HEADER TRANSCRIPTION 21-FEB-07 2JHE
TITLE N-TERMINAL DOMAIN OF TYRR TRANSCRIPTION FACTOR (RESIDUES 1 - 190)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION REGULATOR TYRR;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 1-190;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 83333
KEYWDS TRANSCRIPTION, AROMATIC HYDROCARBONS CATABOLISM, TYRR PROTEIN,
KEYWDS 2 NUCLEOTIDE-BINDING, TRANSCRIPTION REGULATION, ACTIVATOR, REPRESSOR,
KEYWDS 3 ATP-BINDING, DNA-BINDING, TWO-COMPONENT REGULATORY SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR D.VERGER,P.D.CARR,T.KWOK,D.L.OLLIS
REVDAT 5 24-JAN-18 2JHE 1 SOURCE
REVDAT 4 13-JUL-11 2JHE 1 VERSN
REVDAT 3 09-JUN-09 2JHE 1 REMARK
REVDAT 2 24-FEB-09 2JHE 1 VERSN
REVDAT 1 24-JUN-08 2JHE 0
JRNL AUTH D.VERGER,P.D.CARR,T.KWOK,D.L.OLLIS
JRNL TITL CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF THE TYRR
JRNL TITL 2 TRANSCRIPTION FACTOR RESPONSIBLE FOR GENE REGULATION OF
JRNL TITL 3 AROMATIC AMINO ACID BIOSYNTHESIS AND TRANSPORT IN
JRNL TITL 4 ESCHERICHIA COLI K12
JRNL REF J.MOL.BIOL. V. 367 102 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17222426
JRNL DOI 10.1016/J.JMB.2006.12.018
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 38114
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.252
REMARK 3 R VALUE (WORKING SET) : 0.248
REMARK 3 FREE R VALUE : 0.317
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1967
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2668
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.2660
REMARK 3 BIN FREE R VALUE SET COUNT : 139
REMARK 3 BIN FREE R VALUE : 0.3610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5716
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 146
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.15000
REMARK 3 B22 (A**2) : -0.65000
REMARK 3 B33 (A**2) : 2.46000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.14000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.373
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.293
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.244
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.346
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.919
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.866
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5846 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7934 ; 1.871 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 746 ; 8.241 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 258 ;35.545 ;23.566
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 939 ;20.978 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;23.219 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 939 ; 0.128 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4399 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2599 ; 0.264 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3935 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 245 ; 0.178 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 76 ; 0.245 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.403 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3907 ; 0.889 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5994 ; 1.410 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2179 ; 2.327 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1940 ; 3.471 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 75
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7920 2.6860 16.5630
REMARK 3 T TENSOR
REMARK 3 T11: -0.1858 T22: -0.1737
REMARK 3 T33: -0.3385 T12: 0.0605
REMARK 3 T13: 0.0024 T23: 0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 7.5680 L22: 3.9258
REMARK 3 L33: 3.4933 L12: 0.1564
REMARK 3 L13: -1.2559 L23: -2.1656
REMARK 3 S TENSOR
REMARK 3 S11: 0.0288 S12: -0.4119 S13: -0.1709
REMARK 3 S21: 0.2441 S22: 0.0327 S23: -0.1018
