HEADER OXIDOREDUCTASE 11-FEB-11 3QP9
TITLE THE STRUCTURE OF A C2-TYPE KETOREDUCTASE FROM A MODULAR POLYKETIDE
TITLE 2 SYNTHASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYPE I POLYKETIDE SYNTHASE PIKAII;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 920-1423;
COMPND 5 EC: 1.1.1.100;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES VENEZUELAE;
SOURCE 3 ORGANISM_TAXID: 54571;
SOURCE 4 STRAIN: ATCC15439;
SOURCE 5 GENE: PIKAII;
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: PET28B
KEYWDS ROSSMANN FOLD, KETOREDUCTASE, EPIMERIZATION, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ZHENG,A.T.KEATINGE-CLAY
REVDAT 4 13-SEP-23 3QP9 1 SEQADV
REVDAT 3 13-JUL-11 3QP9 1 JRNL
REVDAT 2 22-JUN-11 3QP9 1 JRNL
REVDAT 1 11-MAY-11 3QP9 0
JRNL AUTH J.ZHENG,A.T.KEATINGE-CLAY
JRNL TITL STRUCTURAL AND FUNCTIONAL ANALYSIS OF C2-TYPE KETOREDUCTASES
JRNL TITL 2 FROM MODULAR POLYKETIDE SYNTHASES.
JRNL REF J.MOL.BIOL. V. 410 105 2011
JRNL REFN ISSN 0022-2836
JRNL PMID 21570406
JRNL DOI 10.1016/J.JMB.2011.04.065
REMARK 2
REMARK 2 RESOLUTION. 1.88 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 1.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.23
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 3 NUMBER OF REFLECTIONS : 137509
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) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7250
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) : 1.88
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.93
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9525
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.36
REMARK 3 BIN R VALUE (WORKING SET) : 0.3920
REMARK 3 BIN FREE R VALUE SET COUNT : 511
REMARK 3 BIN FREE R VALUE : 0.4370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13330
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 343
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.68000
REMARK 3 B22 (A**2) : 2.61000
REMARK 3 B33 (A**2) : -2.50000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.08000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.172
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.136
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.435
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13603 ; 0.023 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18647 ; 2.029 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1833 ; 6.498 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 496 ;35.018 ;22.198
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1857 ;18.057 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 129 ;17.660 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2222 ; 0.162 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10383 ; 0.011 ; 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): 9162 ; 1.289 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14464 ; 2.100 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4441 ; 3.149 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4183 ; 4.584 ; 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 : 4
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 -10 A 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9928 -18.3177 27.0953
REMARK 3 T TENSOR
REMARK 3 T11: 0.1475 T22: 0.0371
REMARK 3 T33: 0.1029 T12: -0.0259
REMARK 3 T13: -0.0124 T23: -0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 0.3915 L22: 0.0902
REMARK 3 L33: 0.5315 L12: 0.1352
REMARK 3 L13: 0.2175 L23: 0.1837
REMARK 3 S TENSOR
REMARK 3 S11: 0.0287 S12: -0.0495 S13: 0.0128
REMARK 3 S21: 0.0308 S22: -0.0269 S23: 0.0210
REMARK 3 S31: 0.1456 S32: -0.0028 S33: -0.0019
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 -10 B 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2276 12.0933 66.4617
REMARK 3 T TENSOR
REMARK 3 T11: 0.0567 T22: 0.0885
REMARK 3 T33: 0.1264 T12: -0.0062
REMARK 3 T13: 0.0385 T23: -0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 0.3998 L22: 0.4614
REMARK 3 L33: 0.4076 L12: 0.3754
REMARK 3 L13: -0.0768 L23: -0.2621
REMARK 3 S TENSOR
REMARK 3 S11: -0.0143 S12: 0.0336 S13: 0.0512
REMARK 3 S21: 0.0327 S22: 0.0711 S23: 0.0730
REMARK 3 S31: -0.0728 S32: -0.0193 S33: -0.0569
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 -10 C 9999
REMARK 3 ORIGIN FOR THE GROUP (A): -25.5841 -2.7658 42.1372
REMARK 3 T TENSOR
REMARK 3 T11: 0.0797 T22: 0.1868
REMARK 3 T33: 0.0413 T12: 0.0191
REMARK 3 T13: -0.0199 T23: 0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 0.5352 L22: 0.2738
REMARK 3 L33: 0.5070 L12: -0.0566
REMARK 3 L13: -0.1108 L23: -0.2495
REMARK 3 S TENSOR
REMARK 3 S11: 0.1072 S12: -0.0907 S13: -0.0196
