0.32 SIDE CHAIN
REMARK 500 3 ARG S 63 0.27 SIDE CHAIN
REMARK 500 3 ARG S 69 0.10 SIDE CHAIN
REMARK 500 3 ARG S 84 0.27 SIDE CHAIN
REMARK 500 3 ARG S 97 0.22 SIDE CHAIN
REMARK 500 4 ARG R 15 0.17 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 256 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1WRT R 4 108 UNP P0A881 TRPR_ECOLI 3 107
DBREF 1WRT S 4 108 UNP P0A881 TRPR_ECOLI 3 107
SEQRES 1 R 105 GLN SER PRO TYR SER ALA ALA MET ALA GLU GLN ARG HIS
SEQRES 2 R 105 GLN GLU TRP LEU ARG PHE VAL ASP LEU LEU LYS ASN ALA
SEQRES 3 R 105 TYR GLN ASN ASP LEU HIS LEU PRO LEU LEU ASN LEU MET
SEQRES 4 R 105 LEU THR PRO ASP GLU ARG GLU ALA LEU GLY THR ARG VAL
SEQRES 5 R 105 ARG ILE VAL GLU GLU LEU LEU ARG GLY GLU MET SER GLN
SEQRES 6 R 105 ARG GLU LEU LYS ASN GLU LEU GLY ALA GLY ILE ALA THR
SEQRES 7 R 105 ILE THR ARG GLY SER ASN SER LEU LYS ALA ALA PRO VAL
SEQRES 8 R 105 GLU LEU ARG GLN TRP LEU GLU GLU VAL LEU LEU LYS SER
SEQRES 9 R 105 ASP
SEQRES 1 S 105 GLN SER PRO TYR SER ALA ALA MET ALA GLU GLN ARG HIS
SEQRES 2 S 105 GLN GLU TRP LEU ARG PHE VAL ASP LEU LEU LYS ASN ALA
SEQRES 3 S 105 TYR GLN ASN ASP LEU HIS LEU PRO LEU LEU ASN LEU MET
SEQRES 4 S 105 LEU THR PRO ASP GLU ARG GLU ALA LEU GLY THR ARG VAL
SEQRES 5 S 105 ARG ILE VAL GLU GLU LEU LEU ARG GLY GLU MET SER GLN
SEQRES 6 S 105 ARG GLU LEU LYS ASN GLU LEU GLY ALA GLY ILE ALA THR
SEQRES 7 S 105 ILE THR ARG GLY SER ASN SER LEU LYS ALA ALA PRO VAL
SEQRES 8 S 105 GLU LEU ARG GLN TRP LEU GLU GLU VAL LEU LEU LYS SER
SEQRES 9 S 105 ASP
HELIX 1 1 HIS R 16 GLN R 31 1 16
HELIX 2 2 LEU R 36 MET R 42 1 7
HELIX 3 3 PRO R 45 LEU R 61 1 17
HELIX 4 4 ALA R 80 THR R 83 1 4
HELIX 5 5 PRO R 93 GLU R 95 5 3
HELIX 6 6 ARG R 97 VAL R 103 1 7
HELIX 7 7 GLU S 18 GLN S 31 1 14
HELIX 8 8 HIS S 35 LEU S 41 1 7
HELIX 9 9 PRO S 45 LEU S 61 1 17
HELIX 10 10 PRO S 93 LEU S 104 1 12
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