REMARK 3 S31: -0.1622 S32: 0.0346 S33: -0.0614
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 84 A 190
REMARK 3 ORIGIN FOR THE GROUP (A): 47.1370 16.9660 17.8900
REMARK 3 T TENSOR
REMARK 3 T11: 0.0162 T22: -0.0444
REMARK 3 T33: 0.5592 T12: 0.0421
REMARK 3 T13: -0.0039 T23: -0.0311
REMARK 3 L TENSOR
REMARK 3 L11: 4.4434 L22: 2.6339
REMARK 3 L33: 3.2700 L12: 0.0695
REMARK 3 L13: 1.0165 L23: -1.4351
REMARK 3 S TENSOR
REMARK 3 S11: -0.1184 S12: -0.0846 S13: 0.9946
REMARK 3 S21: -0.0386 S22: 0.1308 S23: -0.3377
REMARK 3 S31: -0.3264 S32: 0.0470 S33: -0.0124
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 75
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8750 11.3770 -1.5150
REMARK 3 T TENSOR
REMARK 3 T11: -0.1635 T22: -0.1430
REMARK 3 T33: -0.3355 T12: 0.0573
REMARK 3 T13: 0.0293 T23: 0.0491
REMARK 3 L TENSOR
REMARK 3 L11: 4.9762 L22: 3.1753
REMARK 3 L33: 4.2042 L12: 0.6257
REMARK 3 L13: 0.1937 L23: -1.8067
REMARK 3 S TENSOR
REMARK 3 S11: -0.0581 S12: 0.5423 S13: 0.3861
REMARK 3 S21: -0.0981 S22: 0.1648 S23: 0.1544
REMARK 3 S31: -0.1279 S32: -0.1853 S33: -0.1067
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 84 B 190
REMARK 3 ORIGIN FOR THE GROUP (A): 48.2370 -2.8960 18.4650
REMARK 3 T TENSOR
REMARK 3 T11: -0.1829 T22: -0.1156
REMARK 3 T33: -0.0149 T12: 0.0760
REMARK 3 T13: -0.0512 T23: -0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 2.6812 L22: 2.2376
REMARK 3 L33: 1.8225 L12: 0.8242
REMARK 3 L13: 0.1694 L23: -0.8766
REMARK 3 S TENSOR
REMARK 3 S11: 0.0640 S12: 0.0500 S13: 0.0598
REMARK 3 S21: -0.0697 S22: 0.0433 S23: -0.0669
REMARK 3 S31: 0.1038 S32: 0.0353 S33: -0.1074
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 75
REMARK 3 ORIGIN FOR THE GROUP (A): -0.2880 6.6790 66.6100
REMARK 3 T TENSOR
REMARK 3 T11: -0.1136 T22: -0.0491
REMARK 3 T33: -0.2891 T12: -0.0378
REMARK 3 T13: -0.0282 T23: 0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 4.7827 L22: 4.3752
REMARK 3 L33: 4.2633 L12: 1.2434
REMARK 3 L13: 0.2517 L23: 1.5324
REMARK 3 S TENSOR
REMARK 3 S11: 0.1497 S12: -0.0719 S13: -0.3484
REMARK 3 S21: 0.5284 S22: 0.0118 S23: -0.4443
REMARK 3 S31: 0.5098 S32: 0.0127 S33: -0.1615
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 84 C 188
REMARK 3 ORIGIN FOR THE GROUP (A): 38.1230 16.4940 66.4950
REMARK 3 T TENSOR
REMARK 3 T11: -0.0759 T22: -0.1312
REMARK 3 T33: -0.0272 T12: 0.0119
REMARK 3 T13: -0.0323 T23: -0.0281
REMARK 3 L TENSOR
REMARK 3 L11: 5.0700 L22: 5.8943
REMARK 3 L33: 2.4859 L12: -0.9139
REMARK 3 L13: -0.5025 L23: -1.3081
REMARK 3 S TENSOR
REMARK 3 S11: 0.0732 S12: 0.3752 S13: -0.1070
REMARK 3 S21: -0.2406 S22: 0.0461 S23: 0.3343
REMARK 3 S31: -0.1249 S32: -0.0349 S33: -0.1194
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 75
REMARK 3 ORIGIN FOR THE GROUP (A): 6.6590 14.0960 49.2510
REMARK 3 T TENSOR
REMARK 3 T11: -0.1842 T22: 0.1115
REMARK 3 T33: -0.2793 T12: -0.0203
REMARK 3 T13: 0.0265 T23: -0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 6.6543 L22: 3.6777
REMARK 3 L33: 5.9358 L12: 0.6437
REMARK 3 L13: 2.0620 L23: -1.4714
REMARK 3 S TENSOR
REMARK 3 S11: 0.1458 S12: 0.6781 S13: 0.0331
REMARK 3 S21: -0.2730 S22: 0.0409 S23: -0.2571
REMARK 3 S31: -0.1311 S32: 0.3477 S33: -0.1867
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 84 D 190
REMARK 3 ORIGIN FOR THE GROUP (A): 38.9400 -2.6710 73.0470
REMARK 3 T TENSOR
REMARK 3 T11: -0.1528 T22: -0.2351
REMARK 3 T33: 0.2086 T12: 0.0003
REMARK 3 T13: -0.0797 T23: -0.0311
REMARK 3 L TENSOR
REMARK 3 L11: 4.1917 L22: 6.3709
REMARK 3 L33: 3.1949 L12: 1.0036
REMARK 3 L13: -0.0657 L23: -0.8186
REMARK 3 S TENSOR
REMARK 3 S11: 0.1969 S12: 0.1626 S13: -0.8752
REMARK 3 S21: 0.1930 S22: 0.0117 S23: 0.3727
REMARK 3 S31: 0.2331 S32: -0.1345 S33: -0.2086
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2JHE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-FEB-07.
