HEADER TRANSFERASE/TRANSCRIPTION REGULATOR 21-JUL-13 4LRY
TITLE CRYSTAL STRUCTURE OF THE E.COLI DHAR(N)-DHAK(T79L) COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PTS-DEPENDENT DIHYDROXYACETONE KINASE, DIHYDROXYACETONE-
COMPND 3 BINDING SUBUNIT DHAK;
COMPND 4 CHAIN: A, B;
COMPND 5 EC: 2.7.-.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PTS-DEPENDENT DIHYDROXYACETONE KINASE OPERON REGULATORY
COMPND 10 PROTEIN;
COMPND 11 CHAIN: C, D;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K-12;
SOURCE 5 GENE: B1200, DHAK, DHAR, JW5187, YCGT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-4T1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 13 ORGANISM_TAXID: 83333;
SOURCE 14 STRAIN: K-12;
SOURCE 15 GENE: B1201, DHAK, DHAR, JW5188, YCGU;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS COILED-COIL, HELIX ROTATION, GAF, PAS, TRANSCRIPTIONAL REGULATION
KEYWDS 2 COMPLEX, TRANSFERASE-TRANSCRIPTION REGULATOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.SHI,L.MCDONALD,M.CYGLER,I.EKIEL
REVDAT 4 28-FEB-24 4LRY 1 REMARK
REVDAT 3 15-NOV-17 4LRY 1 REMARK
REVDAT 2 26-MAR-14 4LRY 1 JRNL
REVDAT 1 29-JAN-14 4LRY 0
JRNL AUTH R.SHI,L.MCDONALD,M.CYGLER,I.EKIEL
JRNL TITL COILED-COIL HELIX ROTATION SELECTS REPRESSING OR ACTIVATING
JRNL TITL 2 STATE OF TRANSCRIPTIONAL REGULATOR DHAR.
JRNL REF STRUCTURE V. 22 478 2014
JRNL REFN ISSN 0969-2126
JRNL PMID 24440518
JRNL DOI 10.1016/J.STR.2013.11.012
REMARK 2
REMARK 2 RESOLUTION. 2.83 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 56422
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2860
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) : 2.83
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.91
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3528
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.3000
REMARK 3 BIN FREE R VALUE SET COUNT : 167
REMARK 3 BIN FREE R VALUE : 0.3360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9892
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 30
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.90000
REMARK 3 B22 (A**2) : -0.90000
REMARK 3 B33 (A**2) : 1.35000
REMARK 3 B12 (A**2) : -0.45000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.496
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.303
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.226
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.762
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10094 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13731 ; 1.937 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1298 ; 7.624 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 435 ;38.358 ;25.057
