HEADER LYASE, BIOSYNTHETIC PROTEIN 22-MAR-11 3R74
TITLE CRYSTAL STRUCTURE OF 2-AMINO-2-DESOXYISOCHORISMATE SYNTHASE (ADIC)
TITLE 2 SYNTHASE PHZE FROM BURKHOLDERIA LATA 383
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTHRANILATE/PARA-AMINOBENZOATE SYNTHASES COMPONENT I;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 4.1.3.27;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA SP.;
SOURCE 3 ORGANISM_TAXID: 269483;
SOURCE 4 STRAIN: 383;
SOURCE 5 GENE: BCEP18194_B1570;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2 PLYS S;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET19MODTEV
KEYWDS AMMONIA CHANNEL, CHORISMATE, TYPE 1 GLUTAMINE AMIDOTRANSFERASE,
KEYWDS 2 PHENAZINE BIOSYNTHESIS, LYASE, SYNTHASE, BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.A.LI,D.V.MAVRODI,L.S.THOMASHOW,M.ROESSLE,W.BLANKENFELDT
REVDAT 4 21-FEB-24 3R74 1 SEQADV
REVDAT 3 01-JUN-11 3R74 1 JRNL
REVDAT 2 13-APR-11 3R74 1 JRNL
REVDAT 1 30-MAR-11 3R74 0
JRNL AUTH Q.A.LI,D.V.MAVRODI,L.S.THOMASHOW,M.ROESSLE,W.BLANKENFELDT
JRNL TITL LIGAND BINDING INDUCES AN AMMONIA CHANNEL IN
JRNL TITL 2 2-AMINO-2-DESOXYISOCHORISMATE (ADIC) SYNTHASE PHZE.
JRNL REF J.BIOL.CHEM. V. 286 18213 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21454481
JRNL DOI 10.1074/JBC.M110.183418
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0077
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 42357
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2120
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2881
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.2550
REMARK 3 BIN FREE R VALUE SET COUNT : 157
REMARK 3 BIN FREE R VALUE : 0.3240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9088
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 80
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 60.36
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 76.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.885
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.326
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.237
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.439
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9269 ; 0.017 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 6056 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12629 ; 1.762 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14677 ; 1.305 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1228 ; 7.744 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 393 ;36.482 ;22.672
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1347 ;20.864 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 85 ;20.981 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1454 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10675 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1940 ; 0.004 ; 0.020
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 6 A 395
REMARK 3 RESIDUE RANGE : B 401 B 427
REMARK 3 ORIGIN FOR THE GROUP (A): 110.6252 20.2429 101.1909
REMARK 3 T TENSOR
REMARK 3 T11: 0.2944 T22: 0.2218
REMARK 3 T33: 0.0731 T12: -0.0882
REMARK 3 T13: 0.0532 T23: 0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 1.1493 L22: 1.2410
REMARK 3 L33: 1.7614 L12: -0.3947
REMARK 3 L13: 0.3555 L23: -0.6524
REMARK 3 S TENSOR
REMARK 3 S11: -0.0333 S12: 0.1182 S13: 0.1266
REMARK 3 S21: -0.0016 S22: -0.0270 S23: -0.2568
REMARK 3 S31: -0.1157 S32: 0.2657 S33: 0.0603
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 440 A 633
REMARK 3 ORIGIN FOR THE GROUP (A): 168.0346 46.5934 72.6451
REMARK 3 T TENSOR
REMARK 3 T11: 0.3394 T22: 0.5988
REMARK 3 T33: 0.1410 T12: 0.0449
REMARK 3 T13: -0.1666 T23: 0.0699
REMARK 3 L TENSOR
REMARK 3 L11: 3.5301 L22: 2.3105
REMARK 3 L33: 9.0308 L12: -0.6246
REMARK 3 L13: 2.5688 L23: -1.5137
REMARK 3 S TENSOR
REMARK 3 S11: 0.0455 S12: -0.0329 S13: 0.2285
REMARK 3 S21: -0.1882 S22: -0.1065 S23: -0.1624
REMARK 3 S31: 0.2097 S32: 0.6971 S33: 0.0610
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 7 B 395
REMARK 3 RESIDUE RANGE : A 401 A 427
REMARK 3 ORIGIN FOR THE GROUP (A): 148.1339 47.4941 103.3023
REMARK 3 T TENSOR
REMARK 3 T11: 0.4478 T22: 1.5666
REMARK 3 T33: 0.4087 T12: 0.0865
REMARK 3 T13: -0.1345 T23: 0.1393
REMARK 3 L TENSOR
REMARK 3 L11: 2.1081 L22: 0.5681
REMARK 3 L33: 2.9210 L12: -0.5335
REMARK 3 L13: -0.3159 L23: 0.4442
REMARK 3 S TENSOR
REMARK 3 S11: -0.2503 S12: -0.7885 S13: 0.2489
REMARK 3 S21: 0.1717 S22: 0.1468 S23: 0.2523
REMARK 3 S31: -0.1949 S32: -0.8197 S33: 0.1036
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 430 B 635
REMARK 3 ORIGIN FOR THE GROUP (A): 85.9496 22.9692 72.7995
REMARK 3 T TENSOR
REMARK 3 T11: 0.3876 T22: 0.3623
REMARK 3 T33: 0.0558 T12: -0.1123
REMARK 3 T13: -0.0047 T23: 0.0905
REMARK 3 L TENSOR
REMARK 3 L11: 2.2275 L22: 2.3812
REMARK 3 L33: 3.2203 L12: 0.2750
REMARK 3 L13: -0.1011 L23: 0.3541
REMARK 3 S TENSOR
REMARK 3 S11: -0.1618 S12: 0.3126 S13: -0.0071
REMARK 3 S21: -0.2821 S22: 0.1389 S23: 0.2390
REMARK 3 S31: -0.0234 S32: -0.4372 S33: 0.0230
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 3R74 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064572.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-NOV-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0, 0.97895, 0.97957, 0.97793
REMARK 200 MONOCHROMATOR : SI(111) MONOCHROMATOR
REMARK 200 OPTICS : SI(111)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42476
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 19.924
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.47000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.680
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PROPANE, 0.2 M KSCN,
REMARK 280 22% (W/V) PEG 3350, 1 MM MG-CHLORIDE, 20 MM CHORISMATE, PH 7.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+2/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-Z+1/3
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 144.29333
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 72.14667
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 0.00000
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 144.29333
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 72.14667
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 144.29333
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 72.14667
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 144.29333
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 72.14667
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 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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 657 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 687 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 664 LIES ON A SPECIAL POSITION.
