Header list of 5gat.pdb file
Complete list - r 16 2 Bytes
HEADER TRANSCRIPTION/DNA 07-NOV-97 5GAT
TITLE SOLUTION NMR STRUCTURE OF THE WILD TYPE DNA BINDING DOMAIN OF AREA
TITLE 2 COMPLEXED TO A 13BP DNA CONTAINING A CGATA SITE, 35 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(*CP*AP*GP*CP*GP*AP*TP*AP*GP*AP*GP*AP*C)-3');
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA (5'-D(*GP*TP*CP*TP*CP*TP*AP*TP*CP*GP*CP*TP*G)-3');
COMPND 7 CHAIN: C;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: NITROGEN REGULATORY PROTEIN AREA;
COMPND 11 CHAIN: A;
COMPND 12 FRAGMENT: DNA BINDING DOMAIN;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: EMERICELLA NIDULANS;
SOURCE 7 ORGANISM_TAXID: 162425;
SOURCE 8 ORGAN: TAIL;
SOURCE 9 GENE: POTENTIAL;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DNA BINDING PROTEIN, TRANSCRIPTION FACTOR, ZINC BINDING DOMAIN,
KEYWDS 2 COMPLEX (TRANSCRIPTION REGULATION-DNA), TRANSCRIPTION-DNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 35
AUTHOR G.M.CLORE,M.STARICH,M.WIKSTROM,A.M.GRONENBORN
REVDAT 4 16-MAR-22 5GAT 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 5GAT 1 VERSN
REVDAT 2 01-APR-03 5GAT 1 JRNL
REVDAT 1 28-JAN-98 5GAT 0
JRNL AUTH M.R.STARICH,M.WIKSTROM,H.N.ARST JR.,G.M.CLORE,A.M.GRONENBORN
JRNL TITL THE SOLUTION STRUCTURE OF A FUNGAL AREA PROTEIN-DNA COMPLEX:
JRNL TITL 2 AN ALTERNATIVE BINDING MODE FOR THE BASIC CARBOXYL TAIL OF
JRNL TITL 3 GATA FACTORS.
JRNL REF J.MOL.BIOL. V. 277 605 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9533883
JRNL DOI 10.1006/JMBI.1998.1625
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:
REMARK 3 THE STRUCTURES WERE CALCULATED USING THE SIMULATED
REMARK 3 ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT.
REMARK 3 229, 129 - 136 AND PROTEIN ENGINEERING 2, 27 - 38 USING
REMARK 3 THE PROGRAM X-PLOR MODIFIED TO INCORPORATE COUPLING
REMARK 3 CONSTANT RESTRAINTS (GARRETT ET AL. (1994) J. MAGN RESON.
REMARK 3 SERIES B 104, 99 - 103), CARBON CHEMICAL SHIFT RESTRAINTS
REMARK 3 (KUSZEWSKI ET AL. (1995) J. MAGN. RESON. SERIES B 106, 92
REMARK 3 - 96) RESTRAINTS, DIPOLAR COUPLING RESTRAINTS (TJANDRA ET
REMARK 3 AL. (1997) NATURE STRUCT BIOL 4, 732-738) AND A
REMARK 3 CONFORMATIONAL DATABASE POTENTIAL FOR PROTEINS AND NUCLEIC
REMARK 3 ACIDS (KUSZEWSKI ET AL. (1996) PROTEIN SCI 5, 1067 - 1080
REMARK 3 AND (1997) J. MAGN. RESON. 125, 171-177)
REMARK 3
REMARK 3 THE 3D STRUCTURE OF THE COMPLEX OF THE WILD TYPE AREA
REMARK 3 DBD-DNA COMPLEX WAS SOLVED BY MULTI-DIMENSIONAL
REMARK 3 HETERONUCLEAR-EDITED AND -FILTERED NMR IS BASED ON THE
REMARK 3 FOLLOWING 1098 EXPERIMENTAL RESTRAINTS
REMARK 3
REMARK 3 (A) PROTEIN: 119 SEQUENTIAL (|I-J|=1), 49 SHORT RANGE (1
REMARK 3 < |I-J| >=5), 68 LONG RANGE (|I-J|>5), AND 64 INTRARESIDUE
REMARK 3 APPROXIMATE INTERPROTON DISTANCE RESTRAINTS; NULL 124
REMARK 3 TORSION ANGLE RESTRAINTS (61 PHI, 8 PSI, 39 CHI1, 15 CHI2,
REMARK 3 AND 1 CHI3), 41 THREE-BOND HN-HA COUPLING CONSTANT
REMARK 3 RESTRAINTS; NULL 77 (41 CALPHA AND 36 CBETA) 13C CHEMICAL
REMARK 3 SHIFT RESTRAINTS; NULL 48 RESIDUAL N-H DIPOLAR COUPLING
REMARK 3 RESTRAINTS; 20 DISTANCE RESTRAINTS FOR 10 BACKBONE
REMARK 3 HYDROGEN BONDS.