REMARK 100 THE DEPOSITION ID IS D_1290030882.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.969
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40199
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 24.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 12.80
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.31 M AMMONIUM SULFATE, 33% PEG-MME
REMARK 280 5000, 0.1 M MES, PH 6.3
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 67.22800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.00450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 67.22800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.00450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 400
REMARK 400 COMPOUND
REMARK 400 INVOLVED IN TRANSCRIPTIONAL REGULATION OF AROMATIC AMINO
REMARK 400 ACID BIOSYNTHESIS AND TRANSPORT. MODULATES THE EXPRESSION OF AT
REMARK 400 LEAST 8 UNLINKED OPERONS. SEVEN OF THESE OPERONS ARE REGULATED IN
REMARK 400 RESPONSE TO CHANGES IN THE CONCENTRATION OF THE THREE AROMATIC
REMARK 400 AMINO ACIDS (PHENYLALANINE, TYROSINE AND TRYPTOPHAN).
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 177
REMARK 465 GLY B 177
REMARK 465 GLY C 177
REMARK 465 GLY C 189
REMARK 465 ARG C 190
REMARK 465 GLY D 177
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ILE A 36 CG1 CG2 CD1
REMARK 470 GLU A 45 CG CD OE1 OE2
REMARK 470 GLU A 47 CG CD OE1 OE2
REMARK 470 PHE A 48 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 49 CG CD OE1 OE2
REMARK 470 GLU A 91 CG CD OE1 OE2
REMARK 470 LYS A 99 CG CD CE NZ
REMARK 470 SER A 100 OG
REMARK 470 LYS A 101 CG CD CE NZ
REMARK 470 LYS A 116 CG CD CE NZ
REMARK 470 ARG A 119 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 130 CG OD1 ND2
REMARK 470 LEU A 135 CG CD1 CD2
REMARK 470 ARG A 136 CG CD NE CZ NH1 NH2
REMARK 470 TRP A 137 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 137 CZ3 CH2
REMARK 470 GLU A 139 CG CD OE1 OE2
REMARK 470 GLU A 141 CG CD OE1 OE2
REMARK 470 GLN A 143 CG CD OE1 NE2
REMARK 470 ASP A 144 CG OD1 OD2
REMARK 470 ASN A 153 CG OD1 ND2
REMARK 470 GLN A 167 CG CD OE1 NE2
REMARK 470 ASP A 168 CG OD1 OD2
REMARK 470 GLU A 169 CG CD OE1 OE2
REMARK 470 ASN A 170 CG OD1 ND2
REMARK 470 THR A 176 OG1 CG2
REMARK 470 LEU A 182 CG CD1 CD2
REMARK 470 ILE A 186 CG1 CG2 CD1
REMARK 470 ARG A 187 CG CD NE CZ NH1 NH2
REMARK 470 MET A 188 CG SD CE
REMARK 470 ARG A 190 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 11 CG CD1 CD2
REMARK 470 SER B 53 OG
REMARK 470 LYS B 99 CG CD CE NZ
REMARK 470 GLN B 111 CG CD OE1 NE2
