HEADER CELL INVASION 02-JUN-14 3WVO
TITLE CRYSTAL STRUCTURE OF THERMOBIFIDA FUSCA CSE1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CRISPR-ASSOCIATED PROTEIN, CSE1 FAMILY;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOBIFIDA FUSCA;
SOURCE 3 ORGANISM_TAXID: 269800;
SOURCE 4 STRAIN: YX;
SOURCE 5 GENE: TFU_1600;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CRISPR, CASCADE, CASA, CELL INVASION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.A.YUAN,M.TAY
REVDAT 3 08-NOV-23 3WVO 1 REMARK
REVDAT 2 24-AUG-22 3WVO 1 JRNL SEQADV
REVDAT 1 14-JAN-15 3WVO 0
JRNL AUTH M.TAY,S.LIU,Y.A.YUAN
JRNL TITL CRYSTAL STRUCTURE OF THERMOBIFIDA FUSCA CSE1 REVEALS TARGET
JRNL TITL 2 DNA BINDING SITE.
JRNL REF PROTEIN SCI. V. 24 236 2015
JRNL REFN ESSN 1469-896X
JRNL PMID 25420472
JRNL DOI 10.1002/PRO.2609
REMARK 2
REMARK 2 RESOLUTION. 3.31 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 3.31
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.4
REMARK 3 NUMBER OF REFLECTIONS : 35245
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) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1873
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) : 3.31
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.40
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1275
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 43.83
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE SET COUNT : 57
REMARK 3 BIN FREE R VALUE : 0.2590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12756
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 28
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 73.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.93000
REMARK 3 B22 (A**2) : -0.91000
REMARK 3 B33 (A**2) : -1.89000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.73000
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): 0.442
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.299
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 40.337
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13068 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17793 ; 1.797 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1619 ; 7.441 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 637 ;33.862 ;23.250
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2064 ;22.662 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 125 ;22.607 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1932 ; 0.112 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10202 ; 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): 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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 3