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1673 ;21.845 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 50 ;21.670 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1603 ; 0.128 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7591 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 6447 ; 0.616 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10344 ; 1.216 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3647 ; 2.099 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3386 ; 3.577 ; 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 : 6
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 356
REMARK 3 ORIGIN FOR THE GROUP (A): 16.8158 -65.6182 -7.0257
REMARK 3 T TENSOR
REMARK 3 T11: 0.2234 T22: 0.1237
REMARK 3 T33: 0.1872 T12: 0.0514
REMARK 3 T13: -0.1657 T23: -0.0742
REMARK 3 L TENSOR
REMARK 3 L11: 1.0165 L22: 1.1334
REMARK 3 L33: 2.6306 L12: 0.0249
REMARK 3 L13: 0.6644 L23: -0.2995
REMARK 3 S TENSOR
REMARK 3 S11: 0.0967 S12: 0.0921 S13: -0.0548
REMARK 3 S21: 0.0435 S22: 0.0558 S23: -0.1636
REMARK 3 S31: 0.3210 S32: 0.3659 S33: -0.1526
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 : B 1 B 356
REMARK 3 ORIGIN FOR THE GROUP (A): -10.0166 -68.8516 -25.0392
REMARK 3 T TENSOR
REMARK 3 T11: 0.2288 T22: 0.0912
REMARK 3 T33: 0.1768 T12: -0.0519
REMARK 3 T13: -0.1723 T23: 0.0412
REMARK 3 L TENSOR
REMARK 3 L11: 0.9800 L22: 0.9391
REMARK 3 L33: 2.7752 L12: -0.0182
REMARK 3 L13: 0.1976 L23: 0.2419
REMARK 3 S TENSOR
REMARK 3 S11: 0.0972 S12: -0.0891 S13: -0.0142
REMARK 3 S21: 0.0031 S22: 0.0644 S23: 0.1010
REMARK 3 S31: 0.3207 S32: -0.2861 S33: -0.1617
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 : C 13 C 203
REMARK 3 ORIGIN FOR THE GROUP (A): 18.7008 -53.6424 22.5625
REMARK 3 T TENSOR
REMARK 3 T11: 0.1190 T22: 0.0070
REMARK 3 T33: 0.1149 T12: 0.0073
REMARK 3 T13: -0.1054 T23: -0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 2.2274 L22: 0.9867
REMARK 3 L33: 1.3965 L12: -0.5354
REMARK 3 L13: 0.6393 L23: -0.0260
REMARK 3 S TENSOR
REMARK 3 S11: 0.0786 S12: -0.0369 S13: -0.0769
REMARK 3 S21: -0.0779 S22: 0.0639 S23: -0.0200
REMARK 3 S31: 0.2351 S32: -0.0113 S33: -0.1426
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 : C 204 C 306
REMARK 3 ORIGIN FOR THE GROUP (A): 60.2983 -84.8473 42.7763
REMARK 3 T TENSOR
REMARK 3 T11: 0.7066 T22: 0.2543
REMARK 3 T33: 0.2734 T12: 0.2531
REMARK 3 T13: -0.0213 T23: -0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 3.2499 L22: 3.1710
REMARK 3 L33: 5.9022 L12: -1.3656
REMARK 3 L13: 2.1672 L23: -0.2124
REMARK 3 S TENSOR
REMARK 3 S11: -0.1278 S12: -0.2455 S13: 0.3018
REMARK 3 S21: 0.4705 S22: 0.0468 S23: -0.4774
REMARK 3 S31: -0.2283 S32: 0.2434 S33: 0.0809
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 : D 13 D 203
REMARK 3 ORIGIN FOR THE GROUP (A): 37.6869 -40.3791 41.0674
REMARK 3 T TENSOR
REMARK 3 T11: 0.0525 T22: 0.0588
REMARK 3 T33: 0.0971 T12: 0.0416
REMARK 3 T13: -0.0638 T23: -0.0657
REMARK 3 L TENSOR
REMARK 3 L11: 1.1448 L22: 2.1887
REMARK 3 L33: 1.8186 L12: 0.0357
REMARK 3 L13: -0.0843 L23: 0.7009
REMARK 3 S TENSOR
REMARK 3 S11: 0.0347 S12: -0.0993 S13: 0.0013
REMARK 3 S21: 0.0905 S22: 0.0090 S23: 0.0344