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 -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 PRO A 5
REMARK 465 GLY A 429
REMARK 465 GLY A 430
REMARK 465 ARG A 431
REMARK 465 GLN A 432
REMARK 465 GLY A 433
REMARK 465 GLU A 434
REMARK 465 MET A 435
REMARK 465 ALA A 436
REMARK 465 ASP A 437
REMARK 465 GLU A 438
REMARK 465 LEU A 439
REMARK 465 ARG A 634
REMARK 465 GLU A 635
REMARK 465 LYS A 636
REMARK 465 ARG A 637
REMARK 465 MET A 638
REMARK 465 THR A 639
REMARK 465 ALA A 640
REMARK 465 LEU A 641
REMARK 465 THR A 642
REMARK 465 ALA A 643
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 ALA B 3
REMARK 465 ALA B 4
REMARK 465 PRO B 5
REMARK 465 ASN B 6
REMARK 465 GLY B 29
REMARK 465 SER B 30
REMARK 465 ALA B 31
REMARK 465 GLY B 32
REMARK 465 GLU B 33
REMARK 465 ARG B 34
REMARK 465 GLY B 433
REMARK 465 GLU B 434
REMARK 465 MET B 435
REMARK 465 ALA B 436
REMARK 465 ASP B 437
REMARK 465 GLU B 438
REMARK 465 LEU B 439
REMARK 465 LYS B 636
REMARK 465 ARG B 637
REMARK 465 MET B 638
REMARK 465 THR B 639
REMARK 465 ALA B 640
REMARK 465 LEU B 641
REMARK 465 THR B 642
REMARK 465 ALA B 643
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 THR A 28 OG1 CG2
REMARK 470 SER A 30 OG
REMARK 470 GLU A 33 CG CD OE1 OE2
REMARK 470 ARG A 34 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 83 CG CD CE NZ
REMARK 470 SER A 225 OG
REMARK 470 ARG A 239 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 240 CG CD CE NZ
REMARK 470 GLU A 398 CG CD OE1 OE2
REMARK 470 LEU A 403 CG CD1 CD2
REMARK 470 GLN A 405 CG CD OE1 NE2
REMARK 470 HIS A 406 CG ND1 CD2 CE1 NE2
REMARK 470 SER A 408 OG
REMARK 470 VAL A 409 CG1 CG2
REMARK 470 GLN A 410 CG CD OE1 NE2
REMARK 470 ARG A 414 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 415 CG CD OE1 OE2
REMARK 470 GLU A 418 CG CD OE1 OE2
REMARK 470 ARG A 426 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 441 CG CD OE1 OE2
REMARK 470 ARG A 446 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 481 CG OD1 OD2
REMARK 470 GLN A 559 CG CD OE1 NE2
REMARK 470 ARG B 7 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 9 CG CD1 CD2
REMARK 470 PHE B 10 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP B 11 CG OD1 OD2
REMARK 470 ARG B 12 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 13 CG1 CG2
REMARK 470 GLN B 17 CG CD OE1 NE2
REMARK 470 MET B 36 CG SD CE
REMARK 470 VAL B 44 CG1 CG2
REMARK 470 LYS B 83 CG CD CE NZ
REMARK 470 HIS B 85 CG ND1 CD2 CE1 NE2
REMARK 470 GLN B 105 CG CD OE1 NE2
REMARK 470 LEU B 106 CG CD1 CD2
REMARK 470 ILE B 111 CG1 CG2 CD1
REMARK 470 ASP B 115 CG OD1 OD2
REMARK 470 THR B 116 OG1 CG2
REMARK 470 LEU B 118 CG CD1 CD2
REMARK 470 GLU B 120 CG CD OE1 OE2
REMARK 470 ARG B 121 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 125 CG1 CG2 CD1
REMARK 470 GLU B 128 CG CD OE1 OE2
REMARK 470 TYR B 130 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 132 CG CD OE1 OE2
REMARK 470 GLU B 135 CG CD OE1 OE2
REMARK 470 ARG B 136 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 154 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 159 CG OD1 OD2