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 545 B 1 545 654 0.08 0.05
REMARK 3 2 A 1 546 C 1 546 661 0.09 0.05
REMARK 3 3 B 1 546 C 1 546 654 0.09 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
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 547
REMARK 3 ORIGIN FOR THE GROUP (A): 46.5104 27.0841 50.4153
REMARK 3 T TENSOR
REMARK 3 T11: 0.0754 T22: 0.1350
REMARK 3 T33: 0.1962 T12: 0.0067
REMARK 3 T13: 0.1020 T23: -0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 2.4066 L22: 2.2453
REMARK 3 L33: 1.7941 L12: 1.3124
REMARK 3 L13: -0.0145 L23: 0.5881
REMARK 3 S TENSOR
REMARK 3 S11: 0.0412 S12: 0.0605 S13: 0.0858
REMARK 3 S21: -0.2325 S22: 0.1100 S23: -0.3593
REMARK 3 S31: -0.2421 S32: 0.1482 S33: -0.1512
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 546
REMARK 3 ORIGIN FOR THE GROUP (A): 45.7304 34.0872 88.6593
REMARK 3 T TENSOR
REMARK 3 T11: 0.2463 T22: 0.3325
REMARK 3 T33: 0.2061 T12: -0.2133
REMARK 3 T13: -0.0831 T23: 0.1043
REMARK 3 L TENSOR
REMARK 3 L11: 0.9580 L22: 4.1470
REMARK 3 L33: 2.8181 L12: 0.4762
REMARK 3 L13: 0.3387 L23: -0.5542
REMARK 3 S TENSOR
REMARK 3 S11: 0.3693 S12: -0.2294 S13: -0.1726
REMARK 3 S21: 0.6050 S22: -0.1172 S23: -0.1155
REMARK 3 S31: 0.2072 S32: -0.2480 S33: -0.2521
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 1 C 546
REMARK 3 ORIGIN FOR THE GROUP (A): -0.6995 -0.6932 19.2732
REMARK 3 T TENSOR
REMARK 3 T11: 0.0795 T22: 0.0787
REMARK 3 T33: 0.0297 T12: 0.0657
REMARK 3 T13: -0.0308 T23: -0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 3.1134 L22: 1.4908
REMARK 3 L33: 2.6729 L12: 1.2313
REMARK 3 L13: 0.3764 L23: 0.3321
REMARK 3 S TENSOR
REMARK 3 S11: 0.0743 S12: 0.0924 S13: -0.1641
REMARK 3 S21: 0.0790 S22: 0.0945 S23: 0.0230
REMARK 3 S31: 0.3714 S32: 0.1568 S33: -0.1688
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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 3WVO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000096850.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-FEB-13
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 : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : NULL
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 : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35245
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 4H3T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, CACODYLATE, POTASSIUM