REMARK 3 S31: 0.1243 S32: 0.0976 S33: -0.0436
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 : D 204 D 306
REMARK 3 ORIGIN FOR THE GROUP (A): 52.2893 -89.7329 18.8935
REMARK 3 T TENSOR
REMARK 3 T11: 0.6124 T22: 0.2886
REMARK 3 T33: 0.2024 T12: 0.2364
REMARK 3 T13: 0.0534 T23: 0.0176
REMARK 3 L TENSOR
REMARK 3 L11: 2.2713 L22: 6.2696
REMARK 3 L33: 5.8301 L12: -0.2825
REMARK 3 L13: 1.3593 L23: 2.2161
REMARK 3 S TENSOR
REMARK 3 S11: -0.0087 S12: 0.4904 S13: 0.0547
REMARK 3 S21: -0.4181 S22: -0.0835 S23: 0.1689
REMARK 3 S31: -0.0280 S32: -0.0550 S33: 0.0923
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4LRY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1000081010.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-AUG-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56455
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.830
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.55200
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% PEG 200, PH 6.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 26.58767
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 53.17533
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 39.88150
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 66.46917
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 13.29383
REMARK 290
REMARK 290 REMARK: NULL
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 MET C 1
REMARK 465 SER C 2
REMARK 465 GLY C 3
REMARK 465 ALA C 4
REMARK 465 PHE C 5
REMARK 465 ASN C 6
REMARK 465 ASN C 7
REMARK 465 ASP C 8
REMARK 465 GLY C 9
REMARK 465 ARG C 10
REMARK 465 GLY C 11
REMARK 465 ILE C 12
REMARK 465 GLU C 307
REMARK 465 GLN C 308
REMARK 465 MET C 309
REMARK 465 ARG C 310
REMARK 465 GLN C 311
REMARK 465 LEU C 312
REMARK 465 MET C 313
REMARK 465 THR C 314
REMARK 465 SER C 315
REMARK 465 GLN C 316
REMARK 465 LEU C 317
REMARK 465 GLY C 318
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 GLY D 3
REMARK 465 ALA D 4
REMARK 465 PHE D 5
REMARK 465 ASN D 6
REMARK 465 ASN D 7
REMARK 465 ASP D 8
REMARK 465 GLY D 9
REMARK 465 ARG D 10
REMARK 465 GLY D 11
REMARK 465 ILE D 12
REMARK 465 GLU D 307
REMARK 465 GLN D 308
REMARK 465 MET D 309
REMARK 465 ARG D 310
REMARK 465 GLN D 311
REMARK 465 LEU D 312
REMARK 465 MET D 313
REMARK 465 THR D 314
REMARK 465 SER D 315
REMARK 465 GLN D 316
REMARK 465 LEU D 317
REMARK 465 GLY D 318
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 MET A 1 SD CE
REMARK 470 MET B 1 SD CE
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 O ASN B 105 OG1 THR B 144 2.13
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 CYS C 73 CB CYS C 73 SG -0.103
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 LEU A 69 CA - CB - CG ANGL. DEV. = 15.5 DEGREES
REMARK 500 LEU A 69 CB - CG - CD1 ANGL. DEV. = -10.8 DEGREES
REMARK 500 LEU D 26 CA - CB - CG ANGL. DEV. = 16.5 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 LEU A 4 78.62 -68.52