REMARK 470 LEU B 160 CG CD1 CD2
REMARK 470 ASP B 161 CG OD1 OD2
REMARK 470 ASP B 162 CG OD1 OD2
REMARK 470 TYR B 163 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 173 CG CD CE NZ
REMARK 470 ARG B 174 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 177 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 179 CG CD OE1 OE2
REMARK 470 GLU B 192 CG CD OE1 OE2
REMARK 470 SER B 225 OG
REMARK 470 ARG B 239 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 240 CG CD CE NZ
REMARK 470 GLU B 241 CG CD OE1 OE2
REMARK 470 LEU B 277 CG CD1 CD2
REMARK 470 ARG B 319 CG CD NE CZ NH1 NH2
REMARK 470 HIS B 320 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 322 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 352 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 355 CG CD OE1 OE2
REMARK 470 ARG B 358 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 362 CG1 CG2
REMARK 470 SER B 368 OG
REMARK 470 HIS B 373 CG ND1 CD2 CE1 NE2
REMARK 470 SER B 374 OG
REMARK 470 VAL B 377 CG1 CG2
REMARK 470 GLU B 379 CG CD OE1 OE2
REMARK 470 MET B 381 CG SD CE
REMARK 470 GLU B 382 CG CD OE1 OE2
REMARK 470 LYS B 386 CG CD CE NZ
REMARK 470 SER B 391 OG
REMARK 470 ASN B 392 CG OD1 ND2
REMARK 470 PHE B 394 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP B 395 CG OD1 OD2
REMARK 470 GLU B 398 CG CD OE1 OE2
REMARK 470 ARG B 431 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 432 CG CD OE1 NE2
REMARK 470 GLU B 441 CG CD OE1 OE2
REMARK 470 GLU B 544 CG CD OE1 OE2
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 A 20 CB CYS A 20 SG -0.118
REMARK 500 CYS A 526 CB CYS A 526 SG 0.184
REMARK 500 CYS B 526 CB CYS B 526 SG 0.127
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 75 CB - CA - C ANGL. DEV. = -15.5 DEGREES
REMARK 500 MET A 300 CG - SD - CE ANGL. DEV. = -15.3 DEGREES
REMARK 500 PRO B 269 C - N - CD ANGL. DEV. = -23.3 DEGREES
REMARK 500 LEU B 469 CA - CB - CG ANGL. DEV. = 14.3 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 ASN A 8 -47.59 -23.62
REMARK 500 THR A 28 87.23 -58.32
REMARK 500 SER A 30 39.36 124.42
REMARK 500 GLU A 33 41.66 88.50
REMARK 500 ARG A 34 88.15 175.67
REMARK 500 PRO A 54 81.69 -66.11
REMARK 500 ALA A 56 163.42 -47.43
REMARK 500 LEU A 77 -16.48 -49.67
REMARK 500 GLU A 79 -18.20 -49.49
REMARK 500 GLU A 120 57.80 33.63
REMARK 500 GLU A 141 -69.60 -103.51
REMARK 500 HIS A 203 -69.05 -92.55
REMARK 500 ASN A 214 67.56 -154.62
REMARK 500 ARG A 239 19.74 45.01
REMARK 500 GLU A 241 58.46 -169.09
REMARK 500 SER A 242 19.95 -58.10
REMARK 500 ASP A 243 -117.17 -48.55
REMARK 500 PHE A 301 115.16 117.42
REMARK 500 THR A 306 -77.68 -127.03
REMARK 500 SER A 329 -1.35 78.86
REMARK 500 ASP A 338 -179.41 -67.61
REMARK 500 ALA A 399 -89.81 -70.72
REMARK 500 PRO A 401 104.74 -53.36
REMARK 500 ALA A 402 178.36 151.22
REMARK 500 LEU A 403 33.77 168.23
REMARK 500 SER A 443 -144.96 7.04
REMARK 500 CYS A 445 156.03 169.49
REMARK 500 GLU A 453 41.80 81.75
REMARK 500 HIS A 477 -6.20 81.26
REMARK 500 CYS A 526 -114.43 28.36
REMARK 500 VAL A 583 -10.62 -144.85
REMARK 500 VAL A 618 -82.81 -74.40