REMARK 280 CHLORIDE, MAGNESIUM SULPHATE, PH 7.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 103.65200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 66.26450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 103.65200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 66.26450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 3080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 GLY A 513
REMARK 465 ARG A 514
REMARK 465 VAL A 515
REMARK 465 ILE A 516
REMARK 465 GLU A 548
REMARK 465 GLN A 549
REMARK 465 THR A 550
REMARK 465 GLY A 551
REMARK 465 GLU A 552
REMARK 465 ALA A 553
REMARK 465 ALA A 554
REMARK 465 SER A 555
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 ILE B 516
REMARK 465 LYS B 517
REMARK 465 GLY B 518
REMARK 465 LYS B 519
REMARK 465 SER B 547
REMARK 465 GLU B 548
REMARK 465 GLN B 549
REMARK 465 THR B 550
REMARK 465 GLY B 551
REMARK 465 GLU B 552
REMARK 465 ALA B 553
REMARK 465 ALA B 554
REMARK 465 SER B 555
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 VAL C 515
REMARK 465 ILE C 516
REMARK 465 LYS C 517
REMARK 465 GLY C 518
REMARK 465 LYS C 519
REMARK 465 ASN C 520
REMARK 465 SER C 547
REMARK 465 GLU C 548
REMARK 465 GLN C 549
REMARK 465 THR C 550
REMARK 465 GLY C 551
REMARK 465 GLU C 552
REMARK 465 ALA C 553
REMARK 465 ALA C 554
REMARK 465 SER C 555
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 NH2 ARG C 103 O GLN C 237 1.93
REMARK 500 NH2 ARG B 103 O GLN B 237 1.99
REMARK 500 OD2 ASP B 169 NZ LYS B 174 2.08
REMARK 500 OD2 ASP C 46 NH1 ARG C 160 2.10
REMARK 500 O THR C 170 NZ LYS C 174 2.13
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 PRO A 48 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500 PRO A 109 C - N - CA ANGL. DEV. = 12.7 DEGREES
REMARK 500 PRO A 137 C - N - CA ANGL. DEV. = 10.2 DEGREES
REMARK 500 LEU A 203 CB - CA - C ANGL. DEV. = -13.0 DEGREES
REMARK 500 PRO C 137 C - N - CA ANGL. DEV. = 11.6 DEGREES
REMARK 500 VAL C 280 CB - CA - C ANGL. DEV. = -12.1 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 PRO A 6 34.31 -97.91
REMARK 500 TRP A 15 -20.21 -152.15
REMARK 500 ASP A 22 41.57 -74.79
REMARK 500 THR A 24 136.15 -34.03
REMARK 500 ALA A 37 -46.73 -24.21
REMARK 500 ASP A 46 -19.28 -45.60
REMARK 500 VAL A 47 129.92 -170.39
REMARK 500 ALA A 65 -8.29 -56.95
REMARK 500 GLN A 86 113.10 -36.73
REMARK 500 THR A 111 58.16 -92.39
REMARK 500 PHE A 114 19.42 56.40
REMARK 500 GLU A 140 -32.80 -35.40
REMARK 500 PHE A 143 45.44 73.81
REMARK 500 ARG A 146 107.73 -34.50
REMARK 500 SER A 171 48.76 -92.15
REMARK 500 ALA A 183 71.92 -52.32
REMARK 500 LYS A 184 106.46 -51.11
REMARK 500 TRP A 235 2.89 -66.55
REMARK 500 THR A 241 -163.36 -113.99
REMARK 500 GLN A 252 71.62 -103.96
REMARK 500 TYR A 261 8.86 -65.08
REMARK 500 ALA A 274 -40.38 -23.96
REMARK 500 ALA A 344 -130.89 38.76