REMARK 500 ASN A 6 -120.49 -97.44
REMARK 500 ASP A 31 72.54 50.55
REMARK 500 VAL A 46 112.96 -35.73
REMARK 500 MET A 68 -133.80 -146.90
REMARK 500 SER A 80 148.16 -39.49
REMARK 500 ASP A 94 108.83 -41.71
REMARK 500 ASN A 105 81.05 -59.79
REMARK 500 THR A 107 -74.15 -17.99
REMARK 500 ASP A 122 -7.29 -59.20
REMARK 500 ASP A 135 101.24 -54.67
REMARK 500 ASP A 140 127.92 60.20
REMARK 500 LEU A 142 -36.65 -36.42
REMARK 500 VAL A 150 -146.22 -117.15
REMARK 500 ARG A 166 -71.13 -28.32
REMARK 500 ASP A 168 141.31 -38.48
REMARK 500 ASP A 208 132.64 -38.83
REMARK 500 PRO A 221 153.71 -47.41
REMARK 500 ASP A 224 -165.61 -170.95
REMARK 500 LEU A 243 -71.13 -78.83
REMARK 500 ALA A 287 21.13 -150.78
REMARK 500 LEU A 323 -123.06 29.97
REMARK 500 ASP A 336 -167.55 -122.58
REMARK 500 ASN A 353 74.78 -151.39
REMARK 500 LYS B 2 49.09 -92.87
REMARK 500 ASN B 6 -110.40 -115.68
REMARK 500 GLU B 57 138.82 -36.68
REMARK 500 MET B 68 -143.37 -142.32
REMARK 500 GLU B 76 171.31 -59.85
REMARK 500 ASP B 94 115.80 -29.89
REMARK 500 ALA B 137 -71.83 -67.99
REMARK 500 ASP B 140 71.66 37.96
REMARK 500 SER B 141 -146.52 -73.62
REMARK 500 VAL B 150 -144.00 -126.73
REMARK 500 ASP B 224 -169.37 -164.88
REMARK 500 SER B 247 123.34 -38.72
REMARK 500 TYR B 248 105.97 -163.09
REMARK 500 ALA B 287 23.34 -147.75
REMARK 500 LEU B 323 -124.27 36.56
REMARK 500 ASP B 324 39.41 -99.37
REMARK 500 ASP B 336 -167.75 -126.88
REMARK 500 PRO B 346 150.43 -43.92
REMARK 500 ASN B 353 61.65 -152.53
REMARK 500 MET C 27 147.57 -175.21
REMARK 500 VAL C 34 113.79 -34.26
REMARK 500 ARG C 71 150.89 177.43
REMARK 500 THR C 115 107.83 -32.89
REMARK 500 ALA C 127 137.58 -38.40
REMARK 500 ALA C 132 -134.03 65.31
REMARK 500 SER C 153 -49.12 -29.04
REMARK 500
REMARK 500 THIS ENTRY HAS 74 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 MET B 1 LYS B 2 -140.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LRX RELATED DB: PDB
REMARK 900 DHAR(N)-DHAK COMPLEX
REMARK 900 RELATED ID: 4LRZ RELATED DB: PDB
DBREF 4LRY A 1 356 UNP P76015 DHAK_ECOLI 1 356
DBREF 4LRY B 1 356 UNP P76015 DHAK_ECOLI 1 356
DBREF 4LRY C 1 318 UNP P76016 DHAR_ECOLI 1 318
DBREF 4LRY D 1 318 UNP P76016 DHAR_ECOLI 1 318
SEQADV 4LRY LEU A 79 UNP P76015 THR 79 ENGINEERED MUTATION
SEQADV 4LRY LEU B 79 UNP P76015 THR 79 ENGINEERED MUTATION
SEQRES 1 A 356 MET LYS LYS LEU ILE ASN ASP VAL GLN ASP VAL LEU ASP
SEQRES 2 A 356 GLU GLN LEU ALA GLY LEU ALA LYS ALA HIS PRO SER LEU
SEQRES 3 A 356 THR LEU HIS GLN ASP PRO VAL TYR VAL THR ARG ALA ASP
SEQRES 4 A 356 ALA PRO VAL ALA GLY LYS VAL ALA LEU LEU SER GLY GLY
SEQRES 5 A 356 GLY SER GLY HIS GLU PRO MET HIS CYS GLY TYR ILE GLY
SEQRES 6 A 356 GLN GLY MET LEU SER GLY ALA CYS PRO GLY GLU ILE PHE
SEQRES 7 A 356 LEU SER PRO THR PRO ASP LYS ILE PHE GLU CYS ALA MET
SEQRES 8 A 356 GLN VAL ASP GLY GLY GLU GLY VAL LEU LEU ILE ILE LYS
SEQRES 9 A 356 ASN TYR THR GLY ASP ILE LEU ASN PHE GLU THR ALA THR