REMARK 3 S21: -0.1071 S22: -0.1019 S23: 0.0649
REMARK 3 S31: 0.0296 S32: 0.2323 S33: -0.0053
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 : D -10 D 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9028 17.9683 2.4442
REMARK 3 T TENSOR
REMARK 3 T11: 0.1179 T22: 0.0809
REMARK 3 T33: 0.0927 T12: -0.0562
REMARK 3 T13: -0.0407 T23: 0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 0.7814 L22: 0.5432
REMARK 3 L33: 0.3696 L12: 0.1919
REMARK 3 L13: 0.4697 L23: 0.1520
REMARK 3 S TENSOR
REMARK 3 S11: -0.0396 S12: 0.0331 S13: 0.0886
REMARK 3 S21: 0.1739 S22: -0.0832 S23: -0.0303
REMARK 3 S31: -0.0259 S32: -0.0238 S33: 0.1228
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3QP9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000063930.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1159
REMARK 200 MONOCHROMATOR : DOUBLE FLAT CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 137509
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.880
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 37.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.68800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: PDB ENTRY 3MJS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 33% PEG4000, 0.25 M SODIUM ACETATE,
REMARK 280 0.1 M TRIS-CL, PH 8.3, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 75.04400
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 LEU A -7
REMARK 465 VAL A -6
REMARK 465 PRO A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 GLY A 1
REMARK 465 SER A 2
REMARK 465 ASP A 20
REMARK 465 ALA A 21
REMARK 465 SER A 22
REMARK 465 GLU A 23
REMARK 465 ARG A 24
REMARK 465 ALA A 25
REMARK 465 PRO A 218
REMARK 465 ALA A 219
REMARK 465 HIS A 220
REMARK 465 GLY A 266
REMARK 465 SER A 267
REMARK 465 GLU A 268
REMARK 465 GLY A 269
REMARK 465 ALA A 270
REMARK 465 GLU A 271
REMARK 465 GLY A 272
REMARK 465 THR A 273
REMARK 465 SER A 274
REMARK 465 GLY A 275
REMARK 465 ALA A 276
REMARK 465 ALA A 277
REMARK 465 GLU A 278
REMARK 465 ASP A 279
REMARK 465 SER A 280
REMARK 465 ALA A 368
REMARK 465 ALA A 369
REMARK 465 GLY A 370
REMARK 465 GLY A 371
REMARK 465 GLN A 501
REMARK 465 GLN A 502
REMARK 465 SER A 503
REMARK 465 THR A 504
REMARK 465 MET B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 GLY B -8
REMARK 465 LEU B -7
REMARK 465 VAL B -6
REMARK 465 PRO B -5
REMARK 465 ARG B -4
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 HIS B -1
REMARK 465 MET B 0
REMARK 465 GLY B 1
REMARK 465 SER B 2
REMARK 465 VAL B 3
REMARK 465 GLN B 4
REMARK 465 ALA B 19
REMARK 465 ASP B 20
REMARK 465 ALA B 21
REMARK 465 SER B 22
REMARK 465 GLU B 23
REMARK 465 ARG B 24
REMARK 465 ALA B 25
REMARK 465 GLY B 266
REMARK 465 SER B 267
REMARK 465 GLU B 268
REMARK 465 GLY B 269
REMARK 465 ALA B 270
REMARK 465 GLU B 271
REMARK 465 GLY B 272
REMARK 465 THR B 273
REMARK 465 SER B 274
REMARK 465 GLY B 275
REMARK 465 ALA B 276
REMARK 465 ALA B 277
REMARK 465 GLU B 278
REMARK 465 ASP B 279
REMARK 465 SER B 280
REMARK 465 GLY B 281
REMARK 465 LEU B 282
REMARK 465 ALA B 283
REMARK 465 ALA B 367
REMARK 465 ALA B 368
REMARK 465 ALA B 369
REMARK 465 GLY B 370
REMARK 465 GLY B 371
REMARK 465 ARG B 372
REMARK 465 ARG B 496
REMARK 465 ALA B 497
REMARK 465 LEU B 498
REMARK 465 ASP B 499
REMARK 465 GLU B 500
REMARK 465 GLN B 501
REMARK 465 GLN B 502
REMARK 465 SER B 503
REMARK 465 THR B 504
REMARK 465 MET C -20
REMARK 465 GLY C -19
REMARK 465 SER C -18
REMARK 465 SER C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 SER C -10
REMARK 465 SER C -9
REMARK 465 GLY C -8
REMARK 465 LEU C -7
REMARK 465 VAL C -6
REMARK 465 PRO C -5
REMARK 465 ARG C -4
REMARK 465 GLY C -3
REMARK 465 SER C -2
REMARK 465 HIS C -1
REMARK 465 MET C 0
REMARK 465 GLY C 1
REMARK 465 SER C 2
REMARK 465 VAL C 18
REMARK 465 ALA C 19
REMARK 465 ASP C 20
REMARK 465 ALA C 21
REMARK 465 SER C 22
REMARK 465 GLU C 23
REMARK 465 ARG C 24
REMARK 465 ALA C 25
REMARK 465 ALA C 219
REMARK 465 HIS C 220
REMARK 465 SER C 267
REMARK 465 GLU C 268
REMARK 465 GLY C 269
REMARK 465 ALA C 270
REMARK 465 GLU C 271
REMARK 465 GLY C 272
REMARK 465 THR C 273
REMARK 465 SER C 274
REMARK 465 GLY C 275
REMARK 465 ALA C 276
REMARK 465 ALA C 277
REMARK 465 GLU C 278
REMARK 465 ASP C 279
REMARK 465 SER C 280
REMARK 465 ALA C 367
REMARK 465 ALA C 368
REMARK 465 ALA C 369
REMARK 465 ARG C 495
REMARK 465 ARG C 496
REMARK 465 ALA C 497
REMARK 465 LEU C 498
REMARK 465 ASP C 499
REMARK 465 GLU C 500
REMARK 465 GLN C 501
REMARK 465 GLN C 502
REMARK 465 SER C 503
REMARK 465 THR C 504
REMARK 465 MET D -20
REMARK 465 GLY D -19
REMARK 465 SER D -18
