HEADER AMINOACYL-TRNA SYNTHETASE 09-JUN-95 1KRT
TITLE SOLUTION STRUCTURE OF THE ANTICODON BINDING DOMAIN OF ESCHERICHIA COLI
TITLE 2 LYSYL-TRNA SYNTHETASE AND STUDIES OF ITS INTERACTIONS WITH TRNA-LYS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSYL-TRNA SYNTHETASE (PRODUCT OF LYSS GENE);
COMPND 3 CHAIN: A;
COMPND 4 EC: 6.1.1.6;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: JM101TR;
SOURCE 5 GENE: LYSS CODONS 40 - 149;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: LAC;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTRC-ND;
SOURCE 10 EXPRESSION_SYSTEM_GENE: LYSS CODONS 40 - 149;
SOURCE 11 OTHER_DETAILS: PTRC99A (IPTG-INDUCIBLE LAC PROMOTER)
KEYWDS AMINOACYL-TRNA SYNTHETASE
EXPDTA SOLUTION NMR
NUMMDL 9
AUTHOR S.COMMANS,F.DARDEL
REVDAT 3 23-FEB-22 1KRT 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1KRT 1 VERSN
REVDAT 1 15-SEP-95 1KRT 0
JRNL AUTH S.COMMANS,P.PLATEAU,S.BLANQUET,F.DARDEL
JRNL TITL SOLUTION STRUCTURE OF THE ANTICODON-BINDING DOMAIN OF
JRNL TITL 2 ESCHERICHIA COLI LYSYL-TRNA SYNTHETASE AND STUDIES OF ITS
JRNL TITL 3 INTERACTION WITH TRNA(LYS).
JRNL REF J.MOL.BIOL. V. 253 100 1995
JRNL REFN ISSN 0022-2836
JRNL PMID 7473706
JRNL DOI 10.1006/JMBI.1995.0539
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.LEVEQUE,P.PLATEAU,P.DESSEN,S.BLANQUET
REMARK 1 TITL HOMOLOGY OF LYSS AND LYSU, THE TWO ESCHERICHIA COLI GENES
REMARK 1 TITL 2 ENCODING DISTINCT LYSYL-TRNA SYNTHETASE SPECIES
REMARK 1 REF NUCLEIC ACIDS RES. V. 18 305 1990
REMARK 1 REFN ISSN 0305-1048
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KRT 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_1000174485.
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 : 9
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 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 1-9
REMARK 465 RES C SSSEQI
REMARK 465 ALA A 30
REMARK 465 GLU A 31
REMARK 465 GLN A 32
REMARK 465 GLY A 33
REMARK 465 ILE A 34
REMARK 465 ALA A 35
REMARK 465 PHE A 36
REMARK 465 PRO A 37
REMARK 465 ASN A 38
REMARK 465 ASP A 39
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: 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 VAL A 70 CB VAL A 70 CG1 -0.155
REMARK 500 1 ALA A 83 CA ALA A 83 CB -0.178
REMARK 500 1 ARG A 94 CA ARG A 94 CB -0.135
REMARK 500 1 VAL A 108 CA VAL A 108 CB -0.186
REMARK 500 1 TYR A 109 CA TYR A 109 CB 0.162
REMARK 500 1 TRP A 116 CG TRP A 116 CD2 -0.110
REMARK 500 1 TRP A 116 NE1 TRP A 116 CE2 -0.093
REMARK 500 1 TRP A 116 CE2 TRP A 116 CZ2 -0.103
REMARK 500 2 HIS A 44 CG HIS A 44 ND1 -0.093
REMARK 500 2 ALA A 69 CA ALA A 69 CB -0.279