SEQRES 10 A 356 GLU LEU LEU HIS ASP SER GLY VAL LYS VAL THR THR VAL
SEQRES 11 A 356 VAL ILE ASP ASP ASP VAL ALA VAL LYS ASP SER LEU TYR
SEQRES 12 A 356 THR ALA GLY ARG ARG GLY VAL ALA ASN THR VAL LEU ILE
SEQRES 13 A 356 GLU LYS LEU VAL GLY ALA ALA ALA GLU ARG GLY ASP SER
SEQRES 14 A 356 LEU ASP ALA CYS ALA GLU LEU GLY ARG LYS LEU ASN ASN
SEQRES 15 A 356 GLN GLY HIS SER ILE GLY ILE ALA LEU GLY ALA CYS THR
SEQRES 16 A 356 VAL PRO ALA ALA GLY LYS PRO SER PHE THR LEU ALA ASP
SEQRES 17 A 356 ASN GLU MET GLU PHE GLY VAL GLY ILE HIS GLY GLU PRO
SEQRES 18 A 356 GLY ILE ASP ARG ARG PRO PHE SER SER LEU ASP GLN THR
SEQRES 19 A 356 VAL ASP GLU MET PHE ASP THR LEU LEU VAL ASN GLY SER
SEQRES 20 A 356 TYR HIS ARG THR LEU ARG PHE TRP ASP TYR GLN GLN GLY
SEQRES 21 A 356 SER TRP GLN GLU GLU GLN GLN THR LYS GLN PRO LEU GLN
SEQRES 22 A 356 SER GLY ASP ARG VAL ILE ALA LEU VAL ASN ASN LEU GLY
SEQRES 23 A 356 ALA THR PRO LEU SER GLU LEU TYR GLY VAL TYR ASN ARG
SEQRES 24 A 356 LEU THR THR ARG CYS GLN GLN ALA GLY LEU THR ILE GLU
SEQRES 25 A 356 ARG ASN LEU ILE GLY ALA TYR CYS THR SER LEU ASP MET
SEQRES 26 A 356 THR GLY PHE SER ILE THR LEU LEU LYS VAL ASP ASP GLU
SEQRES 27 A 356 THR LEU ALA LEU TRP ASP ALA PRO VAL HIS THR PRO ALA
SEQRES 28 A 356 LEU ASN TRP GLY LYS
SEQRES 1 B 356 MET LYS LYS LEU ILE ASN ASP VAL GLN ASP VAL LEU ASP
SEQRES 2 B 356 GLU GLN LEU ALA GLY LEU ALA LYS ALA HIS PRO SER LEU
SEQRES 3 B 356 THR LEU HIS GLN ASP PRO VAL TYR VAL THR ARG ALA ASP
SEQRES 4 B 356 ALA PRO VAL ALA GLY LYS VAL ALA LEU LEU SER GLY GLY
SEQRES 5 B 356 GLY SER GLY HIS GLU PRO MET HIS CYS GLY TYR ILE GLY
SEQRES 6 B 356 GLN GLY MET LEU SER GLY ALA CYS PRO GLY GLU ILE PHE
SEQRES 7 B 356 LEU SER PRO THR PRO ASP LYS ILE PHE GLU CYS ALA MET
SEQRES 8 B 356 GLN VAL ASP GLY GLY GLU GLY VAL LEU LEU ILE ILE LYS
SEQRES 9 B 356 ASN TYR THR GLY ASP ILE LEU ASN PHE GLU THR ALA THR
SEQRES 10 B 356 GLU LEU LEU HIS ASP SER GLY VAL LYS VAL THR THR VAL
SEQRES 11 B 356 VAL ILE ASP ASP ASP VAL ALA VAL LYS ASP SER LEU TYR
SEQRES 12 B 356 THR ALA GLY ARG ARG GLY VAL ALA ASN THR VAL LEU ILE
SEQRES 13 B 356 GLU LYS LEU VAL GLY ALA ALA ALA GLU ARG GLY ASP SER
SEQRES 14 B 356 LEU ASP ALA CYS ALA GLU LEU GLY ARG LYS LEU ASN ASN
SEQRES 15 B 356 GLN GLY HIS SER ILE GLY ILE ALA LEU GLY ALA CYS THR
SEQRES 16 B 356 VAL PRO ALA ALA GLY LYS PRO SER PHE THR LEU ALA ASP
SEQRES 17 B 356 ASN GLU MET GLU PHE GLY VAL GLY ILE HIS GLY GLU PRO
SEQRES 18 B 356 GLY ILE ASP ARG ARG PRO PHE SER SER LEU ASP GLN THR
SEQRES 19 B 356 VAL ASP GLU MET PHE ASP THR LEU LEU VAL ASN GLY SER
SEQRES 20 B 356 TYR HIS ARG THR LEU ARG PHE TRP ASP TYR GLN GLN GLY
SEQRES 21 B 356 SER TRP GLN GLU GLU GLN GLN THR LYS GLN PRO LEU GLN
SEQRES 22 B 356 SER GLY ASP ARG VAL ILE ALA LEU VAL ASN ASN LEU GLY
SEQRES 23 B 356 ALA THR PRO LEU SER GLU LEU TYR GLY VAL TYR ASN ARG
SEQRES 24 B 356 LEU THR THR ARG CYS GLN GLN ALA GLY LEU THR ILE GLU