REMARK 3
REMARK 3 (B) DNA: 75 INTRARESIDUE, 115 SEQUENTIAL INTRASTRAND AND
REMARK 3 20 INTERSTRAND INTERPROTON DISTANCE RESTRAINTS; 66
REMARK 3 DISTANCES FOR WATSON-CRICK BASE PAIR HYDROGEN BONDS; 170
REMARK 3 TORSION ANGLE RESTRAINTS FOR THE DNA BACKBONE COVERING
REMARK 3 VALUES CHARACTERISTIC OF BOTH A AND B DNA.
REMARK 3
REMARK 3 (C) 48 INTERMOLECULAR INTERPROTON DISTANCE RESTRAINTS
REMARK 3
REMARK 3 (D) 2 INTERMOLECULAR DISTANCE RESTRAINTS TO PHOSPHATES
REMARK 3
REMARK 3 (E) 8 'REPULSIVE' RESTRAINTS
REMARK 3
REMARK 3 (F) 4 DISTANCE RESTRAINTS FOR 2 INTERMOLECULAR H-BONDS
REMARK 3 BETWEEN ARG 24 AND BASE OF GUA5.
REMARK 3
REMARK 3 THE FOLLOWING TWO SETS OF COORDINATES DEFINE THE PRINCIPAL
REMARK 3 AXIS OF THE MAGNETIC SUSCEPTIBILITY TENSOR:
REMARK 3 MODEL 1
REMARK 3 POINT 1 102.092-193.887-255.981
REMARK 3 POINT 2 102.732-192.538-255.651
REMARK 3 MODEL 2
REMARK 3 POINT 1 86.136-234.098 -40.447
REMARK 3 POINT 2 86.796-232.777 -40.050
REMARK 3 MODEL 3
REMARK 3 POINT 1 134.979-162.786-132.132
REMARK 3 POINT 2 135.695-161.464-131.850
REMARK 3 MODEL 4
REMARK 3 POINT 1 -70.103 -54.685 51.419
REMARK 3 POINT 2 -69.500 -53.313 51.726
REMARK 3 MODEL 5
REMARK 3 POINT 1 135.883-100.066-174.175
REMARK 3 POINT 2 136.516 -98.700-173.898
REMARK 3 MODEL 6
REMARK 3 POINT 1 76.125-132.662-107.324
REMARK 3 POINT 2 76.655-131.248-107.078
REMARK 3 MODEL 7
REMARK 3 POINT 1 149.063-111.077 -36.611
REMARK 3 POINT 2 149.663-109.715 -36.255
REMARK 3 MODEL 8
REMARK 3 POINT 1 122.564 -99.258 13.431
REMARK 3 POINT 2 123.265 -97.930 13.723
REMARK 3 MODEL 9
REMARK 3 POINT 1 89.110 -79.702 -46.597
REMARK 3 POINT 2 89.824 -78.392 -46.258
REMARK 3 MODEL 10
REMARK 3 POINT 1 142.398 -66.526 -89.227
REMARK 3 POINT 2 143.080 -65.195 -88.905
REMARK 3 MODEL 11
REMARK 3 POINT 1 131.492-187.153 13.577
REMARK 3 POINT 2 132.170-185.854 14.018
REMARK 3 MODEL 12
REMARK 3 POINT 1 210.687-129.261-129.735
REMARK 3 POINT 2 211.314-127.906-129.402
REMARK 3 MODEL 13
REMARK 3 POINT 1 115.833-147.381-125.532
REMARK 3 POINT 2 116.493-146.040-125.205
REMARK 3 MODEL 14
REMARK 3 POINT 1 213.481 -97.161 -62.866
REMARK 3 POINT 2 214.099 -95.785 -62.612
REMARK 3 MODEL 15
REMARK 3 POINT 1 47.875-239.077 -96.187
REMARK 3 POINT 2 48.454-237.709 -95.820
REMARK 3 MODEL 16
REMARK 3 POINT 1 123.077-156.502-154.067
REMARK 3 POINT 2 123.774-155.182-153.731
REMARK 3 MODEL 17
REMARK 3 POINT 1 89.571 -78.309 3.456
REMARK 3 POINT 2 90.142 -76.928 3.784
REMARK 3 MODEL 18
REMARK 3 POINT 1 35.762-246.462 -37.437
REMARK 3 POINT 2 36.440-245.133 -37.101
REMARK 3 MODEL 19
REMARK 3 POINT 1 121.519-157.548 -7.594
REMARK 3 POINT 2 122.144-156.197 -7.236
REMARK 3 MODEL 20
REMARK 3 POINT 1 113.586 -86.299-148.635
REMARK 3 POINT 2 114.193 -84.935-148.298
REMARK 3 MODEL 21
REMARK 3 POINT 1 91.562-134.645 -78.697