REMARK 470 LYS B 116 CG CD CE NZ
REMARK 470 GLU B 169 CG CD OE1 OE2
REMARK 470 ASN B 170 CG OD1 ND2
REMARK 470 GLN B 172 CG CD OE1 NE2
REMARK 470 THR B 176 OG1 CG2
REMARK 470 LEU B 182 CG CD1 CD2
REMARK 470 ILE B 186 CG1 CG2 CD1
REMARK 470 ARG B 187 CG CD NE CZ NH1 NH2
REMARK 470 MET B 188 CG SD CE
REMARK 470 ARG B 190 CG CD NE CZ NH1 NH2
REMARK 470 ILE C 36 CG1 CG2 CD1
REMARK 470 TRP C 72 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP C 72 CZ3 CH2
REMARK 470 LYS C 99 CG CD CE NZ
REMARK 470 LYS C 116 CG CD CE NZ
REMARK 470 ASN C 122 CG OD1 ND2
REMARK 470 LEU C 135 CG CD1 CD2
REMARK 470 GLU C 141 CG CD OE1 OE2
REMARK 470 TYR C 165 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU C 166 CG CD1 CD2
REMARK 470 GLN C 167 CG CD OE1 NE2
REMARK 470 ASP C 168 CG OD1 OD2
REMARK 470 GLU C 169 CG CD OE1 OE2
REMARK 470 ASN C 170 CG OD1 ND2
REMARK 470 LEU C 182 CG CD1 CD2
REMARK 470 ILE C 186 CG1 CG2 CD1
REMARK 470 ARG C 187 CG CD NE CZ NH1 NH2
REMARK 470 MET C 188 CG SD CE
REMARK 470 ILE D 36 CG1 CG2 CD1
REMARK 470 GLU D 45 CG CD OE1 OE2
REMARK 470 LEU D 46 CG CD1 CD2
REMARK 470 GLU D 47 CG CD OE1 OE2
REMARK 470 PHE D 48 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE D 51 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS D 99 CG CD CE NZ
REMARK 470 LYS D 101 CG CD CE NZ
REMARK 470 GLN D 115 CG CD OE1 NE2
REMARK 470 LYS D 116 CG CD CE NZ
REMARK 470 ASP D 118 CG OD1 OD2
REMARK 470 ARG D 119 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 121 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 141 CG CD OE1 OE2
REMARK 470 GLN D 155 CG CD OE1 NE2
REMARK 470 LEU D 166 CG CD1 CD2
REMARK 470 ASN D 170 CG OD1 ND2
REMARK 470 ASP D 171 CG OD1 OD2
REMARK 470 GLN D 172 CG CD OE1 NE2
REMARK 470 THR D 176 OG1 CG2
REMARK 470 LEU D 182 CG CD1 CD2
REMARK 470 ILE D 186 CG1 CG2 CD1
REMARK 470 ARG D 187 CG CD NE CZ NH1 NH2
REMARK 470 MET D 188 CG SD CE
REMARK 470 ARG D 190 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 CG2 THR C 176 CG2 VAL C 180 1.94
REMARK 500 O VAL B 96 CB GLU B 169 2.09
REMARK 500 O LEU A 94 NE2 GLN A 172 2.11
REMARK 500 O THR D 176 N ALA D 178 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O ILE B 36 ND2 ASN D 133 4556 1.87
REMARK 500 NH1 ARG B 59 OE1 GLU C 49 1554 2.04
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 GLU B 49 CG GLU B 49 CD 0.099
REMARK 500 THR B 176 C ALA B 178 N 0.292
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 ARG A 2 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 59 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 59 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 VAL B 67 CB - CA - C ANGL. DEV. = -12.7 DEGREES