REMARK 465 SER D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 SER D -10
REMARK 465 SER D -9
REMARK 465 GLY D -8
REMARK 465 LEU D -7
REMARK 465 VAL D -6
REMARK 465 PRO D -5
REMARK 465 ARG D -4
REMARK 465 GLY D -3
REMARK 465 SER D -2
REMARK 465 HIS D -1
REMARK 465 MET D 0
REMARK 465 GLY D 1
REMARK 465 SER D 2
REMARK 465 VAL D 3
REMARK 465 GLN D 4
REMARK 465 ASP D 5
REMARK 465 VAL D 18
REMARK 465 ALA D 19
REMARK 465 ASP D 20
REMARK 465 ALA D 21
REMARK 465 SER D 22
REMARK 465 GLU D 23
REMARK 465 ARG D 24
REMARK 465 ALA D 25
REMARK 465 PRO D 218
REMARK 465 ALA D 219
REMARK 465 HIS D 220
REMARK 465 GLY D 266
REMARK 465 SER D 267
REMARK 465 GLU D 268
REMARK 465 GLY D 269
REMARK 465 ALA D 270
REMARK 465 GLU D 271
REMARK 465 GLY D 272
REMARK 465 THR D 273
REMARK 465 SER D 274
REMARK 465 GLY D 275
REMARK 465 ALA D 276
REMARK 465 ALA D 277
REMARK 465 GLU D 278
REMARK 465 ASP D 279
REMARK 465 ALA D 368
REMARK 465 ALA D 369
REMARK 465 GLY D 370
REMARK 465 GLY D 371
REMARK 465 ARG D 372
REMARK 465 GLU D 493
REMARK 465 ALA D 494
REMARK 465 ARG D 495
REMARK 465 ARG D 496
REMARK 465 ALA D 497
REMARK 465 LEU D 498
REMARK 465 ASP D 499
REMARK 465 GLU D 500
REMARK 465 GLN D 501
REMARK 465 GLN D 502
REMARK 465 SER D 503
REMARK 465 THR D 504
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 VAL A 138 CB VAL A 138 CG1 0.136
REMARK 500 VAL A 160 CB VAL A 160 CG1 0.148
REMARK 500 TRP B 13 CE3 TRP B 13 CZ3 0.102
REMARK 500 ALA B 94 CA ALA B 94 CB 0.133
REMARK 500 VAL B 415 CB VAL B 415 CG1 0.158
REMARK 500 THR D 398 CB THR D 398 CG2 -0.321
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 10 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 248 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 LEU A 282 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 ARG A 347 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 THR A 398 CA - CB - CG2 ANGL. DEV. = 10.0 DEGREES
REMARK 500 ASP A 471 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 490 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG B 10 NE - CZ - NH1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG B 10 NE - CZ - NH2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG B 15 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 39 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG B 68 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG B 68 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG B 181 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG C 10 NE - CZ - NH1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG C 10 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ASP C 96 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG C 211 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 LEU D 285 CB - CG - CD2 ANGL. DEV. = 12.0 DEGREES
REMARK 500 LEU D 322 CA - CB - CG ANGL. DEV. = 16.4 DEGREES
REMARK 500 THR D 398 N - CA - CB ANGL. DEV. = -11.5 DEGREES
REMARK 500 HIS D 408 CB - CA - C ANGL. DEV. = 14.6 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 GLN A 4 -18.73 178.60
REMARK 500 ALA A 41 -78.17 -26.78
REMARK 500 ALA A 43 -38.89 113.40
REMARK 500 SER A 177 -38.48 -32.88
REMARK 500 ASP A 178 -61.40 -100.60
REMARK 500 ALA A 179 111.34 87.55
REMARK 500 ALA A 215 56.90 -112.72
REMARK 500 LEU A 282 -136.10 -128.81
REMARK 500 SER A 380 -158.44 -108.29
REMARK 500 GLU A 430 15.99 -42.47
REMARK 500 ALA A 432 -74.63 -70.07
REMARK 500 LEU A 440 4.11 -68.04
REMARK 500 ALA B 43 -38.45 95.56
REMARK 500 ASP B 178 64.27 -104.01
REMARK 500 ALA B 215 65.56 -105.78
REMARK 500 HIS B 220 -91.69 -53.25
REMARK 500 THR B 222 112.42 60.95
REMARK 500 PRO B 264 -175.02 -55.24
REMARK 500 LEU B 322 121.50 -33.53
REMARK 500 SER B 380 -159.88 -108.06
REMARK 500 ASP B 411 51.39 -149.56
REMARK 500 THR B 433 63.18 -67.60
REMARK 500 GLU B 435 -60.01 4.38
REMARK 500 THR B 480 41.21 -105.26
REMARK 500 ALA C 179 99.70 36.79
REMARK 500 ALA C 215 60.16 -107.52
REMARK 500 LEU C 322 130.26 -39.00
REMARK 500 ARG C 372 120.24 -36.02
REMARK 500 SER C 380 -159.08 -103.43
REMARK 500 ILE C 385 -60.55 -98.95
REMARK 500 ASP C 411 48.17 -157.73
REMARK 500 ARG C 427 -38.60 -35.62
REMARK 500 PRO C 444 134.47 -39.04
REMARK 500 SER C 474 -40.30 167.19
REMARK 500 THR C 481 -85.00 -92.19
REMARK 500 SER D 28 122.45 -177.69
REMARK 500 ASP D 38 -24.60 73.29
REMARK 500 ALA D 41 -78.56 -52.81
REMARK 500 GLU D 42 -163.65 -61.72
REMARK 500 ALA D 43 -44.39 71.10
REMARK 500 ALA D 81 29.90 -72.87
REMARK 500 ALA D 82 17.38 -160.02
REMARK 500 ALA D 179 98.04 -4.13
REMARK 500 GLU D 335 128.25 -174.56
REMARK 500 SER D 380 -161.41 -104.88
REMARK 500 ARG D 427 -35.43 150.57