REMARK 500 ASP A 619 62.18 -101.77
REMARK 500 LEU B 77 -16.44 -49.67
REMARK 500 ILE B 111 112.86 -166.04
REMARK 500 PRO B 112 46.46 -84.66
REMARK 500 ASP B 115 99.93 -64.52
REMARK 500 ALA B 117 -176.04 -62.91
REMARK 500 ASP B 126 139.61 72.58
REMARK 500 GLU B 141 -70.32 -105.29
REMARK 500 ASP B 162 -40.91 60.30
REMARK 500 TYR B 163 -172.90 71.87
REMARK 500 SER B 164 161.07 97.38
REMARK 500 GLU B 179 44.69 -81.56
REMARK 500 ASN B 214 68.82 -155.45
REMARK 500 PRO B 223 -169.10 -70.17
REMARK 500 ASP B 238 88.71 -38.58
REMARK 500 ARG B 239 31.35 -96.07
REMARK 500 GLU B 241 51.77 -141.60
REMARK 500 ASP B 243 -112.47 -42.64
REMARK 500
REMARK 500 THIS ENTRY HAS 62 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 ASN A 6 ARG A 7 145.67
REMARK 500 MET A 300 PHE A 301 131.68
REMARK 500 THR B 267 GLY B 268 -147.65
REMARK 500 GLY B 268 PRO B 269 -124.22
REMARK 500 MET B 300 PHE B 301 134.17
REMARK 500 TYR B 428 GLY B 429 -148.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3R75 RELATED DB: PDB
REMARK 900 RELATED ID: 3R76 RELATED DB: PDB
REMARK 900 RELATED ID: 3R77 RELATED DB: PDB
DBREF 3R74 A 1 643 UNP Q396C7 Q396C7_BURS3 1 643
DBREF 3R74 B 1 643 UNP Q396C7 Q396C7_BURS3 1 643
SEQADV 3R74 GLY A -1 UNP Q396C7 EXPRESSION TAG
SEQADV 3R74 HIS A 0 UNP Q396C7 EXPRESSION TAG
SEQADV 3R74 GLY B -1 UNP Q396C7 EXPRESSION TAG
SEQADV 3R74 HIS B 0 UNP Q396C7 EXPRESSION TAG
SEQRES 1 A 645 GLY HIS MET ASN ALA ALA PRO ASN ARG ASN LEU PHE ASP
SEQRES 2 A 645 ARG VAL LEU HIS GLY GLN ALA PRO CYS PHE ALA LEU ILE
SEQRES 3 A 645 ALA ARG SER THR GLY SER ALA GLY GLU ARG ALA MET ILE
SEQRES 4 A 645 ASP VAL PHE ALA GLY ALA VAL SER TYR PRO SER SER LEU
SEQRES 5 A 645 ALA GLU LEU PRO LEU ALA ALA PRO THR ALA THR GLY ALA
SEQRES 6 A 645 ASP ARG GLN GLU LEU LEU VAL MET VAL PRO TYR ARG GLN
SEQRES 7 A 645 LEU HIS GLU ARG GLY PHE LYS THR HIS ASP ASP GLY ALA
SEQRES 8 A 645 PRO LEU VAL ALA ILE THR CYS ASP GLU HIS GLU THR VAL
SEQRES 9 A 645 SER ALA GLN LEU ALA LEU ALA ALA ILE PRO ASP ALA ASP
SEQRES 10 A 645 THR ALA LEU GLY GLU ARG HIS PHE ASP ILE ASP ASP GLU
SEQRES 11 A 645 ALA TYR ALA GLU ILE VAL GLU ARG VAL ILE THR ASP GLU
SEQRES 12 A 645 ILE GLY THR GLY ALA GLY SER ASN PHE VAL ILE LYS ARG
SEQRES 13 A 645 THR LEU GLU GLY ASP LEU ASP ASP TYR SER PRO ALA LYS
SEQRES 14 A 645 ALA LEU ALA VAL PHE LYS ARG LEU MET ARG ARG GLU VAL
SEQRES 15 A 645 GLY ALA TYR TRP ILE PHE VAL ILE HIS THR GLY GLU ARG
SEQRES 16 A 645 THR PHE VAL GLY ALA THR PRO GLU ARG HIS LEU THR LEU
SEQRES 17 A 645 HIS GLU GLY CYS ALA THR MET ASN PRO ILE SER GLY THR
SEQRES 18 A 645 TYR ARG TYR PRO GLN SER GLY PRO THR ILE ASP GLY ILE
SEQRES 19 A 645 ASN ALA PHE LEU GLY ASP ARG LYS GLU SER ASP GLU LEU
SEQRES 20 A 645 TYR MET VAL LEU ASP GLU GLU LEU LYS MET MET ALA ARG
SEQRES 21 A 645 ILE CYS PRO ALA GLY GLY GLN VAL THR GLY PRO HIS LEU
SEQRES 22 A 645 ARG GLU MET ALA ARG LEU ALA HIS THR GLU TYR PHE ILE
SEQRES 23 A 645 VAL GLY HIS THR GLU ALA ASP VAL ARG ASP LEU LEU ARG
SEQRES 24 A 645 GLU THR MET PHE ALA PRO THR VAL THR GLY SER PRO ILE
SEQRES 25 A 645 GLU SER ALA THR ARG VAL ILE ALA ARG HIS GLU ARG ALA