REMARK 500 THR B 176 CA - C - N ANGL. DEV. = 16.9 DEGREES
REMARK 500 THR B 176 O - C - N ANGL. DEV. = -17.6 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 ASP A 66 159.06 177.50
REMARK 500 LEU A 89 113.30 -35.19
REMARK 500 LEU A 94 143.03 -175.11
REMARK 500 ASP A 103 -88.35 -113.15
REMARK 500 SER A 140 -4.34 -58.52
REMARK 500 TYR A 165 102.59 49.72
REMARK 500 LEU A 166 -113.62 50.64
REMARK 500 GLU A 169 -136.98 139.39
REMARK 500 ARG A 187 42.96 -67.38
REMARK 500 MET A 188 -41.10 -136.80
REMARK 500 SER B 100 17.08 57.85
REMARK 500 ASP B 103 -66.92 -98.87
REMARK 500 TYR B 165 -141.54 66.94
REMARK 500 GLN B 167 101.77 4.73
REMARK 500 GLU B 169 -130.76 163.03
REMARK 500 ASP C 9 97.36 -68.42
REMARK 500 ILE C 36 -6.30 -55.29
REMARK 500 ALA C 44 -137.41 -80.50
REMARK 500 GLU C 45 58.77 -43.98
REMARK 500 ARG C 77 99.10 -39.76
REMARK 500 GLU C 78 0.40 83.58
REMARK 500 ASP C 103 -72.66 -89.99
REMARK 500 ALA C 105 131.52 -172.83
REMARK 500 LEU C 166 75.77 67.40
REMARK 500 GLU C 169 -141.97 166.08
REMARK 500 ASN C 170 140.97 -170.07
REMARK 500 ARG C 187 -35.50 -33.39
REMARK 500 GLU D 45 126.10 -11.31
REMARK 500 GLU D 47 148.64 -33.75
REMARK 500 PHE D 48 -10.45 -43.73
REMARK 500 GLU D 49 40.92 172.85
REMARK 500 ASN D 153 84.29 30.86
REMARK 500 LEU D 166 74.07 53.83
REMARK 500 GLN D 167 102.83 -40.00
REMARK 500 GLU D 169 -148.93 158.51
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 B 166 GLN B 167 -145.58
REMARK 500 GLU C 78 HIS C 79 144.31
REMARK 500 GLU D 49 SER D 50 140.56
REMARK 500 TYR D 165 LEU D 166 -125.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 THR C 176 11.44
REMARK 500 THR D 176 15.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2001 DISTANCE = 5.81 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PG4 A 1192
REMARK 610 PG4 C 1189
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AE3 A 1191
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 1192
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1191
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 C 1189
DBREF 2JHE A 1 190 UNP P07604 TYRR_ECOLI 1 190
DBREF 2JHE B 1 190 UNP P07604 TYRR_ECOLI 1 190
DBREF 2JHE C 1 190 UNP P07604 TYRR_ECOLI 1 190
DBREF 2JHE D 1 190 UNP P07604 TYRR_ECOLI 1 190
SEQRES 1 A 190 MET ARG LEU GLU VAL PHE CYS GLU ASP ARG LEU GLY LEU
SEQRES 2 A 190 THR ARG GLU LEU LEU ASP LEU LEU VAL LEU ARG GLY ILE
SEQRES 3 A 190 ASP LEU ARG GLY ILE GLU ILE ASP PRO ILE GLY ARG ILE