REMARK 500 2 ALA A 83 CA ALA A 83 CB -0.157
REMARK 500 2 GLN A 112 CA GLN A 112 CB -0.135
REMARK 500 2 TRP A 116 CG TRP A 116 CD2 -0.112
REMARK 500 2 ALA A 124 CA ALA A 124 CB -0.135
REMARK 500 2 GLU A 135 CA GLU A 135 CB -0.146
REMARK 500 3 HIS A 44 CG HIS A 44 ND1 -0.101
REMARK 500 3 ALA A 69 CA ALA A 69 CB -0.304
REMARK 500 3 MET A 74 CA MET A 74 CB -0.147
REMARK 500 3 ARG A 77 CB ARG A 77 CG 0.236
REMARK 500 3 ALA A 83 CA ALA A 83 CB -0.136
REMARK 500 3 ALA A 124 CA ALA A 124 CB -0.135
REMARK 500 4 HIS A 44 CG HIS A 44 ND1 -0.101
REMARK 500 4 LEU A 49 CA LEU A 49 CB -0.189
REMARK 500 4 ALA A 69 CA ALA A 69 CB -0.279
REMARK 500 4 ALA A 83 CA ALA A 83 CB -0.165
REMARK 500 4 GLN A 112 CA GLN A 112 CB -0.134
REMARK 500 4 PHE A 113 CA PHE A 113 CB -0.141
REMARK 500 4 GLU A 135 CA GLU A 135 CB -0.151
REMARK 500 5 HIS A 44 CG HIS A 44 ND1 -0.097
REMARK 500 5 ALA A 69 CA ALA A 69 CB -0.272
REMARK 500 5 ALA A 83 CA ALA A 83 CB -0.184
REMARK 500 5 LEU A 118 CA LEU A 118 CB -0.164
REMARK 500 5 ALA A 124 CA ALA A 124 CB -0.135
REMARK 500 6 HIS A 44 CA HIS A 44 CB -0.234
REMARK 500 6 HIS A 44 NE2 HIS A 44 CD2 -0.072
REMARK 500 6 VAL A 68 CA VAL A 68 CB -0.128
REMARK 500 6 VAL A 68 CB VAL A 68 CG1 -0.140
REMARK 500 6 ALA A 69 CA ALA A 69 CB -0.166
REMARK 500 6 ALA A 83 CA ALA A 83 CB -0.149
REMARK 500 6 TRP A 116 CG TRP A 116 CD2 -0.120
REMARK 500 6 TRP A 116 NE1 TRP A 116 CE2 -0.098
REMARK 500 6 LYS A 127 CA LYS A 127 CB -0.149
REMARK 500 6 GLU A 135 CA GLU A 135 CB -0.197
REMARK 500 7 HIS A 44 CG HIS A 44 ND1 -0.114
REMARK 500 7 ALA A 69 CA ALA A 69 CB -0.127
REMARK 500 7 ALA A 83 CA ALA A 83 CB -0.156
REMARK 500 7 SER A 84 CA SER A 84 CB -0.100
REMARK 500 7 GLN A 112 CA GLN A 112 CB -0.140
REMARK 500 7 TRP A 116 CG TRP A 116 CD2 -0.118
REMARK 500 7 TRP A 116 NE1 TRP A 116 CE2 -0.080
REMARK 500
REMARK 500 THIS ENTRY HAS 65 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 PHE A 40 CB - CG - CD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 1 PHE A 40 CB - CG - CD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 1 ARG A 41 N - CA - C ANGL. DEV. = 19.1 DEGREES
REMARK 500 1 ASP A 43 N - CA - C ANGL. DEV. = -18.6 DEGREES
REMARK 500 1 HIS A 44 CA - CB - CG ANGL. DEV. = 28.5 DEGREES
REMARK 500 1 HIS A 44 CB - CG - CD2 ANGL. DEV. = 9.7 DEGREES
REMARK 500 1 HIS A 44 CB - CG - ND1 ANGL. DEV. = -8.1 DEGREES
REMARK 500 1 LEU A 49 CB - CG - CD2 ANGL. DEV. = -12.4 DEGREES
REMARK 500 1 GLU A 59 CA - C - N ANGL. DEV. = -14.0 DEGREES
REMARK 500 1 VAL A 70 CG1 - CB - CG2 ANGL. DEV. = -23.8 DEGREES
REMARK 500 1 VAL A 70 CA - CB - CG1 ANGL. DEV. = -13.3 DEGREES