SEQRES 26 A 645 GLY ARG GLY TYR TYR SER GLY ILE ALA ALA LEU ILE GLY
SEQRES 27 A 645 ARG ASP ALA ARG GLY GLY ARG THR LEU ASP SER ALA ILE
SEQRES 28 A 645 LEU ILE ARG THR ALA GLU ILE ASP ARG ALA GLY HIS VAL
SEQRES 29 A 645 ARG ILE GLY VAL GLY SER THR LEU VAL ARG HIS SER ASP
SEQRES 30 A 645 ALA VAL SER GLU VAL MET GLU THR HIS ALA LYS VAL ALA
SEQRES 31 A 645 ALA LEU SER ASN ALA PHE ASP PRO PRO GLU ALA GLY PRO
SEQRES 32 A 645 ALA LEU GLY GLN HIS PRO SER VAL GLN ALA ALA LEU ARG
SEQRES 33 A 645 GLU ARG ASN GLU GLY ILE ALA ASP PHE TRP PHE ARG PRO
SEQRES 34 A 645 TYR GLY GLY ARG GLN GLY GLU MET ALA ASP GLU LEU ALA
SEQRES 35 A 645 GLU LEU SER GLY CYS ARG ALA LEU ILE VAL ASP ALA GLU
SEQRES 36 A 645 ASP HIS PHE THR ALA MET ILE ALA GLN GLN LEU SER SER
SEQRES 37 A 645 LEU GLY LEU ALA THR GLU VAL CYS GLY VAL HIS ASP ALA
SEQRES 38 A 645 VAL ASP LEU ALA ARG TYR ASP VAL VAL VAL MET GLY PRO
SEQRES 39 A 645 GLY PRO GLY ASP PRO SER ASP ALA GLY ASP PRO ARG ILE
SEQRES 40 A 645 ALA ARG LEU TYR ALA TRP LEU ARG HIS LEU ILE ASP GLU
SEQRES 41 A 645 GLY LYS PRO PHE MET ALA VAL CYS LEU SER HIS GLN ILE
SEQRES 42 A 645 LEU ASN ALA ILE LEU GLY ILE PRO LEU VAL ARG ARG GLU
SEQRES 43 A 645 VAL PRO ASN GLN GLY ILE GLN VAL GLU ILE ASP LEU PHE
SEQRES 44 A 645 GLY GLN ARG GLU ARG VAL GLY PHE TYR ASN THR TYR VAL
SEQRES 45 A 645 ALA GLN THR VAL ARG ASP GLU MET ASP VAL ASP GLY VAL
SEQRES 46 A 645 GLY THR VAL ALA ILE SER ARG ASP PRO ARG THR GLY GLU
SEQRES 47 A 645 VAL HIS ALA LEU ARG GLY PRO THR PHE SER SER MET GLN
SEQRES 48 A 645 PHE HIS ALA GLU SER VAL LEU THR VAL ASP GLY PRO ARG
SEQRES 49 A 645 ILE LEU GLY GLU ALA ILE THR HIS ALA ILE ARG ARG GLU
SEQRES 50 A 645 LYS ARG MET THR ALA LEU THR ALA
SEQRES 1 B 645 GLY HIS MET ASN ALA ALA PRO ASN ARG ASN LEU PHE ASP
SEQRES 2 B 645 ARG VAL LEU HIS GLY GLN ALA PRO CYS PHE ALA LEU ILE
SEQRES 3 B 645 ALA ARG SER THR GLY SER ALA GLY GLU ARG ALA MET ILE
SEQRES 4 B 645 ASP VAL PHE ALA GLY ALA VAL SER TYR PRO SER SER LEU
SEQRES 5 B 645 ALA GLU LEU PRO LEU ALA ALA PRO THR ALA THR GLY ALA
SEQRES 6 B 645 ASP ARG GLN GLU LEU LEU VAL MET VAL PRO TYR ARG GLN
SEQRES 7 B 645 LEU HIS GLU ARG GLY PHE LYS THR HIS ASP ASP GLY ALA
SEQRES 8 B 645 PRO LEU VAL ALA ILE THR CYS ASP GLU HIS GLU THR VAL
SEQRES 9 B 645 SER ALA GLN LEU ALA LEU ALA ALA ILE PRO ASP ALA ASP
SEQRES 10 B 645 THR ALA LEU GLY GLU ARG HIS PHE ASP ILE ASP ASP GLU
SEQRES 11 B 645 ALA TYR ALA GLU ILE VAL GLU ARG VAL ILE THR ASP GLU
SEQRES 12 B 645 ILE GLY THR GLY ALA GLY SER ASN PHE VAL ILE LYS ARG
SEQRES 13 B 645 THR LEU GLU GLY ASP LEU ASP ASP TYR SER PRO ALA LYS
SEQRES 14 B 645 ALA LEU ALA VAL PHE LYS ARG LEU MET ARG ARG GLU VAL
SEQRES 15 B 645 GLY ALA TYR TRP ILE PHE VAL ILE HIS THR GLY GLU ARG
SEQRES 16 B 645 THR PHE VAL GLY ALA THR PRO GLU ARG HIS LEU THR LEU
SEQRES 17 B 645 HIS GLU GLY CYS ALA THR MET ASN PRO ILE SER GLY THR
SEQRES 18 B 645 TYR ARG TYR PRO GLN SER GLY PRO THR ILE ASP GLY ILE
SEQRES 19 B 645 ASN ALA PHE LEU GLY ASP ARG LYS GLU SER ASP GLU LEU
SEQRES 20 B 645 TYR MET VAL LEU ASP GLU GLU LEU LYS MET MET ALA ARG
SEQRES 21 B 645 ILE CYS PRO ALA GLY GLY GLN VAL THR GLY PRO HIS LEU