SEQRES 4 A 190 TYR LEU ASN PHE ALA GLU LEU GLU PHE GLU SER PHE SER
SEQRES 5 A 190 SER LEU MET ALA GLU ILE ARG ARG ILE ALA GLY VAL THR
SEQRES 6 A 190 ASP VAL ARG THR VAL PRO TRP MET PRO SER GLU ARG GLU
SEQRES 7 A 190 HIS LEU ALA LEU SER ALA LEU LEU GLU ALA LEU PRO GLU
SEQRES 8 A 190 PRO VAL LEU SER VAL ASP MET LYS SER LYS VAL ASP MET
SEQRES 9 A 190 ALA ASN PRO ALA SER CYS GLN LEU PHE GLY GLN LYS LEU
SEQRES 10 A 190 ASP ARG LEU ARG ASN HIS THR ALA ALA GLN LEU ILE ASN
SEQRES 11 A 190 GLY PHE ASN PHE LEU ARG TRP LEU GLU SER GLU PRO GLN
SEQRES 12 A 190 ASP SER HIS ASN GLU HIS VAL VAL ILE ASN GLY GLN ASN
SEQRES 13 A 190 PHE LEU MET GLU ILE THR PRO VAL TYR LEU GLN ASP GLU
SEQRES 14 A 190 ASN ASP GLN HIS VAL LEU THR GLY ALA VAL VAL MET LEU
SEQRES 15 A 190 ARG SER THR ILE ARG MET GLY ARG
SEQRES 1 B 190 MET ARG LEU GLU VAL PHE CYS GLU ASP ARG LEU GLY LEU
SEQRES 2 B 190 THR ARG GLU LEU LEU ASP LEU LEU VAL LEU ARG GLY ILE
SEQRES 3 B 190 ASP LEU ARG GLY ILE GLU ILE ASP PRO ILE GLY ARG ILE
SEQRES 4 B 190 TYR LEU ASN PHE ALA GLU LEU GLU PHE GLU SER PHE SER
SEQRES 5 B 190 SER LEU MET ALA GLU ILE ARG ARG ILE ALA GLY VAL THR
SEQRES 6 B 190 ASP VAL ARG THR VAL PRO TRP MET PRO SER GLU ARG GLU
SEQRES 7 B 190 HIS LEU ALA LEU SER ALA LEU LEU GLU ALA LEU PRO GLU
SEQRES 8 B 190 PRO VAL LEU SER VAL ASP MET LYS SER LYS VAL ASP MET
SEQRES 9 B 190 ALA ASN PRO ALA SER CYS GLN LEU PHE GLY GLN LYS LEU
SEQRES 10 B 190 ASP ARG LEU ARG ASN HIS THR ALA ALA GLN LEU ILE ASN
SEQRES 11 B 190 GLY PHE ASN PHE LEU ARG TRP LEU GLU SER GLU PRO GLN
SEQRES 12 B 190 ASP SER HIS ASN GLU HIS VAL VAL ILE ASN GLY GLN ASN
SEQRES 13 B 190 PHE LEU MET GLU ILE THR PRO VAL TYR LEU GLN ASP GLU
SEQRES 14 B 190 ASN ASP GLN HIS VAL LEU THR GLY ALA VAL VAL MET LEU
SEQRES 15 B 190 ARG SER THR ILE ARG MET GLY ARG
SEQRES 1 C 190 MET ARG LEU GLU VAL PHE CYS GLU ASP ARG LEU GLY LEU
SEQRES 2 C 190 THR ARG GLU LEU LEU ASP LEU LEU VAL LEU ARG GLY ILE
SEQRES 3 C 190 ASP LEU ARG GLY ILE GLU ILE ASP PRO ILE GLY ARG ILE
SEQRES 4 C 190 TYR LEU ASN PHE ALA GLU LEU GLU PHE GLU SER PHE SER
SEQRES 5 C 190 SER LEU MET ALA GLU ILE ARG ARG ILE ALA GLY VAL THR
SEQRES 6 C 190 ASP VAL ARG THR VAL PRO TRP MET PRO SER GLU ARG GLU
SEQRES 7 C 190 HIS LEU ALA LEU SER ALA LEU LEU GLU ALA LEU PRO GLU
SEQRES 8 C 190 PRO VAL LEU SER VAL ASP MET LYS SER LYS VAL ASP MET
SEQRES 9 C 190 ALA ASN PRO ALA SER CYS GLN LEU PHE GLY GLN LYS LEU
SEQRES 10 C 190 ASP ARG LEU ARG ASN HIS THR ALA ALA GLN LEU ILE ASN
SEQRES 11 C 190 GLY PHE ASN PHE LEU ARG TRP LEU GLU SER GLU PRO GLN
SEQRES 12 C 190 ASP SER HIS ASN GLU HIS VAL VAL ILE ASN GLY GLN ASN