REMARK 500 1 VAL A 70 CA - CB - CG2 ANGL. DEV. = -13.2 DEGREES
REMARK 500 1 MET A 74 CA - CB - CG ANGL. DEV. = -11.3 DEGREES
REMARK 500 1 THR A 87 CA - CB - CG2 ANGL. DEV. = -8.5 DEGREES
REMARK 500 1 GLN A 89 CA - CB - CG ANGL. DEV. = -22.9 DEGREES
REMARK 500 1 TYR A 98 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 1 TYR A 98 CB - CG - CD1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 ALA A 100 N - CA - CB ANGL. DEV. = -10.1 DEGREES
REMARK 500 1 GLY A 107 N - CA - C ANGL. DEV. = -15.3 DEGREES
REMARK 500 1 VAL A 108 CA - C - N ANGL. DEV. = -22.2 DEGREES
REMARK 500 1 VAL A 108 O - C - N ANGL. DEV. = 9.7 DEGREES
REMARK 500 1 TYR A 109 N - CA - CB ANGL. DEV. = -11.3 DEGREES
REMARK 500 1 TYR A 109 CA - CB - CG ANGL. DEV. = 17.0 DEGREES
REMARK 500 1 TYR A 109 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 1 GLU A 111 CA - CB - CG ANGL. DEV. = -16.2 DEGREES
REMARK 500 1 GLN A 112 CB - CA - C ANGL. DEV. = 12.1 DEGREES
REMARK 500 1 GLN A 112 N - CA - CB ANGL. DEV. = -15.0 DEGREES
REMARK 500 1 GLN A 112 CA - CB - CG ANGL. DEV. = -13.9 DEGREES
REMARK 500 1 TRP A 116 CA - CB - CG ANGL. DEV. = -18.3 DEGREES
REMARK 500 1 TRP A 116 CB - CG - CD2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 1 TRP A 116 CD1 - CG - CD2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 1 TRP A 116 CB - CG - CD1 ANGL. DEV. = -13.9 DEGREES
REMARK 500 1 ASP A 120 N - CA - CB ANGL. DEV. = -12.9 DEGREES
REMARK 500 1 GLY A 123 N - CA - C ANGL. DEV. = -18.2 DEGREES
REMARK 500 1 LEU A 136 N - CA - CB ANGL. DEV. = -13.4 DEGREES
REMARK 500 1 LEU A 136 N - CA - C ANGL. DEV. = 24.3 DEGREES
REMARK 500 1 LEU A 145 N - CA - CB ANGL. DEV. = -15.5 DEGREES
REMARK 500 1 LEU A 146 CA - CB - CG ANGL. DEV. = -16.1 DEGREES
REMARK 500 1 LEU A 146 CB - CG - CD2 ANGL. DEV. = -17.5 DEGREES
REMARK 500 1 LYS A 148 CA - C - N ANGL. DEV. = -16.4 DEGREES
REMARK 500 2 ASP A 43 N - CA - C ANGL. DEV. = -21.9 DEGREES
REMARK 500 2 HIS A 44 CA - CB - CG ANGL. DEV. = 18.4 DEGREES
REMARK 500 2 ASP A 47 N - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 2 LEU A 49 CB - CG - CD1 ANGL. DEV. = -11.5 DEGREES
REMARK 500 2 LEU A 49 CB - CG - CD2 ANGL. DEV. = -15.1 DEGREES
REMARK 500 2 GLU A 59 CA - C - N ANGL. DEV. = -14.3 DEGREES
REMARK 500 2 VAL A 68 CA - C - N ANGL. DEV. = -20.6 DEGREES
REMARK 500 2 VAL A 68 O - C - N ANGL. DEV. = 10.0 DEGREES
REMARK 500 2 ALA A 69 N - CA - CB ANGL. DEV. = -12.9 DEGREES
REMARK 500 2 ALA A 69 N - CA - C ANGL. DEV. = 21.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 325 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 ARG A 41 -54.51 -121.55
REMARK 500 1 ARG A 42 103.86 -169.09