SEQRES 22 B 645 ARG GLU MET ALA ARG LEU ALA HIS THR GLU TYR PHE ILE
SEQRES 23 B 645 VAL GLY HIS THR GLU ALA ASP VAL ARG ASP LEU LEU ARG
SEQRES 24 B 645 GLU THR MET PHE ALA PRO THR VAL THR GLY SER PRO ILE
SEQRES 25 B 645 GLU SER ALA THR ARG VAL ILE ALA ARG HIS GLU ARG ALA
SEQRES 26 B 645 GLY ARG GLY TYR TYR SER GLY ILE ALA ALA LEU ILE GLY
SEQRES 27 B 645 ARG ASP ALA ARG GLY GLY ARG THR LEU ASP SER ALA ILE
SEQRES 28 B 645 LEU ILE ARG THR ALA GLU ILE ASP ARG ALA GLY HIS VAL
SEQRES 29 B 645 ARG ILE GLY VAL GLY SER THR LEU VAL ARG HIS SER ASP
SEQRES 30 B 645 ALA VAL SER GLU VAL MET GLU THR HIS ALA LYS VAL ALA
SEQRES 31 B 645 ALA LEU SER ASN ALA PHE ASP PRO PRO GLU ALA GLY PRO
SEQRES 32 B 645 ALA LEU GLY GLN HIS PRO SER VAL GLN ALA ALA LEU ARG
SEQRES 33 B 645 GLU ARG ASN GLU GLY ILE ALA ASP PHE TRP PHE ARG PRO
SEQRES 34 B 645 TYR GLY GLY ARG GLN GLY GLU MET ALA ASP GLU LEU ALA
SEQRES 35 B 645 GLU LEU SER GLY CYS ARG ALA LEU ILE VAL ASP ALA GLU
SEQRES 36 B 645 ASP HIS PHE THR ALA MET ILE ALA GLN GLN LEU SER SER
SEQRES 37 B 645 LEU GLY LEU ALA THR GLU VAL CYS GLY VAL HIS ASP ALA
SEQRES 38 B 645 VAL ASP LEU ALA ARG TYR ASP VAL VAL VAL MET GLY PRO
SEQRES 39 B 645 GLY PRO GLY ASP PRO SER ASP ALA GLY ASP PRO ARG ILE
SEQRES 40 B 645 ALA ARG LEU TYR ALA TRP LEU ARG HIS LEU ILE ASP GLU
SEQRES 41 B 645 GLY LYS PRO PHE MET ALA VAL CYS LEU SER HIS GLN ILE
SEQRES 42 B 645 LEU ASN ALA ILE LEU GLY ILE PRO LEU VAL ARG ARG GLU
SEQRES 43 B 645 VAL PRO ASN GLN GLY ILE GLN VAL GLU ILE ASP LEU PHE
SEQRES 44 B 645 GLY GLN ARG GLU ARG VAL GLY PHE TYR ASN THR TYR VAL
SEQRES 45 B 645 ALA GLN THR VAL ARG ASP GLU MET ASP VAL ASP GLY VAL
SEQRES 46 B 645 GLY THR VAL ALA ILE SER ARG ASP PRO ARG THR GLY GLU
SEQRES 47 B 645 VAL HIS ALA LEU ARG GLY PRO THR PHE SER SER MET GLN
SEQRES 48 B 645 PHE HIS ALA GLU SER VAL LEU THR VAL ASP GLY PRO ARG
SEQRES 49 B 645 ILE LEU GLY GLU ALA ILE THR HIS ALA ILE ARG ARG GLU
SEQRES 50 B 645 LYS ARG MET THR ALA LEU THR ALA
FORMUL 3 HOH *80(H2 O)
HELIX 1 1 ARG A 7 HIS A 15 1 9
HELIX 2 2 SER A 49 LEU A 53 5 5
HELIX 3 3 PRO A 73 GLY A 81 5 9
HELIX 4 4 ALA A 104 ILE A 111 1 8
HELIX 5 5 ASP A 126 GLU A 141 1 16
HELIX 6 6 ILE A 142 GLY A 145 5 4
HELIX 7 7 SER A 164 GLU A 179 1 16
HELIX 8 8 THR A 228 ARG A 239 1 12
HELIX 9 9 SER A 242 CYS A 260 1 19
HELIX 10 10 ASP A 291 THR A 299 1 9
HELIX 11 11 ALA A 302 VAL A 305 5 4
HELIX 12 12 PRO A 309 GLU A 321 1 13
HELIX 13 13 ASP A 375 VAL A 387 1 13
HELIX 14 14 VAL A 387 ASP A 395 1 9
HELIX 15 15 HIS A 406 ARG A 416 1 11
HELIX 16 16 ASN A 417 GLY A 419 5 3
HELIX 17 17 ASP A 422 ARG A 426 5 5
HELIX 18 18 HIS A 455 LEU A 467 1 13
HELIX 19 19 ASP A 481 TYR A 485 5 5
HELIX 20 20 ASP A 502 GLY A 519 1 18
HELIX 21 21 CYS A 526 GLY A 537 1 12
HELIX 22 22 ASP A 619 ILE A 632 1 14
HELIX 23 23 LEU B 9 LEU B 14 1 6
HELIX 24 24 SER B 49 LEU B 53 5 5
HELIX 25 25 PRO B 73 GLY B 81 5 9
HELIX 26 26 ALA B 104 ALA B 110 1 7
HELIX 27 27 ASP B 126 GLU B 141 1 16
HELIX 28 28 ILE B 142 GLY B 145 5 4
HELIX 29 29 SER B 164 GLU B 179 1 16
HELIX 30 30 THR B 228 ASP B 238 1 11