SEQRES 25 B 356 ARG ASN LEU ILE GLY ALA TYR CYS THR SER LEU ASP MET
SEQRES 26 B 356 THR GLY PHE SER ILE THR LEU LEU LYS VAL ASP ASP GLU
SEQRES 27 B 356 THR LEU ALA LEU TRP ASP ALA PRO VAL HIS THR PRO ALA
SEQRES 28 B 356 LEU ASN TRP GLY LYS
SEQRES 1 C 318 MET SER GLY ALA PHE ASN ASN ASP GLY ARG GLY ILE SER
SEQRES 2 C 318 PRO LEU ILE ALA THR SER TRP GLU ARG CYS ASN LYS LEU
SEQRES 3 C 318 MET LYS ARG GLU THR TRP ASN VAL PRO HIS GLN ALA GLN
SEQRES 4 C 318 GLY VAL THR PHE ALA SER ILE TYR ARG ARG LYS LYS ALA
SEQRES 5 C 318 MET LEU THR LEU GLY GLN ALA ALA LEU GLU ASP ALA TRP
SEQRES 6 C 318 GLU TYR MET ALA PRO ARG GLU CYS ALA LEU PHE ILE LEU
SEQRES 7 C 318 ASP GLU THR ALA CYS ILE LEU SER ARG ASN GLY ASP PRO
SEQRES 8 C 318 GLN THR LEU GLN GLN LEU SER ALA LEU GLY PHE ASN ASP
SEQRES 9 C 318 GLY THR TYR CYS ALA GLU GLY ILE ILE GLY THR CYS ALA
SEQRES 10 C 318 LEU SER LEU ALA ALA ILE SER GLY GLN ALA VAL LYS THR
SEQRES 11 C 318 MET ALA ASP GLN HIS PHE LYS GLN VAL LEU TRP ASN TRP
SEQRES 12 C 318 ALA PHE CYS ALA THR PRO LEU PHE ASP SER LYS GLY ARG
SEQRES 13 C 318 LEU THR GLY THR ILE ALA LEU ALA CYS PRO VAL GLU GLN
SEQRES 14 C 318 THR THR ALA ALA ASP LEU PRO LEU THR LEU ALA ILE ALA
SEQRES 15 C 318 ARG GLU VAL GLY ASN LEU LEU LEU THR ASP SER LEU LEU
SEQRES 16 C 318 ALA GLU THR ASN ARG HIS LEU ASN GLN LEU ASN ALA LEU
SEQRES 17 C 318 LEU GLU SER MET ASP ASP GLY VAL ILE SER TRP ASP GLU
SEQRES 18 C 318 GLN GLY ASN LEU GLN PHE ILE ASN ALA GLN ALA ALA ARG
SEQRES 19 C 318 VAL LEU ARG LEU ASP ALA THR ALA SER GLN GLY ARG ALA
SEQRES 20 C 318 ILE THR GLU LEU LEU THR LEU PRO ALA VAL LEU GLN GLN
SEQRES 21 C 318 ALA ILE LYS GLN ALA HIS PRO LEU LYS HIS VAL GLU ALA
SEQRES 22 C 318 THR PHE GLU SER GLN HIS GLN PHE ILE ASP ALA VAL ILE
SEQRES 23 C 318 THR LEU LYS PRO ILE ILE GLU THR GLN GLY THR SER PHE
SEQRES 24 C 318 ILE LEU LEU LEU HIS PRO VAL GLU GLN MET ARG GLN LEU
SEQRES 25 C 318 MET THR SER GLN LEU GLY
SEQRES 1 D 318 MET SER GLY ALA PHE ASN ASN ASP GLY ARG GLY ILE SER
SEQRES 2 D 318 PRO LEU ILE ALA THR SER TRP GLU ARG CYS ASN LYS LEU
SEQRES 3 D 318 MET LYS ARG GLU THR TRP ASN VAL PRO HIS GLN ALA GLN
SEQRES 4 D 318 GLY VAL THR PHE ALA SER ILE TYR ARG ARG LYS LYS ALA
SEQRES 5 D 318 MET LEU THR LEU GLY GLN ALA ALA LEU GLU ASP ALA TRP
SEQRES 6 D 318 GLU TYR MET ALA PRO ARG GLU CYS ALA LEU PHE ILE LEU
SEQRES 7 D 318 ASP GLU THR ALA CYS ILE LEU SER ARG ASN GLY ASP PRO
SEQRES 8 D 318 GLN THR LEU GLN GLN LEU SER ALA LEU GLY PHE ASN ASP
SEQRES 9 D 318 GLY THR TYR CYS ALA GLU GLY ILE ILE GLY THR CYS ALA
SEQRES 10 D 318 LEU SER LEU ALA ALA ILE SER GLY GLN ALA VAL LYS THR
SEQRES 11 D 318 MET ALA ASP GLN HIS PHE LYS GLN VAL LEU TRP ASN TRP
SEQRES 12 D 318 ALA PHE CYS ALA THR PRO LEU PHE ASP SER LYS GLY ARG
SEQRES 13 D 318 LEU THR GLY THR ILE ALA LEU ALA CYS PRO VAL GLU GLN
SEQRES 14 D 318 THR THR ALA ALA ASP LEU PRO LEU THR LEU ALA ILE ALA
SEQRES 15 D 318 ARG GLU VAL GLY ASN LEU LEU LEU THR ASP SER LEU LEU