REMARK 3 POINT 2 92.233-133.317 -78.335
REMARK 3 MODEL 22
REMARK 3 POINT 1 118.977-218.365-122.566
REMARK 3 POINT 2 119.576-217.008-122.192
REMARK 3 MODEL 23
REMARK 3 POINT 1 80.952-182.035 -80.709
REMARK 3 POINT 2 81.615-180.694 -80.392
REMARK 3 MODEL 24
REMARK 3 POINT 1 188.361-123.949-146.548
REMARK 3 POINT 2 189.022-122.608-146.225
REMARK 3 MODEL 25
REMARK 3 POINT 1 114.771-280.049 -48.411
REMARK 3 POINT 2 115.463-278.730 -48.065
REMARK 3 MODEL 26
REMARK 3 POINT 1 161.250-143.808 74.628
REMARK 3 POINT 2 161.956-142.504 75.004
REMARK 3 MODEL 27
REMARK 3 POINT 1 143.106-116.338 -57.993
REMARK 3 POINT 2 143.761-114.989 -57.690
REMARK 3 MODEL 28
REMARK 3 POINT 1 114.944-162.825 -21.630
REMARK 3 POINT 2 115.575-161.468 -21.310
REMARK 3 MODEL 29
REMARK 3 POINT 1 89.010-134.313-122.747
REMARK 3 POINT 2 89.573-132.932-122.407
REMARK 3 MODEL 30
REMARK 3 POINT 1 81.718-198.065 -81.738
REMARK 3 POINT 2 82.448-196.759 -81.416
REMARK 3 MODEL 31
REMARK 3 POINT 1 177.911-171.893 -37.695
REMARK 3 POINT 2 178.512-170.518 -37.399
REMARK 3 MODEL 32
REMARK 3 POINT 1 100.216-159.685-185.688
REMARK 3 POINT 2 100.906-158.386-185.268
REMARK 3 MODEL 33
REMARK 3 POINT 1 64.235-177.747 -56.722
REMARK 3 POINT 2 64.894-176.431 -56.302
REMARK 3 MODEL 34
REMARK 3 POINT 1 237.150 -92.701 -2.650
REMARK 3 POINT 2 237.781 -91.352 -2.296
REMARK 3 MODEL 35
REMARK 3 POINT 1 91.957-116.106 -54.093
REMARK 3 POINT 2 92.589-114.744 -53.797
REMARK 4
REMARK 4 5GAT 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_1000179712.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.1
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 : 360 MHZ; 500 MHZ; 600 MHZ; 750
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : AM360; AMX500; DMX500; AMX600;
REMARK 210 DMX600; DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR MODIFIED MODIFIED
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 35
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 35
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: DATA WERE RECORDED ON A 1:1 COMPLEX
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, 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 O ASN A 26 H GLY A 29 1.59
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 DT B 107 C5 DT B 107 C7 0.040
REMARK 500 1 DT C 115 C5 DT C 115 C7 0.037
REMARK 500 1 DT C 121 C5 DT C 121 C7 0.040
REMARK 500 2 DT B 107 C5 DT B 107 C7 0.039
REMARK 500 2 DT C 115 C5 DT C 115 C7 0.037
REMARK 500 2 DT C 119 C5 DT C 119 C7 0.037
REMARK 500 2 DT C 121 C5 DT C 121 C7 0.041
REMARK 500 3 DT B 107 C5 DT B 107 C7 0.038
REMARK 500 3 DT C 117 C5 DT C 117 C7 0.037
REMARK 500 3 DT C 121 C5 DT C 121 C7 0.039
REMARK 500 3 DT C 125 C5 DT C 125 C7 0.036
REMARK 500 4 DT B 107 C5 DT B 107 C7 0.036
REMARK 500 4 DT C 121 C5 DT C 121 C7 0.036
REMARK 500 4 DT C 125 C5 DT C 125 C7 0.038