HELIX 31 31 SER B 242 CYS B 260 1 19
HELIX 32 32 ASP B 291 THR B 299 1 9
HELIX 33 33 ALA B 302 VAL B 305 5 4
HELIX 34 34 PRO B 309 ARG B 319 1 11
HELIX 35 35 ASP B 375 VAL B 387 1 13
HELIX 36 36 VAL B 387 ASN B 392 1 6
HELIX 37 37 ALA B 402 GLN B 405 5 4
HELIX 38 38 HIS B 406 ARG B 416 1 11
HELIX 39 39 ASP B 422 ARG B 426 5 5
HELIX 40 40 HIS B 455 LEU B 467 1 13
HELIX 41 41 ASP B 481 TYR B 485 5 5
HELIX 42 42 ASP B 502 GLY B 519 1 18
HELIX 43 43 CYS B 526 GLY B 537 1 12
HELIX 44 44 ASP B 619 ARG B 633 1 15
SHEET 1 A 9 GLU A 98 SER A 103 0
SHEET 2 A 9 MET A 36 ALA A 41 -1 N VAL A 39 O GLU A 100
SHEET 3 A 9 PHE A 21 ARG A 26 -1 N ILE A 24 O ASP A 38
SHEET 4 A 9 TRP A 184 HIS A 189 -1 O HIS A 189 N PHE A 21
SHEET 5 A 9 ARG A 193 THR A 199 -1 O PHE A 195 N ILE A 188
SHEET 6 A 9 THR A 353 ASP A 357 -1 O ALA A 354 N VAL A 196
SHEET 7 A 9 HIS A 361 LEU A 370 -1 O ARG A 363 N GLU A 355
SHEET 8 A 9 ASN A 149 LEU A 160 -1 N LEU A 156 O ILE A 364
SHEET 9 A 9 LEU A 118 PHE A 123 -1 N GLY A 119 O ASP A 159
SHEET 1 B 9 GLU A 98 SER A 103 0
SHEET 2 B 9 MET A 36 ALA A 41 -1 N VAL A 39 O GLU A 100
SHEET 3 B 9 PHE A 21 ARG A 26 -1 N ILE A 24 O ASP A 38
SHEET 4 B 9 TRP A 184 HIS A 189 -1 O HIS A 189 N PHE A 21
SHEET 5 B 9 ARG A 193 THR A 199 -1 O PHE A 195 N ILE A 188
SHEET 6 B 9 THR A 353 ASP A 357 -1 O ALA A 354 N VAL A 196
SHEET 7 B 9 HIS A 361 LEU A 370 -1 O ARG A 363 N GLU A 355
SHEET 8 B 9 ASN A 149 LEU A 160 -1 N LEU A 156 O ILE A 364
SHEET 9 B 9 GLY A 307 SER A 308 -1 O SER A 308 N ASN A 149
SHEET 1 C 9 VAL A 44 SER A 45 0
SHEET 2 C 9 VAL A 92 THR A 95 -1 O ALA A 93 N SER A 45
SHEET 3 C 9 ARG A 65 VAL A 72 -1 N LEU A 69 O ILE A 94
SHEET 4 C 9 ILE A 331 ARG A 337 -1 O ILE A 331 N VAL A 72
SHEET 5 C 9 ARG A 343 ILE A 349 -1 O ASP A 346 N LEU A 334
SHEET 6 C 9 ARG A 202 HIS A 207 -1 N HIS A 203 O SER A 347
SHEET 7 C 9 CYS A 210 MET A 213 -1 O THR A 212 N THR A 205
SHEET 8 C 9 LEU A 277 HIS A 287 -1 O GLY A 286 N ALA A 211
SHEET 9 C 9 ILE A 216 ARG A 221 -1 N TYR A 220 O ALA A 278
SHEET 1 D 9 VAL A 44 SER A 45 0
SHEET 2 D 9 VAL A 92 THR A 95 -1 O ALA A 93 N SER A 45
SHEET 3 D 9 ARG A 65 VAL A 72 -1 N LEU A 69 O ILE A 94
SHEET 4 D 9 ILE A 331 ARG A 337 -1 O ILE A 331 N VAL A 72
SHEET 5 D 9 ARG A 343 ILE A 349 -1 O ASP A 346 N LEU A 334
SHEET 6 D 9 ARG A 202 HIS A 207 -1 N HIS A 203 O SER A 347
SHEET 7 D 9 CYS A 210 MET A 213 -1 O THR A 212 N THR A 205
SHEET 8 D 9 LEU A 277 HIS A 287 -1 O GLY A 286 N ALA A 211
SHEET 9 D 9 GLN A 265 GLU A 273 -1 N HIS A 270 O GLU A 281
SHEET 1 E 8 LEU A 469 GLY A 475 0
SHEET 2 E 8 CYS A 445 ASP A 451 1 N CYS A 445 O ALA A 470
SHEET 3 E 8 VAL A 487 MET A 490 1 O VAL A 489 N LEU A 448
SHEET 4 E 8 PHE A 522 VAL A 525 1 O MET A 523 N MET A 490
SHEET 5 E 8 PHE A 605 MET A 608 1 O MET A 608 N ALA A 524
SHEET 6 E 8 VAL A 597 ARG A 601 -1 N LEU A 600 O SER A 607
SHEET 7 E 8 GLY A 584 ARG A 590 -1 N SER A 589 O HIS A 598
SHEET 8 E 8 GLU A 577 VAL A 580 -1 N VAL A 580 O GLY A 584
SHEET 1 F 2 LEU A 540 ARG A 542 0
SHEET 2 F 2 TYR A 569 ALA A 571 -1 O VAL A 570 N VAL A 541
SHEET 1 G 2 ILE A 550 LEU A 556 0