REMARK 500 THR D 481 -99.72 -78.44
REMARK 500 ASP D 490 -8.55 158.39
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3QP9 A 1 504 UNP Q9ZGI4 Q9ZGI4_9ACTO 920 1423
DBREF 3QP9 B 1 504 UNP Q9ZGI4 Q9ZGI4_9ACTO 920 1423
DBREF 3QP9 C 1 504 UNP Q9ZGI4 Q9ZGI4_9ACTO 920 1423
DBREF 3QP9 D 1 504 UNP Q9ZGI4 Q9ZGI4_9ACTO 920 1423
SEQADV 3QP9 MET A -20 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 GLY A -19 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 SER A -18 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 SER A -17 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS A -16 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS A -15 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS A -14 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS A -13 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS A -12 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS A -11 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 SER A -10 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 SER A -9 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 GLY A -8 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 LEU A -7 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 VAL A -6 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 PRO A -5 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 ARG A -4 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 GLY A -3 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 SER A -2 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS A -1 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 MET A 0 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 MET B -20 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 GLY B -19 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 SER B -18 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 SER B -17 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS B -16 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS B -15 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS B -14 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS B -13 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS B -12 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS B -11 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 SER B -10 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 SER B -9 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 GLY B -8 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 LEU B -7 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 VAL B -6 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 PRO B -5 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 ARG B -4 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 GLY B -3 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 SER B -2 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS B -1 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 MET B 0 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 MET C -20 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 GLY C -19 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 SER C -18 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 SER C -17 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS C -16 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS C -15 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS C -14 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS C -13 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS C -12 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS C -11 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 SER C -10 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 SER C -9 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 GLY C -8 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 LEU C -7 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 VAL C -6 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 PRO C -5 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 ARG C -4 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 GLY C -3 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 SER C -2 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS C -1 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 MET C 0 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 MET D -20 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 GLY D -19 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 SER D -18 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 SER D -17 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS D -16 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS D -15 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS D -14 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS D -13 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS D -12 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS D -11 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 SER D -10 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 SER D -9 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 GLY D -8 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 LEU D -7 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 VAL D -6 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 PRO D -5 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 ARG D -4 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 GLY D -3 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 SER D -2 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 HIS D -1 UNP Q9ZGI4 EXPRESSION TAG
SEQADV 3QP9 MET D 0 UNP Q9ZGI4 EXPRESSION TAG
SEQRES 1 A 525 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 525 LEU VAL PRO ARG GLY SER HIS MET GLY SER VAL GLN ASP
SEQRES 3 A 525 SER TRP ARG TYR ARG ILE ASP TRP LYS ARG LEU ALA VAL
SEQRES 4 A 525 ALA ASP ALA SER GLU ARG ALA GLY LEU SER GLY ARG TRP
SEQRES 5 A 525 LEU VAL VAL VAL PRO GLU ASP ARG SER ALA GLU ALA ALA
SEQRES 6 A 525 PRO VAL LEU ALA ALA LEU SER GLY ALA GLY ALA ASP PRO
SEQRES 7 A 525 VAL GLN LEU ASP VAL SER PRO LEU GLY ASP ARG GLN ARG
SEQRES 8 A 525 LEU ALA ALA THR LEU GLY GLU ALA LEU ALA ALA ALA GLY
SEQRES 9 A 525 GLY ALA VAL ASP GLY VAL LEU SER LEU LEU ALA TRP ASP
SEQRES 10 A 525 GLU SER ALA HIS PRO GLY HIS PRO ALA PRO PHE THR ARG
SEQRES 11 A 525 GLY THR GLY ALA THR LEU THR LEU VAL GLN ALA LEU GLU
SEQRES 12 A 525 ASP ALA GLY VAL ALA ALA PRO LEU TRP CYS VAL THR HIS
SEQRES 13 A 525 GLY ALA VAL SER VAL GLY ARG ALA ASP HIS VAL THR SER
SEQRES 14 A 525 PRO ALA GLN ALA MET VAL TRP GLY MET GLY ARG VAL ALA
SEQRES 15 A 525 ALA LEU GLU HIS PRO GLU ARG TRP GLY GLY LEU ILE ASP
SEQRES 16 A 525 LEU PRO SER ASP ALA ASP ARG ALA ALA LEU ASP ARG MET
SEQRES 17 A 525 THR THR VAL LEU ALA GLY GLY THR GLY GLU ASP GLN VAL
SEQRES 18 A 525 ALA VAL ARG ALA SER GLY LEU LEU ALA ARG ARG LEU VAL
SEQRES 19 A 525 ARG ALA SER LEU PRO ALA HIS GLY THR ALA SER PRO TRP
SEQRES 20 A 525 TRP GLN ALA ASP GLY THR VAL LEU VAL THR GLY ALA GLU
SEQRES 21 A 525 GLU PRO ALA ALA ALA GLU ALA ALA ARG ARG LEU ALA ARG
SEQRES 22 A 525 ASP GLY ALA GLY HIS LEU LEU LEU HIS THR THR PRO SER
SEQRES 23 A 525 GLY SER GLU GLY ALA GLU GLY THR SER GLY ALA ALA GLU
SEQRES 24 A 525 ASP SER GLY LEU ALA GLY LEU VAL ALA GLU LEU ALA ASP
SEQRES 25 A 525 LEU GLY ALA THR ALA THR VAL VAL THR CYS ASP LEU THR
SEQRES 26 A 525 ASP ALA GLU ALA ALA ALA ARG LEU LEU ALA GLY VAL SER
SEQRES 27 A 525 ASP ALA HIS PRO LEU SER ALA VAL LEU HIS LEU PRO PRO
SEQRES 28 A 525 THR VAL ASP SER GLU PRO LEU ALA ALA THR ASP ALA ASP
SEQRES 29 A 525 ALA LEU ALA ARG VAL VAL THR ALA LYS ALA THR ALA ALA
SEQRES 30 A 525 LEU HIS LEU ASP ARG LEU LEU ARG GLU ALA ALA ALA ALA
SEQRES 31 A 525 GLY GLY ARG PRO PRO VAL LEU VAL LEU PHE SER SER VAL
SEQRES 32 A 525 ALA ALA ILE TRP GLY GLY ALA GLY GLN GLY ALA TYR ALA
SEQRES 33 A 525 ALA GLY THR ALA PHE LEU ASP ALA LEU ALA GLY GLN HIS
SEQRES 34 A 525 ARG ALA ASP GLY PRO THR VAL THR SER VAL ALA TRP SER
SEQRES 35 A 525 PRO TRP GLU GLY SER ARG VAL THR GLU GLY ALA THR GLY
SEQRES 36 A 525 GLU ARG LEU ARG ARG LEU GLY LEU ARG PRO LEU ALA PRO
SEQRES 37 A 525 ALA THR ALA LEU THR ALA LEU ASP THR ALA LEU GLY HIS
SEQRES 38 A 525 GLY ASP THR ALA VAL THR ILE ALA ASP VAL ASP TRP SER
SEQRES 39 A 525 SER PHE ALA PRO GLY PHE THR THR ALA ARG PRO GLY THR
SEQRES 40 A 525 LEU LEU ALA ASP LEU PRO GLU ALA ARG ARG ALA LEU ASP
SEQRES 41 A 525 GLU GLN GLN SER THR
SEQRES 1 B 525 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 525 LEU VAL PRO ARG GLY SER HIS MET GLY SER VAL GLN ASP
SEQRES 3 B 525 SER TRP ARG TYR ARG ILE ASP TRP LYS ARG LEU ALA VAL
SEQRES 4 B 525 ALA ASP ALA SER GLU ARG ALA GLY LEU SER GLY ARG TRP
SEQRES 5 B 525 LEU VAL VAL VAL PRO GLU ASP ARG SER ALA GLU ALA ALA
SEQRES 6 B 525 PRO VAL LEU ALA ALA LEU SER GLY ALA GLY ALA ASP PRO
SEQRES 7 B 525 VAL GLN LEU ASP VAL SER PRO LEU GLY ASP ARG GLN ARG
SEQRES 8 B 525 LEU ALA ALA THR LEU GLY GLU ALA LEU ALA ALA ALA GLY
SEQRES 9 B 525 GLY ALA VAL ASP GLY VAL LEU SER LEU LEU ALA TRP ASP
SEQRES 10 B 525 GLU SER ALA HIS PRO GLY HIS PRO ALA PRO PHE THR ARG
SEQRES 11 B 525 GLY THR GLY ALA THR LEU THR LEU VAL GLN ALA LEU GLU
SEQRES 12 B 525 ASP ALA GLY VAL ALA ALA PRO LEU TRP CYS VAL THR HIS
SEQRES 13 B 525 GLY ALA VAL SER VAL GLY ARG ALA ASP HIS VAL THR SER