SEQRES 16 D 318 ALA GLU THR ASN ARG HIS LEU ASN GLN LEU ASN ALA LEU
SEQRES 17 D 318 LEU GLU SER MET ASP ASP GLY VAL ILE SER TRP ASP GLU
SEQRES 18 D 318 GLN GLY ASN LEU GLN PHE ILE ASN ALA GLN ALA ALA ARG
SEQRES 19 D 318 VAL LEU ARG LEU ASP ALA THR ALA SER GLN GLY ARG ALA
SEQRES 20 D 318 ILE THR GLU LEU LEU THR LEU PRO ALA VAL LEU GLN GLN
SEQRES 21 D 318 ALA ILE LYS GLN ALA HIS PRO LEU LYS HIS VAL GLU ALA
SEQRES 22 D 318 THR PHE GLU SER GLN HIS GLN PHE ILE ASP ALA VAL ILE
SEQRES 23 D 318 THR LEU LYS PRO ILE ILE GLU THR GLN GLY THR SER PHE
SEQRES 24 D 318 ILE LEU LEU LEU HIS PRO VAL GLU GLN MET ARG GLN LEU
SEQRES 25 D 318 MET THR SER GLN LEU GLY
HET GOL A 401 6
HET GOL B 401 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 7 HOH *30(H2 O)
HELIX 1 1 ASP A 10 HIS A 23 1 14
HELIX 2 2 HIS A 60 ILE A 64 5 5
HELIX 3 3 THR A 82 ASP A 94 1 13
HELIX 4 4 TYR A 106 ASP A 122 1 17
HELIX 5 5 ALA A 151 GLY A 167 1 17
HELIX 6 6 SER A 169 ASN A 182 1 14
HELIX 7 7 SER A 230 ASN A 245 1 16
HELIX 8 8 PRO A 289 GLY A 308 1 20
HELIX 9 9 ASP A 336 ALA A 345 1 10
HELIX 10 10 ASP B 10 HIS B 23 1 14
HELIX 11 11 HIS B 60 ILE B 64 5 5
HELIX 12 12 THR B 82 ASP B 94 1 13
HELIX 13 13 TYR B 106 ASP B 122 1 17
HELIX 14 14 ALA B 151 GLY B 167 1 17
HELIX 15 15 SER B 169 ASN B 182 1 14
HELIX 16 16 VAL B 196 GLY B 200 5 5
HELIX 17 17 SER B 230 ASN B 245 1 16
HELIX 18 18 PRO B 289 ALA B 307 1 19
HELIX 19 19 ASP B 336 ASP B 344 1 9
HELIX 20 20 PRO C 14 MET C 27 1 14
HELIX 21 21 GLN C 39 ARG C 49 1 11
HELIX 22 22 LYS C 50 TYR C 67 1 18
HELIX 23 23 ASP C 90 ALA C 99 1 10
HELIX 24 24 ALA C 109 GLY C 114 1 6
HELIX 25 25 CYS C 116 GLY C 125 1 10
HELIX 26 26 ASP C 133 HIS C 135 5 3
HELIX 27 27 LYS C 137 TRP C 141 5 5
HELIX 28 28 GLU C 168 THR C 170 5 3
HELIX 29 29 ALA C 173 GLU C 210 1 38
HELIX 30 30 ASN C 229 ARG C 237 1 9
HELIX 31 31 ASP C 239 GLN C 244 1 6
HELIX 32 32 ALA C 247 LEU C 252 1 6
HELIX 33 33 PRO C 255 ALA C 265 1 11
HELIX 34 34 PRO D 14 LYS D 25 1 12
HELIX 35 35 GLN D 39 LYS D 50 1 12
HELIX 36 36 LYS D 50 TYR D 67 1 18
HELIX 37 37 ASP D 90 LEU D 100 1 11
HELIX 38 38 ALA D 109 GLY D 114 1 6
HELIX 39 39 CYS D 116 GLY D 125 1 10
HELIX 40 40 ASP D 133 HIS D 135 5 3
HELIX 41 41 LYS D 137 TRP D 141 5 5
HELIX 42 42 GLU D 168 THR D 170 5 3
HELIX 43 43 ALA D 173 SER D 211 1 39
HELIX 44 44 ASN D 229 LEU D 236 1 8
HELIX 45 45 ASP D 239 GLN D 244 1 6
HELIX 46 46 ALA D 247 LEU D 252 1 6
HELIX 47 47 PRO D 255 ALA D 265 1 11
SHEET 1 A 6 LEU A 26 HIS A 29 0
SHEET 2 A 6 TYR A 34 ARG A 37 -1 O THR A 36 N THR A 27
SHEET 3 A 6 GLY A 71 ILE A 77 -1 O ALA A 72 N VAL A 35
SHEET 4 A 6 ALA A 47 SER A 54 1 N GLY A 52 O CYS A 73
SHEET 5 A 6 VAL A 99 LYS A 104 1 O LEU A 100 N ALA A 47
SHEET 6 A 6 VAL A 127 ILE A 132 1 O VAL A 130 N LEU A 101
SHEET 1 B 6 ASP A 224 PRO A 227 0
SHEET 2 B 6 GLU A 210 VAL A 215 -1 N MET A 211 O ARG A 226
SHEET 3 B 6 GLY A 184 GLY A 192 -1 N ALA A 190 O GLU A 212