REMARK 500 1 HIS A 44 -171.66 -9.11
REMARK 500 1 SER A 46 3.83 -171.30
REMARK 500 1 ASP A 54 94.69 -58.97
REMARK 500 1 LYS A 56 164.48 -29.42
REMARK 500 1 LEU A 61 -35.56 -37.72
REMARK 500 1 ASN A 65 143.47 -15.76
REMARK 500 1 ALA A 69 -131.91 -174.19
REMARK 500 1 VAL A 70 -114.57 139.29
REMARK 500 1 MET A 74 -159.43 -160.82
REMARK 500 1 MET A 75 -20.87 -141.87
REMARK 500 1 MET A 80 39.46 -151.73
REMARK 500 1 LYS A 82 -168.84 -115.71
REMARK 500 1 ALA A 83 109.24 -0.49
REMARK 500 1 GLN A 89 -140.03 -156.46
REMARK 500 1 ASP A 90 -136.29 -140.16
REMARK 500 1 VAL A 91 -37.14 -24.98
REMARK 500 1 ARG A 101 49.46 -109.94
REMARK 500 1 GLU A 106 -176.34 -55.12
REMARK 500 1 VAL A 108 59.44 2.34
REMARK 500 1 TYR A 109 -145.90 -93.32
REMARK 500 1 ASP A 117 -158.08 -112.29
REMARK 500 1 LYS A 130 109.34 -34.26
REMARK 500 1 GLU A 135 -147.34 -126.09
REMARK 500 1 LEU A 136 15.92 -22.48
REMARK 500 1 THR A 141 -43.74 -131.64
REMARK 500 1 LEU A 146 -92.58 -157.01
REMARK 500 2 ARG A 41 -155.05 -109.39
REMARK 500 2 HIS A 44 -76.74 -12.70
REMARK 500 2 SER A 46 64.02 172.75
REMARK 500 2 ASP A 54 -66.71 -18.75
REMARK 500 2 GLU A 59 -50.83 -29.96
REMARK 500 2 ASN A 65 119.97 -8.83
REMARK 500 2 MET A 74 -159.82 -164.45
REMARK 500 2 THR A 76 -166.12 -3.61
REMARK 500 2 ARG A 77 -96.26 -114.27
REMARK 500 2 ARG A 78 129.95 122.38
REMARK 500 2 LYS A 82 -30.00 102.94
REMARK 500 2 VAL A 91 -51.49 -26.66
REMARK 500 2 ARG A 101 69.28 -153.42
REMARK 500 2 ASP A 102 33.59 -88.33
REMARK 500 2 GLU A 106 -165.17 -79.35
REMARK 500 2 VAL A 108 -18.70 -46.76
REMARK 500 2 TYR A 109 -140.19 -83.41
REMARK 500 2 ASN A 110 -20.06 -38.49
REMARK 500 2 ASP A 117 -161.20 -110.73
REMARK 500 2 THR A 131 33.66 -76.76
REMARK 500 2 LYS A 132 -44.32 -141.93
REMARK 500 2 GLU A 135 -18.30 -160.73
REMARK 500
REMARK 500 THIS ENTRY HAS 235 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 LEU A 104 PRO A 105 8 -115.76
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 41 0.30 SIDE CHAIN
REMARK 500 1 ARG A 42 0.30 SIDE CHAIN
REMARK 500 1 ARG A 77 0.28 SIDE CHAIN
REMARK 500 1 ARG A 78 0.31 SIDE CHAIN
REMARK 500 1 ARG A 94 0.27 SIDE CHAIN
REMARK 500 1 ARG A 101 0.25 SIDE CHAIN
REMARK 500 1 ARG A 144 0.29 SIDE CHAIN
REMARK 500 2 ARG A 41 0.26 SIDE CHAIN
REMARK 500 2 ARG A 42 0.19 SIDE CHAIN
REMARK 500 2 ARG A 73 0.29 SIDE CHAIN
REMARK 500 2 ARG A 77 0.28 SIDE CHAIN
REMARK 500 2 ARG A 78 0.31 SIDE CHAIN
REMARK 500 2 ARG A 94 0.32 SIDE CHAIN
REMARK 500 2 ARG A 101 0.24 SIDE CHAIN
REMARK 500 2 ARG A 144 0.30 SIDE CHAIN
REMARK 500 3 ARG A 41 0.29 SIDE CHAIN
REMARK 500 3 ARG A 42 0.30 SIDE CHAIN