SEQRES 14 B 525 PRO ALA GLN ALA MET VAL TRP GLY MET GLY ARG VAL ALA
SEQRES 15 B 525 ALA LEU GLU HIS PRO GLU ARG TRP GLY GLY LEU ILE ASP
SEQRES 16 B 525 LEU PRO SER ASP ALA ASP ARG ALA ALA LEU ASP ARG MET
SEQRES 17 B 525 THR THR VAL LEU ALA GLY GLY THR GLY GLU ASP GLN VAL
SEQRES 18 B 525 ALA VAL ARG ALA SER GLY LEU LEU ALA ARG ARG LEU VAL
SEQRES 19 B 525 ARG ALA SER LEU PRO ALA HIS GLY THR ALA SER PRO TRP
SEQRES 20 B 525 TRP GLN ALA ASP GLY THR VAL LEU VAL THR GLY ALA GLU
SEQRES 21 B 525 GLU PRO ALA ALA ALA GLU ALA ALA ARG ARG LEU ALA ARG
SEQRES 22 B 525 ASP GLY ALA GLY HIS LEU LEU LEU HIS THR THR PRO SER
SEQRES 23 B 525 GLY SER GLU GLY ALA GLU GLY THR SER GLY ALA ALA GLU
SEQRES 24 B 525 ASP SER GLY LEU ALA GLY LEU VAL ALA GLU LEU ALA ASP
SEQRES 25 B 525 LEU GLY ALA THR ALA THR VAL VAL THR CYS ASP LEU THR
SEQRES 26 B 525 ASP ALA GLU ALA ALA ALA ARG LEU LEU ALA GLY VAL SER
SEQRES 27 B 525 ASP ALA HIS PRO LEU SER ALA VAL LEU HIS LEU PRO PRO
SEQRES 28 B 525 THR VAL ASP SER GLU PRO LEU ALA ALA THR ASP ALA ASP
SEQRES 29 B 525 ALA LEU ALA ARG VAL VAL THR ALA LYS ALA THR ALA ALA
SEQRES 30 B 525 LEU HIS LEU ASP ARG LEU LEU ARG GLU ALA ALA ALA ALA
SEQRES 31 B 525 GLY GLY ARG PRO PRO VAL LEU VAL LEU PHE SER SER VAL
SEQRES 32 B 525 ALA ALA ILE TRP GLY GLY ALA GLY GLN GLY ALA TYR ALA
SEQRES 33 B 525 ALA GLY THR ALA PHE LEU ASP ALA LEU ALA GLY GLN HIS
SEQRES 34 B 525 ARG ALA ASP GLY PRO THR VAL THR SER VAL ALA TRP SER
SEQRES 35 B 525 PRO TRP GLU GLY SER ARG VAL THR GLU GLY ALA THR GLY
SEQRES 36 B 525 GLU ARG LEU ARG ARG LEU GLY LEU ARG PRO LEU ALA PRO
SEQRES 37 B 525 ALA THR ALA LEU THR ALA LEU ASP THR ALA LEU GLY HIS
SEQRES 38 B 525 GLY ASP THR ALA VAL THR ILE ALA ASP VAL ASP TRP SER
SEQRES 39 B 525 SER PHE ALA PRO GLY PHE THR THR ALA ARG PRO GLY THR
SEQRES 40 B 525 LEU LEU ALA ASP LEU PRO GLU ALA ARG ARG ALA LEU ASP
SEQRES 41 B 525 GLU GLN GLN SER THR
SEQRES 1 C 525 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 525 LEU VAL PRO ARG GLY SER HIS MET GLY SER VAL GLN ASP
SEQRES 3 C 525 SER TRP ARG TYR ARG ILE ASP TRP LYS ARG LEU ALA VAL
SEQRES 4 C 525 ALA ASP ALA SER GLU ARG ALA GLY LEU SER GLY ARG TRP
SEQRES 5 C 525 LEU VAL VAL VAL PRO GLU ASP ARG SER ALA GLU ALA ALA
SEQRES 6 C 525 PRO VAL LEU ALA ALA LEU SER GLY ALA GLY ALA ASP PRO
SEQRES 7 C 525 VAL GLN LEU ASP VAL SER PRO LEU GLY ASP ARG GLN ARG
SEQRES 8 C 525 LEU ALA ALA THR LEU GLY GLU ALA LEU ALA ALA ALA GLY
SEQRES 9 C 525 GLY ALA VAL ASP GLY VAL LEU SER LEU LEU ALA TRP ASP
SEQRES 10 C 525 GLU SER ALA HIS PRO GLY HIS PRO ALA PRO PHE THR ARG
SEQRES 11 C 525 GLY THR GLY ALA THR LEU THR LEU VAL GLN ALA LEU GLU
SEQRES 12 C 525 ASP ALA GLY VAL ALA ALA PRO LEU TRP CYS VAL THR HIS
SEQRES 13 C 525 GLY ALA VAL SER VAL GLY ARG ALA ASP HIS VAL THR SER
SEQRES 14 C 525 PRO ALA GLN ALA MET VAL TRP GLY MET GLY ARG VAL ALA
SEQRES 15 C 525 ALA LEU GLU HIS PRO GLU ARG TRP GLY GLY LEU ILE ASP
SEQRES 16 C 525 LEU PRO SER ASP ALA ASP ARG ALA ALA LEU ASP ARG MET
SEQRES 17 C 525 THR THR VAL LEU ALA GLY GLY THR GLY GLU ASP GLN VAL
SEQRES 18 C 525 ALA VAL ARG ALA SER GLY LEU LEU ALA ARG ARG LEU VAL
SEQRES 19 C 525 ARG ALA SER LEU PRO ALA HIS GLY THR ALA SER PRO TRP
SEQRES 20 C 525 TRP GLN ALA ASP GLY THR VAL LEU VAL THR GLY ALA GLU
SEQRES 21 C 525 GLU PRO ALA ALA ALA GLU ALA ALA ARG ARG LEU ALA ARG
SEQRES 22 C 525 ASP GLY ALA GLY HIS LEU LEU LEU HIS THR THR PRO SER
SEQRES 23 C 525 GLY SER GLU GLY ALA GLU GLY THR SER GLY ALA ALA GLU
SEQRES 24 C 525 ASP SER GLY LEU ALA GLY LEU VAL ALA GLU LEU ALA ASP
SEQRES 25 C 525 LEU GLY ALA THR ALA THR VAL VAL THR CYS ASP LEU THR
SEQRES 26 C 525 ASP ALA GLU ALA ALA ALA ARG LEU LEU ALA GLY VAL SER
SEQRES 27 C 525 ASP ALA HIS PRO LEU SER ALA VAL LEU HIS LEU PRO PRO
SEQRES 28 C 525 THR VAL ASP SER GLU PRO LEU ALA ALA THR ASP ALA ASP
SEQRES 29 C 525 ALA LEU ALA ARG VAL VAL THR ALA LYS ALA THR ALA ALA
SEQRES 30 C 525 LEU HIS LEU ASP ARG LEU LEU ARG GLU ALA ALA ALA ALA
SEQRES 31 C 525 GLY GLY ARG PRO PRO VAL LEU VAL LEU PHE SER SER VAL
SEQRES 32 C 525 ALA ALA ILE TRP GLY GLY ALA GLY GLN GLY ALA TYR ALA
SEQRES 33 C 525 ALA GLY THR ALA PHE LEU ASP ALA LEU ALA GLY GLN HIS
SEQRES 34 C 525 ARG ALA ASP GLY PRO THR VAL THR SER VAL ALA TRP SER
SEQRES 35 C 525 PRO TRP GLU GLY SER ARG VAL THR GLU GLY ALA THR GLY
SEQRES 36 C 525 GLU ARG LEU ARG ARG LEU GLY LEU ARG PRO LEU ALA PRO
SEQRES 37 C 525 ALA THR ALA LEU THR ALA LEU ASP THR ALA LEU GLY HIS
SEQRES 38 C 525 GLY ASP THR ALA VAL THR ILE ALA ASP VAL ASP TRP SER
SEQRES 39 C 525 SER PHE ALA PRO GLY PHE THR THR ALA ARG PRO GLY THR
SEQRES 40 C 525 LEU LEU ALA ASP LEU PRO GLU ALA ARG ARG ALA LEU ASP
SEQRES 41 C 525 GLU GLN GLN SER THR