REMARK 500 GLU A 345 -73.63 14.13
REMARK 500 ASP A 374 27.48 -79.72
REMARK 500 GLN A 390 6.81 54.47
REMARK 500 ASP A 412 -105.94 -79.65
REMARK 500 ALA A 480 -70.13 -51.25
REMARK 500 ASN A 520 -79.37 -59.62
REMARK 500 THR A 521 -2.43 -55.79
REMARK 500 LEU A 542 63.81 -112.19
REMARK 500 THR A 546 -51.78 14.42
REMARK 500 ALA B 5 74.65 -103.43
REMARK 500 TRP B 15 -11.29 -175.31
REMARK 500 ASP B 22 44.24 -70.06
REMARK 500 THR B 24 131.57 -39.76
REMARK 500 ASP B 46 -9.88 -57.21
REMARK 500 VAL B 47 140.02 -170.50
REMARK 500 ASP B 82 83.37 -63.77
REMARK 500 GLU B 83 -33.55 -36.60
REMARK 500 GLU B 85 -61.07 -107.06
REMARK 500 GLN B 86 89.46 -10.89
REMARK 500 THR B 111 59.65 -103.81
REMARK 500 PHE B 114 20.70 44.87
REMARK 500 ASN B 124 70.01 56.43
REMARK 500 GLU B 140 -39.52 -38.87
REMARK 500 ARG B 148 51.55 -110.36
REMARK 500 LYS B 184 96.44 -52.38
REMARK 500 GLN B 191 25.22 -143.57
REMARK 500 PRO B 229 -30.66 -35.33
REMARK 500
REMARK 500 THIS ENTRY HAS 85 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 ALA A 344 GLU A 345 147.09
REMARK 500 GLY C 172 ILE C 173 141.06
REMARK 500 LEU C 199 GLY C 200 148.08
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3WVO A 1 555 UNP Q47PI4 Q47PI4_THEFY 1 555
DBREF 3WVO B 1 555 UNP Q47PI4 Q47PI4_THEFY 1 555
DBREF 3WVO C 1 555 UNP Q47PI4 Q47PI4_THEFY 1 555
SEQADV 3WVO GLY A -2 UNP Q47PI4 EXPRESSION TAG
SEQADV 3WVO SER A -1 UNP Q47PI4 EXPRESSION TAG
SEQADV 3WVO HIS A 0 UNP Q47PI4 EXPRESSION TAG
SEQADV 3WVO GLY B -2 UNP Q47PI4 EXPRESSION TAG
SEQADV 3WVO SER B -1 UNP Q47PI4 EXPRESSION TAG
SEQADV 3WVO HIS B 0 UNP Q47PI4 EXPRESSION TAG
SEQADV 3WVO GLY C -2 UNP Q47PI4 EXPRESSION TAG
SEQADV 3WVO SER C -1 UNP Q47PI4 EXPRESSION TAG
SEQADV 3WVO HIS C 0 UNP Q47PI4 EXPRESSION TAG
SEQRES 1 A 558 GLY SER HIS MET THR THR ASP ALA PRO SER PHE ASN LEU
SEQRES 2 A 558 ILE THR GLN PRO TRP LEU PRO VAL GLN TYR ARG ASP GLY
SEQRES 3 A 558 THR GLU LYS GLU LEU SER LEU LEU GLU VAL PHE LYS GLN
SEQRES 4 A 558 ALA PRO LEU LEU ARG ARG LEU VAL GLY ASP VAL PRO THR
SEQRES 5 A 558 GLN GLU PHE ALA LEU LEU ARG LEU LEU LEU ALA ILE LEU
SEQRES 6 A 558 HIS ASP ALA ILE GLY GLY PRO GLU ASP SER ASP GLU TRP
SEQRES 7 A 558 ALA GLU LEU TRP THR GLN ASP GLU ALA GLU GLN GLN LEU
SEQRES 8 A 558 PRO PHE ASP CYS ILE ALA SER TYR LEU GLU GLN TYR TYR
SEQRES 9 A 558 HIS ARG PHE ASP LEU LEU HIS PRO THR THR PRO PHE PHE
SEQRES 10 A 558 GLN VAL ALA ASP LEU HIS THR GLN LYS ASN ASP VAL PHE
SEQRES 11 A 558 SER LEU ASP ARG ILE VAL ALA ASP VAL PRO ASN GLY GLU
SEQRES 12 A 558 LEU PHE PHE THR MET ARG ALA ARG GLY VAL ASP ARG LEU
SEQRES 13 A 558 SER PHE ALA GLU ALA ALA ARG TRP LEU VAL HIS ALA HIS