SEQRES 13 C 190 PHE LEU MET GLU ILE THR PRO VAL TYR LEU GLN ASP GLU
SEQRES 14 C 190 ASN ASP GLN HIS VAL LEU THR GLY ALA VAL VAL MET LEU
SEQRES 15 C 190 ARG SER THR ILE ARG MET GLY ARG
SEQRES 1 D 190 MET ARG LEU GLU VAL PHE CYS GLU ASP ARG LEU GLY LEU
SEQRES 2 D 190 THR ARG GLU LEU LEU ASP LEU LEU VAL LEU ARG GLY ILE
SEQRES 3 D 190 ASP LEU ARG GLY ILE GLU ILE ASP PRO ILE GLY ARG ILE
SEQRES 4 D 190 TYR LEU ASN PHE ALA GLU LEU GLU PHE GLU SER PHE SER
SEQRES 5 D 190 SER LEU MET ALA GLU ILE ARG ARG ILE ALA GLY VAL THR
SEQRES 6 D 190 ASP VAL ARG THR VAL PRO TRP MET PRO SER GLU ARG GLU
SEQRES 7 D 190 HIS LEU ALA LEU SER ALA LEU LEU GLU ALA LEU PRO GLU
SEQRES 8 D 190 PRO VAL LEU SER VAL ASP MET LYS SER LYS VAL ASP MET
SEQRES 9 D 190 ALA ASN PRO ALA SER CYS GLN LEU PHE GLY GLN LYS LEU
SEQRES 10 D 190 ASP ARG LEU ARG ASN HIS THR ALA ALA GLN LEU ILE ASN
SEQRES 11 D 190 GLY PHE ASN PHE LEU ARG TRP LEU GLU SER GLU PRO GLN
SEQRES 12 D 190 ASP SER HIS ASN GLU HIS VAL VAL ILE ASN GLY GLN ASN
SEQRES 13 D 190 PHE LEU MET GLU ILE THR PRO VAL TYR LEU GLN ASP GLU
SEQRES 14 D 190 ASN ASP GLN HIS VAL LEU THR GLY ALA VAL VAL MET LEU
SEQRES 15 D 190 ARG SER THR ILE ARG MET GLY ARG
HET AE3 A1191 9
HET PG4 A1192 12
HET SO4 B1191 5
HET PG4 C1189 12
HETNAM AE3 2-(2-ETHOXYETHOXY)ETHANOL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM SO4 SULFATE ION
FORMUL 5 AE3 C6 H14 O3
FORMUL 6 PG4 2(C8 H18 O5)
FORMUL 7 SO4 O4 S 2-
FORMUL 9 HOH *146(H2 O)
HELIX 1 1 GLY A 12 ARG A 24 1 13
HELIX 2 2 GLU A 47 ILE A 61 1 15
HELIX 3 3 GLU A 76 LEU A 89 1 14
HELIX 4 4 ASN A 106 GLY A 114 1 9
HELIX 5 5 LYS A 116 ARG A 121 1 6
HELIX 6 6 ALA A 125 LEU A 128 5 4
HELIX 7 7 ASN A 133 SER A 140 1 8
HELIX 8 8 ALA A 178 ILE A 186 1 9
HELIX 9 9 GLY B 12 ARG B 24 1 13
HELIX 10 10 GLU B 47 ARG B 60 1 14
HELIX 11 11 MET B 73 LEU B 89 1 17
HELIX 12 12 ASN B 106 GLY B 114 1 9
HELIX 13 13 LYS B 116 ARG B 121 1 6
HELIX 14 14 ALA B 125 LEU B 128 5 4
HELIX 15 15 ASN B 133 GLU B 139 1 7
HELIX 16 16 ALA B 178 MET B 188 1 11
HELIX 17 17 GLY C 12 ARG C 24 1 13
HELIX 18 18 GLU C 47 ARG C 59 1 13
HELIX 19 19 LEU C 80 LEU C 89 1 10
HELIX 20 20 ASN C 106 GLY C 114 1 9
HELIX 21 21 LYS C 116 ARG C 121 1 6
HELIX 22 22 ALA C 125 LEU C 128 5 4
HELIX 23 23 ASN C 133 SER C 140 1 8
HELIX 24 24 ALA C 178 ARG C 187 1 10
HELIX 25 25 GLY D 12 LEU D 23 1 12
HELIX 26 26 SER D 50 ARG D 60 1 11
HELIX 27 27 MET D 73 GLU D 87 1 15
HELIX 28 28 ASN D 106 GLY D 114 1 9
HELIX 29 29 LYS D 116 ARG D 121 1 6
HELIX 30 30 ASN D 133 GLU D 139 1 7
HELIX 31 31 ALA D 178 GLY D 189 1 12