REMARK 500 3 ARG A 73 0.29 SIDE CHAIN
REMARK 500 3 ARG A 77 0.19 SIDE CHAIN
REMARK 500 3 ARG A 78 0.31 SIDE CHAIN
REMARK 500 3 ARG A 94 0.28 SIDE CHAIN
REMARK 500 3 ARG A 101 0.16 SIDE CHAIN
REMARK 500 3 ARG A 144 0.26 SIDE CHAIN
REMARK 500 4 ARG A 41 0.30 SIDE CHAIN
REMARK 500 4 ARG A 42 0.26 SIDE CHAIN
REMARK 500 4 ARG A 73 0.32 SIDE CHAIN
REMARK 500 4 ARG A 77 0.19 SIDE CHAIN
REMARK 500 4 ARG A 78 0.28 SIDE CHAIN
REMARK 500 4 ARG A 94 0.27 SIDE CHAIN
REMARK 500 4 ARG A 101 0.22 SIDE CHAIN
REMARK 500 4 ARG A 144 0.32 SIDE CHAIN
REMARK 500 5 ARG A 41 0.28 SIDE CHAIN
REMARK 500 5 ARG A 42 0.31 SIDE CHAIN
REMARK 500 5 ARG A 73 0.30 SIDE CHAIN
REMARK 500 5 ARG A 77 0.29 SIDE CHAIN
REMARK 500 5 ARG A 78 0.26 SIDE CHAIN
REMARK 500 5 ARG A 94 0.29 SIDE CHAIN
REMARK 500 5 ARG A 101 0.29 SIDE CHAIN
REMARK 500 5 ARG A 144 0.31 SIDE CHAIN
REMARK 500 6 ARG A 41 0.32 SIDE CHAIN
REMARK 500 6 ARG A 42 0.15 SIDE CHAIN
REMARK 500 6 ARG A 77 0.31 SIDE CHAIN
REMARK 500 6 ARG A 78 0.23 SIDE CHAIN
REMARK 500 6 ARG A 94 0.29 SIDE CHAIN
REMARK 500 6 ARG A 101 0.20 SIDE CHAIN
REMARK 500 6 ARG A 144 0.16 SIDE CHAIN
REMARK 500 7 ARG A 41 0.28 SIDE CHAIN
REMARK 500 7 ARG A 42 0.30 SIDE CHAIN
REMARK 500 7 ARG A 73 0.28 SIDE CHAIN
REMARK 500 7 ARG A 77 0.16 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 69 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KRS RELATED DB: PDB
DBREF 1KRT A 30 149 UNP P0A8N3 SYK1_ECOLI 26 148
SEQADV 1KRT A UNP P0A8N3 ASN 27 DELETION
SEQADV 1KRT A UNP P0A8N3 LEU 28 DELETION
SEQADV 1KRT A UNP P0A8N3 ARG 29 DELETION
SEQRES 1 A 120 ALA GLU GLN GLY ILE ALA PHE PRO ASN ASP PHE ARG ARG
SEQRES 2 A 120 ASP HIS THR SER ASP GLN LEU HIS ALA GLU PHE ASP GLY
SEQRES 3 A 120 LYS GLU ASN GLU GLU LEU GLU ALA LEU ASN ILE GLU VAL
SEQRES 4 A 120 ALA VAL ALA GLY ARG MET MET THR ARG ARG ILE MET GLY
SEQRES 5 A 120 LYS ALA SER PHE VAL THR LEU GLN ASP VAL GLY GLY ARG
SEQRES 6 A 120 ILE GLN LEU TYR VAL ALA ARG ASP ASP LEU PRO GLU GLY
SEQRES 7 A 120 VAL TYR ASN GLU GLN PHE LYS LYS TRP ASP LEU GLY ASP
SEQRES 8 A 120 ILE LEU GLY ALA LYS GLY LYS LEU PHE LYS THR LYS THR
SEQRES 9 A 120 GLY GLU LEU SER ILE HIS CYS THR GLU LEU ARG LEU LEU
SEQRES 10 A 120 THR LYS ALA
HELIX 1 1 ASP A 47 GLU A 52 1 6
HELIX 2 2 ASN A 58 ALA A 63 1 6
HELIX 3 3 GLN A 112 LYS A 115 1 4
SHEET 1 A 3 ILE A 95 VAL A 99 0
SHEET 2 A 3 SER A 84 GLN A 89 -1 N LEU A 88 O ILE A 95
SHEET 3 A 3 ARG A 73 ARG A 78 -1 N ARG A 78 O PHE A 85
SHEET 1 B 2 ALA A 124 PHE A 129 0
SHEET 2 B 2 SER A 137 LEU A 143 -1 N GLU A 142 O LYS A 125
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
(ATOM LINES ARE NOT SHOWN.)
END