SEQRES 14 A 558 ALA TYR ASP THR SER GLY ILE LYS SER GLY ALA VAL GLY
SEQRES 15 A 558 ASP PRO ARG ALA LYS GLY GLY LYS GLY TYR PRO GLN GLY
SEQRES 16 A 558 VAL SER TRP ALA GLY ASN LEU GLY GLY ILE LEU VAL GLU
SEQRES 17 A 558 GLY ALA ASN LEU TYR GLU THR LEU LEU LEU ASN LEU VAL
SEQRES 18 A 558 ALA PHE ASP THR ASP ASN LEU ILE VAL THR PRO GLU ASP
SEQRES 19 A 558 ARG PRO ALA TRP ARG GLN PRO PRO THR THR ALA ALA PRO
SEQRES 20 A 558 ALA ASP ASP GLU GLU LEU ALA GLN ARG PRO TYR GLY LEU
SEQRES 21 A 558 CYS ASP LEU TYR THR TRP GLN SER ARG ARG ILE ARG LEU
SEQRES 22 A 558 HIS TYR ASP ALA ASP GLY VAL TYR GLY VAL LEU LEU ALA
SEQRES 23 A 558 TYR GLY ASP PRO LEU ALA PRO HIS ASN LYS HIS ASN HIS
SEQRES 24 A 558 GLU PRO MET THR ALA TRP ARG ARG SER PRO ALA GLN GLU
SEQRES 25 A 558 LYS LYS LEU LYS LYS PRO GLN VAL TYR LEU PRO ARG GLU
SEQRES 26 A 558 HIS ASP PRO THR ARG SER ALA TRP ARG GLY LEU GLY ALA
SEQRES 27 A 558 LEU VAL ALA GLY GLU ALA SER GLY ALA GLU GLN ARG GLY
SEQRES 28 A 558 GLU ALA ALA ALA ILE VAL ARG PRO ARG ILE LEU ASP TRP
SEQRES 29 A 558 VAL ALA ARG LEU VAL ASN GLU GLY PHE LEU PRO GLU ASP
SEQRES 30 A 558 TYR PHE ILE ARG THR ARG LEU ILE GLY VAL SER TYR GLY
SEQRES 31 A 558 THR GLN GLN ALA VAL ILE ASP GLU ILE VAL ASP ASP HIS
SEQRES 32 A 558 VAL ALA MET ALA VAL VAL LEU LEU HIS GLU ARG ASP SER
SEQRES 33 A 558 GLY LEU GLY ARG THR ALA ILE LYS ALA VAL GLU ASP ALA
SEQRES 34 A 558 GLU LYS ALA VAL THR VAL LEU GLY GLY LEU ALA ALA ASP
SEQRES 35 A 558 LEU ALA LYS ALA ALA GLY ALA ASP PRO GLU THR PRO ARG
SEQRES 36 A 558 ALA ALA ALA ARG ASP ARG GLY PHE GLY MET LEU ASP GLY
SEQRES 37 A 558 PRO PHE ARG THR TRP LEU ALA THR LEU ALA PRO GLY THR
SEQRES 38 A 558 ASP ALA THR GLU ARG ARG ARG ALA TRP GLN GLN LYS ALA
SEQRES 39 A 558 HIS ARG ILE ILE SER ASP LEU GLY ARG GLN LEU VAL ALA
SEQRES 40 A 558 GLU ALA GLY GLU ALA ALA TRP ASN GLY ARG VAL ILE LYS
SEQRES 41 A 558 GLY LYS ASN THR ASP VAL TRP LEU ASN ALA SER ARG ALA
SEQRES 42 A 558 ASP LEU LYS PHE ARG ALA GLU LEU LYS LYS GLU LEU PRO
SEQRES 43 A 558 MET ALA THR SER GLU GLN THR GLY GLU ALA ALA SER
SEQRES 1 B 558 GLY SER HIS MET THR THR ASP ALA PRO SER PHE ASN LEU
SEQRES 2 B 558 ILE THR GLN PRO TRP LEU PRO VAL GLN TYR ARG ASP GLY
SEQRES 3 B 558 THR GLU LYS GLU LEU SER LEU LEU GLU VAL PHE LYS GLN
SEQRES 4 B 558 ALA PRO LEU LEU ARG ARG LEU VAL GLY ASP VAL PRO THR
SEQRES 5 B 558 GLN GLU PHE ALA LEU LEU ARG LEU LEU LEU ALA ILE LEU
SEQRES 6 B 558 HIS ASP ALA ILE GLY GLY PRO GLU ASP SER ASP GLU TRP
SEQRES 7 B 558 ALA GLU LEU TRP THR GLN ASP GLU ALA GLU GLN GLN LEU
SEQRES 8 B 558 PRO PHE ASP CYS ILE ALA SER TYR LEU GLU GLN TYR TYR
SEQRES 9 B 558 HIS ARG PHE ASP LEU LEU HIS PRO THR THR PRO PHE PHE