SHEET 1 AA 8 VAL A 64 VAL A 70 0
SHEET 2 AA 8 ARG A 2 CYS A 7 -1 O ARG A 2 N VAL A 70
SHEET 3 AA 8 ARG A 38 PHE A 43 -1 O ILE A 39 N VAL A 5
SHEET 4 AA 8 LEU A 28 ASP A 34 -1 N ARG A 29 O ASN A 42
SHEET 5 AA 8 LEU B 28 ASP B 34 -1 O ARG B 29 N ILE A 33
SHEET 6 AA 8 ARG B 38 PHE B 43 -1 O ARG B 38 N ASP B 34
SHEET 7 AA 8 ARG B 2 CYS B 7 -1 O LEU B 3 N LEU B 41
SHEET 8 AA 8 VAL B 64 THR B 69 -1 N THR B 65 O PHE B 6
SHEET 1 AB 5 VAL A 102 ALA A 105 0
SHEET 2 AB 5 VAL A 93 VAL A 96 -1 O SER A 95 N ASP A 103
SHEET 3 AB 5 GLU A 169 THR A 176 -1 O ASN A 170 N VAL A 96
SHEET 4 AB 5 GLN A 155 VAL A 164 -1 O LEU A 158 N LEU A 175
SHEET 5 AB 5 HIS A 146 ILE A 152 -1 O HIS A 146 N ILE A 161
SHEET 1 BA 5 VAL B 102 ALA B 105 0
SHEET 2 BA 5 VAL B 93 ASP B 97 -1 O SER B 95 N ASP B 103
SHEET 3 BA 5 GLU B 169 THR B 176 -1 O ASN B 170 N VAL B 96
SHEET 4 BA 5 GLN B 155 VAL B 164 -1 O LEU B 158 N LEU B 175
SHEET 5 BA 5 HIS B 146 ILE B 152 -1 O HIS B 146 N ILE B 161
SHEET 1 CA 8 VAL C 64 THR C 69 0
SHEET 2 CA 8 ARG C 2 CYS C 7 -1 O GLU C 4 N ARG C 68
SHEET 3 CA 8 ARG C 38 PHE C 43 -1 O ILE C 39 N VAL C 5
SHEET 4 CA 8 LEU C 28 ASP C 34 -1 N ARG C 29 O ASN C 42
SHEET 5 CA 8 LEU D 28 ASP D 34 -1 O ARG D 29 N ILE C 33
SHEET 6 CA 8 ARG D 38 PHE D 43 -1 O ARG D 38 N ASP D 34
SHEET 7 CA 8 ARG D 2 PHE D 6 -1 O LEU D 3 N LEU D 41
SHEET 8 CA 8 ASP D 66 THR D 69 -1 O ASP D 66 N PHE D 6
SHEET 1 CB 5 VAL C 102 ALA C 105 0
SHEET 2 CB 5 VAL C 93 VAL C 96 -1 O SER C 95 N ASP C 103
SHEET 3 CB 5 GLU C 169 THR C 176 -1 O ASN C 170 N VAL C 96
SHEET 4 CB 5 GLN C 155 VAL C 164 -1 O LEU C 158 N LEU C 175
SHEET 5 CB 5 HIS C 146 ILE C 152 -1 O HIS C 146 N ILE C 161
SHEET 1 DA 5 VAL D 102 ALA D 105 0
SHEET 2 DA 5 VAL D 93 VAL D 96 -1 O SER D 95 N ASP D 103
SHEET 3 DA 5 GLU D 169 THR D 176 -1 O ASN D 170 N VAL D 96
SHEET 4 DA 5 GLN D 155 VAL D 164 -1 O LEU D 158 N LEU D 175
SHEET 5 DA 5 HIS D 146 ILE D 152 -1 O HIS D 146 N ILE D 161
SITE 1 AC1 8 CYS A 7 ARG A 10 GLY A 12 LEU A 13
SITE 2 AC1 8 THR A 14 ILE A 33 GLY A 37 ILE A 39
SITE 1 AC2 6 GLU A 91 LEU A 175 THR A 176 VAL A 180
SITE 2 AC2 6 ARG A 183 GLU B 160
SITE 1 AC3 4 GLY B 12 LEU B 13 THR B 14 ARG B 15
SITE 1 AC4 8 ARG C 10 GLY C 12 LEU C 13 THR C 14
SITE 2 AC4 8 ARG C 15 GLY C 37 VAL D 22 LEU D 23
CRYST1 134.456 72.009 96.814 90.00 98.46 90.00 C 1 2 1 16
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 0.007437 0.000000 0.001106 0.00000
SCALE2 0.000000 0.013887 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010443 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