REMARK 500 5 DT C 121 C5 DT C 121 C7 0.040
REMARK 500 5 DT C 125 C5 DT C 125 C7 0.037
REMARK 500 6 DT B 107 C5 DT B 107 C7 0.039
REMARK 500 6 DT C 121 C5 DT C 121 C7 0.038
REMARK 500 7 DT B 107 C5 DT B 107 C7 0.038
REMARK 500 7 DT C 121 C5 DT C 121 C7 0.041
REMARK 500 8 DT C 115 C5 DT C 115 C7 0.037
REMARK 500 8 DT C 117 C5 DT C 117 C7 0.037
REMARK 500 8 DT C 119 C5 DT C 119 C7 0.037
REMARK 500 8 DT C 121 C5 DT C 121 C7 0.038
REMARK 500 8 DT C 125 C5 DT C 125 C7 0.038
REMARK 500 9 DT B 107 C5 DT B 107 C7 0.038
REMARK 500 9 DT C 115 C5 DT C 115 C7 0.037
REMARK 500 9 DT C 119 C5 DT C 119 C7 0.037
REMARK 500 9 DT C 121 C5 DT C 121 C7 0.040
REMARK 500 10 DT B 107 C5 DT B 107 C7 0.037
REMARK 500 10 DT C 117 C5 DT C 117 C7 0.038
REMARK 500 10 DT C 121 C5 DT C 121 C7 0.040
REMARK 500 10 DT C 125 C5 DT C 125 C7 0.038
REMARK 500 11 DT B 107 C5 DT B 107 C7 0.037
REMARK 500 11 DT C 115 C5 DT C 115 C7 0.036
REMARK 500 11 DT C 121 C5 DT C 121 C7 0.041
REMARK 500 11 DT C 125 C5 DT C 125 C7 0.037
REMARK 500 12 DT B 107 C5 DT B 107 C7 0.037
REMARK 500 12 DT C 115 C5 DT C 115 C7 0.036
REMARK 500 12 DT C 117 C5 DT C 117 C7 0.039
REMARK 500 12 DT C 121 C5 DT C 121 C7 0.044
REMARK 500 13 DT B 107 C5 DT B 107 C7 0.037
REMARK 500 13 DT C 115 C5 DT C 115 C7 0.036
REMARK 500 13 DT C 119 C5 DT C 119 C7 0.037
REMARK 500 13 DT C 121 C5 DT C 121 C7 0.040
REMARK 500 14 DT C 115 C5 DT C 115 C7 0.036
REMARK 500 14 DT C 121 C5 DT C 121 C7 0.037
REMARK 500 14 DT C 125 C5 DT C 125 C7 0.037
REMARK 500 15 DT B 107 C5 DT B 107 C7 0.037
REMARK 500 15 DT C 119 C5 DT C 119 C7 0.038
REMARK 500
REMARK 500 THIS ENTRY HAS 116 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 DA B 102 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 1 DG B 103 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 1 DG B 105 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 1 DA B 106 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 1 DT B 107 O4' - C1' - N1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 1 DA B 108 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 1 DG B 109 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 1 DA B 110 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 1 DG B 111 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 1 DA B 112 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DC B 113 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 1 DG C 114 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 1 DT C 115 O4' - C1' - N1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 1 DC C 116 O4' - C1' - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 1 DT C 117 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 1 DC C 118 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 1 DT C 119 O4' - C1' - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 1 DA C 120 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DT C 121 O4' - C1' - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 1 DC C 122 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 1 DG C 123 O4' - C1' - N9 ANGL. DEV. = 3.4 DEGREES