SEQRES 10 B 558 GLN VAL ALA ASP LEU HIS THR GLN LYS ASN ASP VAL PHE
SEQRES 11 B 558 SER LEU ASP ARG ILE VAL ALA ASP VAL PRO ASN GLY GLU
SEQRES 12 B 558 LEU PHE PHE THR MET ARG ALA ARG GLY VAL ASP ARG LEU
SEQRES 13 B 558 SER PHE ALA GLU ALA ALA ARG TRP LEU VAL HIS ALA HIS
SEQRES 14 B 558 ALA TYR ASP THR SER GLY ILE LYS SER GLY ALA VAL GLY
SEQRES 15 B 558 ASP PRO ARG ALA LYS GLY GLY LYS GLY TYR PRO GLN GLY
SEQRES 16 B 558 VAL SER TRP ALA GLY ASN LEU GLY GLY ILE LEU VAL GLU
SEQRES 17 B 558 GLY ALA ASN LEU TYR GLU THR LEU LEU LEU ASN LEU VAL
SEQRES 18 B 558 ALA PHE ASP THR ASP ASN LEU ILE VAL THR PRO GLU ASP
SEQRES 19 B 558 ARG PRO ALA TRP ARG GLN PRO PRO THR THR ALA ALA PRO
SEQRES 20 B 558 ALA ASP ASP GLU GLU LEU ALA GLN ARG PRO TYR GLY LEU
SEQRES 21 B 558 CYS ASP LEU TYR THR TRP GLN SER ARG ARG ILE ARG LEU
SEQRES 22 B 558 HIS TYR ASP ALA ASP GLY VAL TYR GLY VAL LEU LEU ALA
SEQRES 23 B 558 TYR GLY ASP PRO LEU ALA PRO HIS ASN LYS HIS ASN HIS
SEQRES 24 B 558 GLU PRO MET THR ALA TRP ARG ARG SER PRO ALA GLN GLU
SEQRES 25 B 558 LYS LYS LEU LYS LYS PRO GLN VAL TYR LEU PRO ARG GLU
SEQRES 26 B 558 HIS ASP PRO THR ARG SER ALA TRP ARG GLY LEU GLY ALA
SEQRES 27 B 558 LEU VAL ALA GLY GLU ALA SER GLY ALA GLU GLN ARG GLY
SEQRES 28 B 558 GLU ALA ALA ALA ILE VAL ARG PRO ARG ILE LEU ASP TRP
SEQRES 29 B 558 VAL ALA ARG LEU VAL ASN GLU GLY PHE LEU PRO GLU ASP
SEQRES 30 B 558 TYR PHE ILE ARG THR ARG LEU ILE GLY VAL SER TYR GLY
SEQRES 31 B 558 THR GLN GLN ALA VAL ILE ASP GLU ILE VAL ASP ASP HIS
SEQRES 32 B 558 VAL ALA MET ALA VAL VAL LEU LEU HIS GLU ARG ASP SER
SEQRES 33 B 558 GLY LEU GLY ARG THR ALA ILE LYS ALA VAL GLU ASP ALA
SEQRES 34 B 558 GLU LYS ALA VAL THR VAL LEU GLY GLY LEU ALA ALA ASP
SEQRES 35 B 558 LEU ALA LYS ALA ALA GLY ALA ASP PRO GLU THR PRO ARG
SEQRES 36 B 558 ALA ALA ALA ARG ASP ARG GLY PHE GLY MET LEU ASP GLY
SEQRES 37 B 558 PRO PHE ARG THR TRP LEU ALA THR LEU ALA PRO GLY THR
SEQRES 38 B 558 ASP ALA THR GLU ARG ARG ARG ALA TRP GLN GLN LYS ALA
SEQRES 39 B 558 HIS ARG ILE ILE SER ASP LEU GLY ARG GLN LEU VAL ALA
SEQRES 40 B 558 GLU ALA GLY GLU ALA ALA TRP ASN GLY ARG VAL ILE LYS
SEQRES 41 B 558 GLY LYS ASN THR ASP VAL TRP LEU ASN ALA SER ARG ALA
SEQRES 42 B 558 ASP LEU LYS PHE ARG ALA GLU LEU LYS LYS GLU LEU PRO
SEQRES 43 B 558 MET ALA THR SER GLU GLN THR GLY GLU ALA ALA SER
SEQRES 1 C 558 GLY SER HIS MET THR THR ASP ALA PRO SER PHE ASN LEU
SEQRES 2 C 558 ILE THR GLN PRO TRP LEU PRO VAL GLN TYR ARG ASP GLY
SEQRES 3 C 558 THR GLU LYS GLU LEU SER LEU LEU GLU VAL PHE LYS GLN
SEQRES 4 C 558 ALA PRO LEU LEU ARG ARG LEU VAL GLY ASP VAL PRO THR
SEQRES 5 C 558 GLN GLU PHE ALA LEU LEU ARG LEU LEU LEU ALA ILE LEU