SEQRES 1 D 525 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 525 LEU VAL PRO ARG GLY SER HIS MET GLY SER VAL GLN ASP
SEQRES 3 D 525 SER TRP ARG TYR ARG ILE ASP TRP LYS ARG LEU ALA VAL
SEQRES 4 D 525 ALA ASP ALA SER GLU ARG ALA GLY LEU SER GLY ARG TRP
SEQRES 5 D 525 LEU VAL VAL VAL PRO GLU ASP ARG SER ALA GLU ALA ALA
SEQRES 6 D 525 PRO VAL LEU ALA ALA LEU SER GLY ALA GLY ALA ASP PRO
SEQRES 7 D 525 VAL GLN LEU ASP VAL SER PRO LEU GLY ASP ARG GLN ARG
SEQRES 8 D 525 LEU ALA ALA THR LEU GLY GLU ALA LEU ALA ALA ALA GLY
SEQRES 9 D 525 GLY ALA VAL ASP GLY VAL LEU SER LEU LEU ALA TRP ASP
SEQRES 10 D 525 GLU SER ALA HIS PRO GLY HIS PRO ALA PRO PHE THR ARG
SEQRES 11 D 525 GLY THR GLY ALA THR LEU THR LEU VAL GLN ALA LEU GLU
SEQRES 12 D 525 ASP ALA GLY VAL ALA ALA PRO LEU TRP CYS VAL THR HIS
SEQRES 13 D 525 GLY ALA VAL SER VAL GLY ARG ALA ASP HIS VAL THR SER
SEQRES 14 D 525 PRO ALA GLN ALA MET VAL TRP GLY MET GLY ARG VAL ALA
SEQRES 15 D 525 ALA LEU GLU HIS PRO GLU ARG TRP GLY GLY LEU ILE ASP
SEQRES 16 D 525 LEU PRO SER ASP ALA ASP ARG ALA ALA LEU ASP ARG MET
SEQRES 17 D 525 THR THR VAL LEU ALA GLY GLY THR GLY GLU ASP GLN VAL
SEQRES 18 D 525 ALA VAL ARG ALA SER GLY LEU LEU ALA ARG ARG LEU VAL
SEQRES 19 D 525 ARG ALA SER LEU PRO ALA HIS GLY THR ALA SER PRO TRP
SEQRES 20 D 525 TRP GLN ALA ASP GLY THR VAL LEU VAL THR GLY ALA GLU
SEQRES 21 D 525 GLU PRO ALA ALA ALA GLU ALA ALA ARG ARG LEU ALA ARG
SEQRES 22 D 525 ASP GLY ALA GLY HIS LEU LEU LEU HIS THR THR PRO SER
SEQRES 23 D 525 GLY SER GLU GLY ALA GLU GLY THR SER GLY ALA ALA GLU
SEQRES 24 D 525 ASP SER GLY LEU ALA GLY LEU VAL ALA GLU LEU ALA ASP
SEQRES 25 D 525 LEU GLY ALA THR ALA THR VAL VAL THR CYS ASP LEU THR
SEQRES 26 D 525 ASP ALA GLU ALA ALA ALA ARG LEU LEU ALA GLY VAL SER
SEQRES 27 D 525 ASP ALA HIS PRO LEU SER ALA VAL LEU HIS LEU PRO PRO
SEQRES 28 D 525 THR VAL ASP SER GLU PRO LEU ALA ALA THR ASP ALA ASP
SEQRES 29 D 525 ALA LEU ALA ARG VAL VAL THR ALA LYS ALA THR ALA ALA
SEQRES 30 D 525 LEU HIS LEU ASP ARG LEU LEU ARG GLU ALA ALA ALA ALA
SEQRES 31 D 525 GLY GLY ARG PRO PRO VAL LEU VAL LEU PHE SER SER VAL
SEQRES 32 D 525 ALA ALA ILE TRP GLY GLY ALA GLY GLN GLY ALA TYR ALA
SEQRES 33 D 525 ALA GLY THR ALA PHE LEU ASP ALA LEU ALA GLY GLN HIS
SEQRES 34 D 525 ARG ALA ASP GLY PRO THR VAL THR SER VAL ALA TRP SER
SEQRES 35 D 525 PRO TRP GLU GLY SER ARG VAL THR GLU GLY ALA THR GLY
SEQRES 36 D 525 GLU ARG LEU ARG ARG LEU GLY LEU ARG PRO LEU ALA PRO
SEQRES 37 D 525 ALA THR ALA LEU THR ALA LEU ASP THR ALA LEU GLY HIS
SEQRES 38 D 525 GLY ASP THR ALA VAL THR ILE ALA ASP VAL ASP TRP SER
SEQRES 39 D 525 SER PHE ALA PRO GLY PHE THR THR ALA ARG PRO GLY THR
SEQRES 40 D 525 LEU LEU ALA ASP LEU PRO GLU ALA ARG ARG ALA LEU ASP
SEQRES 41 D 525 GLU GLN GLN SER THR
FORMUL 5 HOH *343(H2 O)
HELIX 1 1 GLN A 4 SER A 6 5 3
HELIX 2 2 ASP A 38 SER A 40 5 3
HELIX 3 3 ALA A 43 ALA A 53 1 11
HELIX 4 4 ASP A 67 ALA A 82 1 16
HELIX 5 5 LEU A 93 ASP A 96 5 4
HELIX 6 6 THR A 108 ALA A 124 1 17
HELIX 7 7 SER A 148 HIS A 165 1 18
HELIX 8 8 ASP A 180 ALA A 192 1 13
HELIX 9 9 GLU A 240 GLY A 254 1 15
HELIX 10 10 LEU A 282 GLY A 293 1 12
HELIX 11 11 ASP A 305 GLY A 315 1 11
HELIX 12 12 ASP A 341 ALA A 366 1 26
HELIX 13 13 GLN A 391 GLY A 406 1 16
HELIX 14 14 SER A 426 GLU A 430 5 5
HELIX 15 15 GLY A 431 LEU A 440 1 10
HELIX 16 16 ALA A 446 GLY A 461 1 16
HELIX 17 17 ASP A 471 THR A 481 1 11
HELIX 18 18 LEU A 491 ARG A 496 1 6
HELIX 19 19 ASP B 38 SER B 40 5 3
HELIX 20 20 ALA B 43 ALA B 53 1 11
HELIX 21 21 ASP B 67 ALA B 82 1 16
HELIX 22 22 LEU B 93 ASP B 96 5 4
HELIX 23 23 THR B 108 ALA B 124 1 17
HELIX 24 24 GLN B 151 HIS B 165 1 15
HELIX 25 25 ASP B 180 GLY B 193 1 14
HELIX 26 26 GLU B 240 ASP B 253 1 14
HELIX 27 27 GLY B 284 GLY B 293 1 10
HELIX 28 28 ASP B 305 GLY B 315 1 11
HELIX 29 29 ASP B 341 ARG B 364 1 24
HELIX 30 30 GLN B 391 GLY B 406 1 16
HELIX 31 31 SER B 426 GLU B 430 5 5
HELIX 32 32 GLU B 435 LEU B 440 1 6
HELIX 33 33 ALA B 446 HIS B 460 1 15
HELIX 34 34 ASP B 471 THR B 480 1 10
HELIX 35 35 VAL C 3 SER C 6 5 4
HELIX 36 36 ASP C 38 GLU C 42 5 5
HELIX 37 37 ALA C 43 GLY C 52 1 10
HELIX 38 38 ASP C 67 ALA C 81 1 15
HELIX 39 39 LEU C 93 ASP C 96 5 4
HELIX 40 40 THR C 108 GLY C 125 1 18
HELIX 41 41 SER C 148 HIS C 165 1 18
HELIX 42 42 ASP C 180 GLY C 193 1 14
HELIX 43 43 GLU C 240 GLY C 254 1 15
HELIX 44 44 LEU C 282 GLY C 293 1 12
HELIX 45 45 ASP C 305 GLY C 315 1 11
HELIX 46 46 ASP C 341 ARG C 364 1 24
HELIX 47 47 GLN C 391 GLY C 406 1 16
HELIX 48 48 SER C 426 THR C 429 5 4
HELIX 49 49 GLU C 430 GLY C 441 1 12
HELIX 50 50 ALA C 446 HIS C 460 1 15
HELIX 51 51 ASP C 471 THR C 480 1 10