SHEET 4 B 6 THR A 326 VAL A 335 -1 O THR A 326 N LEU A 191
SHEET 5 B 6 ARG A 277 ASN A 284 -1 N ASN A 283 O SER A 329
SHEET 6 B 6 THR A 310 GLY A 317 1 O GLU A 312 N VAL A 278
SHEET 1 C 2 TYR A 248 ASP A 256 0
SHEET 2 C 2 SER A 261 LYS A 269 -1 O GLU A 265 N LEU A 252
SHEET 1 D 6 LEU B 26 HIS B 29 0
SHEET 2 D 6 TYR B 34 ARG B 37 -1 O TYR B 34 N HIS B 29
SHEET 3 D 6 GLY B 71 ILE B 77 -1 O ALA B 72 N VAL B 35
SHEET 4 D 6 ALA B 47 SER B 54 1 N GLY B 52 O GLY B 75
SHEET 5 D 6 VAL B 99 LYS B 104 1 O LEU B 100 N LEU B 49
SHEET 6 D 6 VAL B 127 ILE B 132 1 O VAL B 130 N ILE B 103
SHEET 1 E 6 ASP B 224 PRO B 227 0
SHEET 2 E 6 GLU B 210 PHE B 213 -1 N MET B 211 O ARG B 226
SHEET 3 E 6 GLY B 184 GLY B 192 -1 N ALA B 190 O GLU B 212
SHEET 4 E 6 THR B 326 LYS B 334 -1 O THR B 326 N LEU B 191
SHEET 5 E 6 ARG B 277 ASN B 284 -1 N ASN B 283 O SER B 329
SHEET 6 E 6 THR B 310 GLY B 317 1 O GLU B 312 N VAL B 278
SHEET 1 F 2 TYR B 248 ASP B 256 0
SHEET 2 F 2 SER B 261 LYS B 269 -1 O GLN B 267 N ARG B 250
SHEET 1 G 5 ILE C 84 GLY C 89 0
SHEET 2 G 5 ALA C 74 ASP C 79 -1 N LEU C 75 O ASN C 88
SHEET 3 G 5 LEU C 157 PRO C 166 -1 O THR C 160 N LEU C 78
SHEET 4 G 5 TRP C 143 PHE C 151 -1 N LEU C 150 O THR C 158
SHEET 5 G 5 VAL C 128 MET C 131 -1 N THR C 130 O PHE C 145
SHEET 1 H 5 LEU C 225 ILE C 228 0
SHEET 2 H 5 GLY C 215 TRP C 219 -1 N SER C 218 O PHE C 227
SHEET 3 H 5 THR C 297 HIS C 304 -1 O LEU C 303 N GLY C 215
SHEET 4 H 5 GLN C 280 ILE C 292 -1 N THR C 287 O LEU C 302
SHEET 5 H 5 LEU C 268 SER C 277 -1 N ALA C 273 O ALA C 284
SHEET 1 I 5 ILE D 84 GLY D 89 0
SHEET 2 I 5 ALA D 74 LEU D 78 -1 N ILE D 77 O LEU D 85
SHEET 3 I 5 LEU D 157 PRO D 166 -1 O THR D 160 N LEU D 78
SHEET 4 I 5 TRP D 143 PHE D 151 -1 N CYS D 146 O LEU D 163
SHEET 5 I 5 VAL D 128 MET D 131 -1 N THR D 130 O PHE D 145
SHEET 1 J 5 LEU D 225 ILE D 228 0
SHEET 2 J 5 GLY D 215 TRP D 219 -1 N SER D 218 O GLN D 226
SHEET 3 J 5 GLY D 296 HIS D 304 -1 O LEU D 301 N ILE D 217
SHEET 4 J 5 GLN D 280 GLU D 293 -1 N VAL D 285 O HIS D 304
SHEET 5 J 5 LEU D 268 SER D 277 -1 N VAL D 271 O ILE D 286
CISPEP 1 ASP A 31 PRO A 32 0 -6.18
CISPEP 2 ALA A 40 PRO A 41 0 -2.70
CISPEP 3 GLU A 57 PRO A 58 0 15.86
CISPEP 4 MET A 59 HIS A 60 0 13.76
CISPEP 5 ASP B 31 PRO B 32 0 -0.25
CISPEP 6 ALA B 40 PRO B 41 0 -4.80
CISPEP 7 GLU B 57 PRO B 58 0 3.89
CISPEP 8 MET B 59 HIS B 60 0 -2.74
CISPEP 9 ALA C 69 PRO C 70 0 4.53
CISPEP 10 ALA D 69 PRO D 70 0 -9.56
SITE 1 AC1 7 GLY A 52 GLY A 53 HIS A 56 SER A 80
SITE 2 AC1 7 LYS A 104 ASP A 109 HIS A 218
SITE 1 AC2 8 GLY B 52 GLY B 53 HIS B 56 SER B 80
SITE 2 AC2 8 LYS B 104 TYR B 106 ASP B 109 HIS B 218
CRYST1 231.397 231.397 79.763 90.00 90.00 120.00 P 61 12
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 0.004322 0.002495 0.000000 0.00000
SCALE2 0.000000 0.004990 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012537 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