SEQRES 6 C 558 HIS ASP ALA ILE GLY GLY PRO GLU ASP SER ASP GLU TRP
SEQRES 7 C 558 ALA GLU LEU TRP THR GLN ASP GLU ALA GLU GLN GLN LEU
SEQRES 8 C 558 PRO PHE ASP CYS ILE ALA SER TYR LEU GLU GLN TYR TYR
SEQRES 9 C 558 HIS ARG PHE ASP LEU LEU HIS PRO THR THR PRO PHE PHE
SEQRES 10 C 558 GLN VAL ALA ASP LEU HIS THR GLN LYS ASN ASP VAL PHE
SEQRES 11 C 558 SER LEU ASP ARG ILE VAL ALA ASP VAL PRO ASN GLY GLU
SEQRES 12 C 558 LEU PHE PHE THR MET ARG ALA ARG GLY VAL ASP ARG LEU
SEQRES 13 C 558 SER PHE ALA GLU ALA ALA ARG TRP LEU VAL HIS ALA HIS
SEQRES 14 C 558 ALA TYR ASP THR SER GLY ILE LYS SER GLY ALA VAL GLY
SEQRES 15 C 558 ASP PRO ARG ALA LYS GLY GLY LYS GLY TYR PRO GLN GLY
SEQRES 16 C 558 VAL SER TRP ALA GLY ASN LEU GLY GLY ILE LEU VAL GLU
SEQRES 17 C 558 GLY ALA ASN LEU TYR GLU THR LEU LEU LEU ASN LEU VAL
SEQRES 18 C 558 ALA PHE ASP THR ASP ASN LEU ILE VAL THR PRO GLU ASP
SEQRES 19 C 558 ARG PRO ALA TRP ARG GLN PRO PRO THR THR ALA ALA PRO
SEQRES 20 C 558 ALA ASP ASP GLU GLU LEU ALA GLN ARG PRO TYR GLY LEU
SEQRES 21 C 558 CYS ASP LEU TYR THR TRP GLN SER ARG ARG ILE ARG LEU
SEQRES 22 C 558 HIS TYR ASP ALA ASP GLY VAL TYR GLY VAL LEU LEU ALA
SEQRES 23 C 558 TYR GLY ASP PRO LEU ALA PRO HIS ASN LYS HIS ASN HIS
SEQRES 24 C 558 GLU PRO MET THR ALA TRP ARG ARG SER PRO ALA GLN GLU
SEQRES 25 C 558 LYS LYS LEU LYS LYS PRO GLN VAL TYR LEU PRO ARG GLU
SEQRES 26 C 558 HIS ASP PRO THR ARG SER ALA TRP ARG GLY LEU GLY ALA
SEQRES 27 C 558 LEU VAL ALA GLY GLU ALA SER GLY ALA GLU GLN ARG GLY
SEQRES 28 C 558 GLU ALA ALA ALA ILE VAL ARG PRO ARG ILE LEU ASP TRP
SEQRES 29 C 558 VAL ALA ARG LEU VAL ASN GLU GLY PHE LEU PRO GLU ASP
SEQRES 30 C 558 TYR PHE ILE ARG THR ARG LEU ILE GLY VAL SER TYR GLY
SEQRES 31 C 558 THR GLN GLN ALA VAL ILE ASP GLU ILE VAL ASP ASP HIS
SEQRES 32 C 558 VAL ALA MET ALA VAL VAL LEU LEU HIS GLU ARG ASP SER
SEQRES 33 C 558 GLY LEU GLY ARG THR ALA ILE LYS ALA VAL GLU ASP ALA
SEQRES 34 C 558 GLU LYS ALA VAL THR VAL LEU GLY GLY LEU ALA ALA ASP
SEQRES 35 C 558 LEU ALA LYS ALA ALA GLY ALA ASP PRO GLU THR PRO ARG
SEQRES 36 C 558 ALA ALA ALA ARG ASP ARG GLY PHE GLY MET LEU ASP GLY
SEQRES 37 C 558 PRO PHE ARG THR TRP LEU ALA THR LEU ALA PRO GLY THR
SEQRES 38 C 558 ASP ALA THR GLU ARG ARG ARG ALA TRP GLN GLN LYS ALA
SEQRES 39 C 558 HIS ARG ILE ILE SER ASP LEU GLY ARG GLN LEU VAL ALA
SEQRES 40 C 558 GLU ALA GLY GLU ALA ALA TRP ASN GLY ARG VAL ILE LYS
SEQRES 41 C 558 GLY LYS ASN THR ASP VAL TRP LEU ASN ALA SER ARG ALA
SEQRES 42 C 558 ASP LEU LYS PHE ARG ALA GLU LEU LYS LYS GLU LEU PRO
SEQRES 43 C 558 MET ALA THR SER GLU GLN THR GLY GLU ALA ALA SER
FORMUL 4 HOH *28(H2 O)
HELIX 1 1 SER A 29 ALA A 37 1 9