REMARK 500 1 DC C 124 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 1 DT C 125 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 1 DG C 126 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 2 DA B 102 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 2 DG B 103 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 2 DC B 104 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 2 DG B 105 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 2 DA B 106 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 2 DT B 107 O4' - C1' - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 2 DA B 108 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 2 DG B 109 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 2 DA B 110 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 2 DG B 111 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 2 DA B 112 O4' - C1' - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 2 DC B 113 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 2 DG C 114 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 2 DT C 115 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 2 DC C 116 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 2 DT C 117 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 2 DC C 118 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 2 DT C 119 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 2 DA C 120 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 2 DT C 121 O4' - C1' - N1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 2 DC C 122 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 2 DG C 123 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 2 DC C 124 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 2 DT C 125 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 2 DG C 126 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 3 DC B 101 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 886 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 GLU A 5 -148.02 -70.01
REMARK 500 1 ASN A 7 -26.32 -142.47
REMARK 500 1 PRO A 27 -7.65 -44.22
REMARK 500 1 CYS A 33 -138.87 -86.90
REMARK 500 1 ASN A 34 -71.66 -82.81
REMARK 500 1 PRO A 48 113.49 -34.52
REMARK 500 1 ASN A 60 -179.21 -65.81
REMARK 500 2 ASN A 7 -51.77 -137.39
REMARK 500 2 PRO A 9 160.37 -39.94
REMARK 500 2 PHE A 16 3.89 55.70
REMARK 500 2 PRO A 27 -7.92 -45.99
REMARK 500 2 CYS A 33 -137.81 -86.16
REMARK 500 2 ASN A 34 -70.66 -83.21
REMARK 500 2 VAL A 46 119.22 -37.40
REMARK 500 2 ARG A 47 102.52 -41.52