SHEET 2 G 2 GLN A 559 PHE A 565 -1 O PHE A 565 N ILE A 550
SHEET 1 H 9 GLU B 98 SER B 103 0
SHEET 2 H 9 MET B 36 ALA B 41 -1 N VAL B 39 O GLU B 100
SHEET 3 H 9 PHE B 21 ARG B 26 -1 N ILE B 24 O ASP B 38
SHEET 4 H 9 TRP B 184 HIS B 189 -1 O HIS B 189 N PHE B 21
SHEET 5 H 9 THR B 194 THR B 199 -1 O PHE B 195 N ILE B 188
SHEET 6 H 9 THR B 353 ILE B 356 -1 O ALA B 354 N VAL B 196
SHEET 7 H 9 HIS B 361 LEU B 370 -1 O ARG B 363 N GLU B 355
SHEET 8 H 9 ASN B 149 ASP B 159 -1 N LEU B 156 O ILE B 364
SHEET 9 H 9 GLY B 119 PHE B 123 -1 N HIS B 122 O GLU B 157
SHEET 1 I 9 GLU B 98 SER B 103 0
SHEET 2 I 9 MET B 36 ALA B 41 -1 N VAL B 39 O GLU B 100
SHEET 3 I 9 PHE B 21 ARG B 26 -1 N ILE B 24 O ASP B 38
SHEET 4 I 9 TRP B 184 HIS B 189 -1 O HIS B 189 N PHE B 21
SHEET 5 I 9 THR B 194 THR B 199 -1 O PHE B 195 N ILE B 188
SHEET 6 I 9 THR B 353 ILE B 356 -1 O ALA B 354 N VAL B 196
SHEET 7 I 9 HIS B 361 LEU B 370 -1 O ARG B 363 N GLU B 355
SHEET 8 I 9 ASN B 149 ASP B 159 -1 N LEU B 156 O ILE B 364
SHEET 9 I 9 GLY B 307 SER B 308 -1 O SER B 308 N ASN B 149
SHEET 1 J 9 VAL B 44 SER B 45 0
SHEET 2 J 9 VAL B 92 THR B 95 -1 O ALA B 93 N SER B 45
SHEET 3 J 9 ARG B 65 VAL B 72 -1 N LEU B 69 O ILE B 94
SHEET 4 J 9 ILE B 331 ARG B 337 -1 O ILE B 331 N VAL B 72
SHEET 5 J 9 ARG B 343 ILE B 349 -1 O ASP B 346 N LEU B 334
SHEET 6 J 9 ARG B 202 HIS B 207 -1 N LEU B 206 O LEU B 345
SHEET 7 J 9 CYS B 210 MET B 213 -1 O CYS B 210 N HIS B 207
SHEET 8 J 9 LEU B 277 HIS B 287 -1 O GLY B 286 N ALA B 211
SHEET 9 J 9 ILE B 216 ARG B 221 -1 N TYR B 220 O ALA B 278
SHEET 1 K 9 VAL B 44 SER B 45 0
SHEET 2 K 9 VAL B 92 THR B 95 -1 O ALA B 93 N SER B 45
SHEET 3 K 9 ARG B 65 VAL B 72 -1 N LEU B 69 O ILE B 94
SHEET 4 K 9 ILE B 331 ARG B 337 -1 O ILE B 331 N VAL B 72
SHEET 5 K 9 ARG B 343 ILE B 349 -1 O ASP B 346 N LEU B 334
SHEET 6 K 9 ARG B 202 HIS B 207 -1 N LEU B 206 O LEU B 345
SHEET 7 K 9 CYS B 210 MET B 213 -1 O CYS B 210 N HIS B 207
SHEET 8 K 9 LEU B 277 HIS B 287 -1 O GLY B 286 N ALA B 211
SHEET 9 K 9 GLN B 265 GLU B 273 -1 N ARG B 272 O HIS B 279
SHEET 1 L 8 ALA B 470 GLY B 475 0
SHEET 2 L 8 ARG B 446 ASP B 451 1 N ALA B 447 O ALA B 470
SHEET 3 L 8 VAL B 487 MET B 490 1 O VAL B 489 N LEU B 448
SHEET 4 L 8 PHE B 522 VAL B 525 1 O MET B 523 N MET B 490
SHEET 5 L 8 PHE B 605 MET B 608 1 O MET B 608 N ALA B 524
SHEET 6 L 8 VAL B 597 ARG B 601 -1 N LEU B 600 O SER B 607
SHEET 7 L 8 GLY B 584 ARG B 590 -1 N ALA B 587 O ARG B 601
SHEET 8 L 8 GLU B 577 VAL B 580 -1 N VAL B 580 O GLY B 584
SHEET 1 M 2 LEU B 540 ARG B 542 0
SHEET 2 M 2 TYR B 569 ALA B 571 -1 O VAL B 570 N VAL B 541
SHEET 1 N 2 ILE B 550 LEU B 556 0
SHEET 2 N 2 GLN B 559 PHE B 565 -1 O PHE B 565 N ILE B 550
CISPEP 1 GLN A 224 SER A 225 0 6.11
CISPEP 2 GLY A 268 PRO A 269 0 3.60
CISPEP 3 SER A 308 PRO A 309 0 2.83
CISPEP 4 SER B 308 PRO B 309 0 0.24
CRYST1 172.360 172.360 216.440 90.00 90.00 120.00 P 62 2 2 24
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 0.005802 0.003350 0.000000 0.00000
SCALE2 0.000000 0.006699 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004620 0.00000
(ATOM LINES ARE NOT SHOWN.)
END