HELIX 52 52 ALA D 43 ALA D 53 1 11
HELIX 53 53 ASP D 67 ALA D 81 1 15
HELIX 54 54 LEU D 93 ASP D 96 5 4
HELIX 55 55 THR D 108 ALA D 124 1 17
HELIX 56 56 SER D 148 ALA D 150 5 3
HELIX 57 57 GLN D 151 HIS D 165 1 15
HELIX 58 58 ASP D 180 ALA D 192 1 13
HELIX 59 59 GLU D 240 GLY D 254 1 15
HELIX 60 60 LEU D 282 GLY D 293 1 12
HELIX 61 61 ASP D 305 GLY D 315 1 11
HELIX 62 62 PRO D 336 THR D 340 5 5
HELIX 63 63 ASP D 341 ALA D 367 1 27
HELIX 64 64 ALA D 383 ILE D 385 5 3
HELIX 65 65 GLN D 391 GLY D 406 1 16
HELIX 66 66 GLU D 430 GLY D 441 1 12
HELIX 67 67 ALA D 446 HIS D 460 1 15
HELIX 68 68 ASP D 471 THR D 480 1 10
SHEET 1 A15 ASP A 56 VAL A 62 0
SHEET 2 A15 ARG A 30 PRO A 36 1 N TRP A 31 O VAL A 58
SHEET 3 A15 GLY A 88 SER A 91 1 O LEU A 90 N LEU A 32
SHEET 4 A15 LEU A 130 HIS A 135 1 O TRP A 131 N VAL A 89
SHEET 5 A15 TRP A 169 LEU A 175 1 O LEU A 175 N THR A 134
SHEET 6 A15 GLN A 199 ARG A 203 1 O VAL A 202 N ASP A 174
SHEET 7 A15 GLY A 206 ARG A 214 -1 O LEU A 208 N ALA A 201
SHEET 8 A15 ARG A 8 ARG A 15 -1 N LYS A 14 O ALA A 209
SHEET 9 A15 ALA A 464 ILE A 467 -1 O THR A 466 N TYR A 9
SHEET 10 A15 THR A 414 TRP A 420 1 N ALA A 419 O VAL A 465
SHEET 11 A15 VAL A 375 SER A 381 1 N LEU A 378 O VAL A 418
SHEET 12 A15 LEU A 322 HIS A 327 1 N VAL A 325 O VAL A 375
SHEET 13 A15 THR A 232 VAL A 235 1 N LEU A 234 O LEU A 326
SHEET 14 A15 HIS A 257 THR A 262 1 O HIS A 261 N VAL A 235
SHEET 15 A15 THR A 295 THR A 300 1 O VAL A 299 N LEU A 260
SHEET 1 B15 ASP B 56 VAL B 62 0
SHEET 2 B15 ARG B 30 PRO B 36 1 N VAL B 33 O VAL B 58
SHEET 3 B15 GLY B 88 SER B 91 1 O LEU B 90 N LEU B 32
SHEET 4 B15 LEU B 130 HIS B 135 1 O TRP B 131 N SER B 91
SHEET 5 B15 TRP B 169 LEU B 175 1 O LEU B 175 N THR B 134
SHEET 6 B15 GLN B 199 ARG B 203 1 O VAL B 202 N ASP B 174
SHEET 7 B15 GLY B 206 ARG B 214 -1 O LEU B 208 N ALA B 201
SHEET 8 B15 ARG B 8 ARG B 15 -1 N LYS B 14 O ALA B 209
SHEET 9 B15 ALA B 464 ILE B 467 -1 O THR B 466 N TYR B 9
SHEET 10 B15 THR B 414 TRP B 420 1 N ALA B 419 O VAL B 465
SHEET 11 B15 VAL B 375 SER B 381 1 N SER B 380 O VAL B 418
SHEET 12 B15 LEU B 322 HIS B 327 1 N VAL B 325 O VAL B 377
SHEET 13 B15 THR B 232 VAL B 235 1 N THR B 232 O SER B 323
SHEET 14 B15 HIS B 257 THR B 262 1 O LEU B 259 N VAL B 233
SHEET 15 B15 THR B 295 THR B 300 1 O THR B 297 N LEU B 260
SHEET 1 C15 ASP C 56 VAL C 62 0
SHEET 2 C15 ARG C 30 PRO C 36 1 N VAL C 33 O LEU C 60
SHEET 3 C15 GLY C 88 SER C 91 1 O LEU C 90 N LEU C 32
SHEET 4 C15 LEU C 130 HIS C 135 1 O TRP C 131 N SER C 91
SHEET 5 C15 TRP C 169 LEU C 175 1 O LEU C 175 N THR C 134
SHEET 6 C15 GLN C 199 ARG C 203 1 O VAL C 200 N ASP C 174
SHEET 7 C15 GLY C 206 ARG C 214 -1 O LEU C 208 N ALA C 201
SHEET 8 C15 ARG C 8 ARG C 15 -1 N ASP C 12 O ARG C 211
SHEET 9 C15 ALA C 464 ILE C 467 -1 O THR C 466 N TYR C 9
SHEET 10 C15 THR C 414 TRP C 420 1 N ALA C 419 O VAL C 465
SHEET 11 C15 VAL C 375 SER C 381 1 N LEU C 378 O THR C 416
SHEET 12 C15 LEU C 322 HIS C 327 1 N HIS C 327 O VAL C 377
SHEET 13 C15 THR C 232 VAL C 235 1 N LEU C 234 O LEU C 326
SHEET 14 C15 HIS C 257 THR C 262 1 O LEU C 259 N VAL C 235
SHEET 15 C15 THR C 295 THR C 300 1 O THR C 297 N LEU C 260
SHEET 1 D15 ASP D 56 VAL D 62 0
SHEET 2 D15 ARG D 30 PRO D 36 1 N VAL D 35 O VAL D 62
SHEET 3 D15 GLY D 88 SER D 91 1 O LEU D 90 N LEU D 32
SHEET 4 D15 LEU D 130 HIS D 135 1 O TRP D 131 N SER D 91
SHEET 5 D15 TRP D 169 LEU D 175 1 O LEU D 175 N THR D 134
SHEET 6 D15 GLN D 199 ARG D 203 1 O VAL D 202 N ASP D 174
SHEET 7 D15 GLY D 206 ARG D 214 -1 O GLY D 206 N ARG D 203
SHEET 8 D15 ARG D 8 ARG D 15 -1 N ASP D 12 O ARG D 211
SHEET 9 D15 ALA D 464 ILE D 467 -1 O THR D 466 N TYR D 9
SHEET 10 D15 THR D 414 TRP D 420 1 N ALA D 419 O VAL D 465
SHEET 11 D15 VAL D 375 SER D 381 1 N LEU D 378 O VAL D 418
SHEET 12 D15 LEU D 322 HIS D 327 1 N VAL D 325 O VAL D 377
SHEET 13 D15 THR D 232 VAL D 235 1 N THR D 232 O SER D 323
SHEET 14 D15 HIS D 257 THR D 262 1 O HIS D 257 N VAL D 233
SHEET 15 D15 THR D 295 THR D 300 1 O THR D 297 N LEU D 260
CISPEP 1 ALA A 105 PRO A 106 0 17.25
CISPEP 2 GLY A 412 PRO A 413 0 -7.10
CISPEP 3 ALA B 105 PRO B 106 0 9.55
CISPEP 4 GLY B 412 PRO B 413 0 -1.51
CISPEP 5 GLY B 434 GLU B 435 0 12.81
CISPEP 6 ALA C 105 PRO C 106 0 16.44
CISPEP 7 GLY C 412 PRO C 413 0 -4.74
CISPEP 8 ALA D 105 PRO D 106 0 13.59
CISPEP 9 GLY D 412 PRO D 413 0 3.92
CRYST1 79.636 150.088 86.868 90.00 105.12 90.00 P 1 21 1 8
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 0.012557 0.000000 0.003392 0.00000
SCALE2 0.000000 0.006663 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011924 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