REMARK 500 3 LYS A 2 -140.68 49.63
REMARK 500 3 GLU A 5 -91.40 0.89
REMARK 500 3 ASN A 7 -110.21 -0.76
REMARK 500 3 PRO A 9 48.86 -61.65
REMARK 500 3 PRO A 27 -9.34 -42.96
REMARK 500 3 CYS A 33 -144.66 -82.19
REMARK 500 3 VAL A 46 153.41 -49.89
REMARK 500 3 PRO A 48 96.42 -35.48
REMARK 500 3 SER A 50 -5.82 -56.70
REMARK 500 3 ASN A 60 -159.54 -80.79
REMARK 500 4 LYS A 2 -141.24 50.06
REMARK 500 4 GLU A 5 89.97 -46.29
REMARK 500 4 ASN A 7 -93.45 -161.91
REMARK 500 4 PRO A 9 -170.19 -68.26
REMARK 500 4 PHE A 16 5.27 56.13
REMARK 500 4 PRO A 27 -11.87 -44.53
REMARK 500 4 CYS A 33 -140.39 -84.19
REMARK 500 4 ASN A 34 -70.73 -82.11
REMARK 500 4 PRO A 48 96.21 -47.51
REMARK 500 4 ASN A 60 -161.15 -76.80
REMARK 500 5 PHE A 16 1.41 56.39
REMARK 500 5 PRO A 27 -6.79 -47.20
REMARK 500 5 CYS A 33 -140.45 -83.14
REMARK 500 5 PRO A 48 104.88 -40.38
REMARK 500 5 ASN A 60 -162.27 -78.69
REMARK 500 6 GLN A 6 78.13 -65.84
REMARK 500 6 PRO A 9 25.76 -74.04
REMARK 500 6 PHE A 16 4.86 58.75
REMARK 500 6 PRO A 27 -10.60 -44.12
REMARK 500 6 CYS A 33 -134.07 -85.00
REMARK 500 6 ASN A 34 -83.11 -83.19
REMARK 500 6 PRO A 48 108.65 -34.27
REMARK 500 6 LEU A 49 -8.39 -59.69
REMARK 500 6 ASN A 60 -163.33 -78.87
REMARK 500 7 GLN A 6 -99.77 -98.65
REMARK 500
REMARK 500 THIS ENTRY HAS 249 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 67 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 12 SG
REMARK 620 2 CYS A 15 SG 109.1
REMARK 620 3 CYS A 33 SG 109.0 110.3
REMARK 620 4 CYS A 36 SG 109.5 110.9 108.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 67
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GAT RELATED DB: PDB
REMARK 900 REGULARIZED MEAN STRUCTURE
DBREF 5GAT A 1 66 UNP P17429 AREA_EMENI 662 727
DBREF 5GAT B 101 113 PDB 5GAT 5GAT 101 113
DBREF 5GAT C 114 126 PDB 5GAT 5GAT 114 126
SEQADV 5GAT MET A 1 UNP P17429 THR 662 CONFLICT
SEQRES 1 B 13 DC DA DG DC DG DA DT DA DG DA DG DA DC
SEQRES 1 C 13 DG DT DC DT DC DT DA DT DC DG DC DT DG
SEQRES 1 A 66 MET LYS ASN GLY GLU GLN ASN GLY PRO THR THR CYS THR
SEQRES 2 A 66 ASN CYS PHE THR GLN THR THR PRO LEU TRP ARG ARG ASN
SEQRES 3 A 66 PRO GLU GLY GLN PRO LEU CYS ASN ALA CYS GLY LEU PHE
SEQRES 4 A 66 LEU LYS LEU HIS GLY VAL VAL ARG PRO LEU SER LEU LYS
SEQRES 5 A 66 THR ASP VAL ILE LYS LYS ARG ASN ARG ASN SER ALA ASN
SEQRES 6 A 66 SER
HET ZN A 67 1
HETNAM ZN ZINC ION
FORMUL 4 ZN ZN 2+
HELIX 1 1 ALA A 35 HIS A 43 1 9
HELIX 2 2 LEU A 49 LEU A 51 5 3
SHEET 1 A 2 ARG A 24 ASN A 26 0
SHEET 2 A 2 GLN A 30 LEU A 32 -1 N LEU A 32 O ARG A 24
LINK SG CYS A 12 ZN ZN A 67 1555 1555 2.30
LINK SG CYS A 15 ZN ZN A 67 1555 1555 2.30
LINK SG CYS A 33 ZN ZN A 67 1555 1555 2.29
LINK SG CYS A 36 ZN ZN A 67 1555 1555 2.29
SITE 1 AC1 4 CYS A 12 CYS A 15 CYS A 33 CYS A 36
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