HELIX 2 2 VAL A 47 GLY A 67 1 21
HELIX 3 3 ASP A 71 GLU A 77 1 7
HELIX 4 4 PRO A 89 TYR A 100 1 12
HELIX 5 5 TYR A 101 PHE A 104 5 4
HELIX 6 6 SER A 128 ILE A 132 5 5
HELIX 7 7 ASN A 138 PHE A 143 1 6
HELIX 8 8 SER A 154 TYR A 168 1 15
HELIX 9 9 ALA A 183 GLY A 185 5 3
HELIX 10 10 SER A 194 LEU A 199 5 6
HELIX 11 11 ASN A 208 ASN A 216 1 9
HELIX 12 12 PRO A 233 GLN A 237 5 5
HELIX 13 13 ASP A 246 GLN A 252 1 7
HELIX 14 14 GLY A 256 TYR A 261 1 6
HELIX 15 15 SER A 305 LYS A 313 1 9
HELIX 16 16 SER A 328 ARG A 331 5 4
HELIX 17 17 GLY A 332 GLY A 339 1 8
HELIX 18 18 GLY A 343 ARG A 347 5 5
HELIX 19 19 ALA A 350 ARG A 355 1 6
HELIX 20 20 PRO A 356 GLU A 368 1 13
HELIX 21 21 THR A 388 ALA A 391 5 4
HELIX 22 22 VAL A 405 GLU A 410 1 6
HELIX 23 23 GLY A 414 ALA A 443 1 30
HELIX 24 24 PRO A 448 ALA A 472 1 25
HELIX 25 25 ASP A 479 ALA A 510 1 32
HELIX 26 26 LYS A 519 LEU A 542 1 24
HELIX 27 27 SER B 29 ALA B 37 1 9
HELIX 28 28 VAL B 47 ILE B 66 1 20
HELIX 29 29 ASP B 71 GLU B 77 1 7
HELIX 30 30 PRO B 89 TYR B 100 1 12
HELIX 31 31 TYR B 101 PHE B 104 5 4
HELIX 32 32 SER B 128 ILE B 132 5 5
HELIX 33 33 ASN B 138 PHE B 143 1 6
HELIX 34 34 PHE B 155 TYR B 168 1 14
HELIX 35 35 ALA B 183 GLY B 185 5 3
HELIX 36 36 SER B 194 LEU B 199 5 6
HELIX 37 37 ASN B 208 ASN B 216 1 9
HELIX 38 38 PRO B 233 GLN B 237 5 5
HELIX 39 39 ASP B 246 ALA B 251 1 6
HELIX 40 40 GLY B 256 TYR B 261 1 6
HELIX 41 41 SER B 305 LYS B 313 1 9
HELIX 42 42 SER B 328 ARG B 331 5 4
HELIX 43 43 GLY B 332 GLY B 339 1 8
HELIX 44 44 GLY B 343 GLY B 348 1 6
HELIX 45 45 ALA B 350 ARG B 355 1 6
HELIX 46 46 PRO B 356 GLU B 368 1 13
HELIX 47 47 THR B 388 ALA B 391 5 4
HELIX 48 48 VAL B 405 GLU B 410 1 6
HELIX 49 49 GLY B 414 GLY B 445 1 32
HELIX 50 50 PRO B 448 ALA B 472 1 25
HELIX 51 51 ASP B 479 ALA B 509 1 31
HELIX 52 52 THR B 521 LEU B 542 1 22
HELIX 53 53 SER C 29 ALA C 37 1 9
HELIX 54 54 VAL C 47 ALA C 65 1 19
HELIX 55 55 ASP C 71 GLU C 77 1 7
HELIX 56 56 PRO C 89 TYR C 100 1 12
HELIX 57 57 TYR C 101 PHE C 104 5 4
HELIX 58 58 SER C 128 ILE C 132 5 5
HELIX 59 59 ASN C 138 PHE C 142 5 5
HELIX 60 60 SER C 154 TYR C 168 1 15
HELIX 61 61 SER C 194 LEU C 199 5 6
HELIX 62 62 ASN C 208 ASN C 216 1 9
HELIX 63 63 PRO C 233 GLN C 237 5 5
HELIX 64 64 ASP C 246 ALA C 251 1 6
HELIX 65 65 GLY C 256 TYR C 261 1 6
HELIX 66 66 SER C 305 LYS C 313 1 9
HELIX 67 67 SER C 328 ARG C 331 5 4
HELIX 68 68 GLY C 332 GLY C 339 1 8
HELIX 69 69 GLY C 343 ARG C 347 5 5
HELIX 70 70 ALA C 350 ARG C 355 1 6
HELIX 71 71 PRO C 356 GLU C 368 1 13
HELIX 72 72 THR C 388 ALA C 391 5 4
HELIX 73 73 VAL C 405 GLU C 410 1 6
HELIX 74 74 GLY C 414 ALA C 444 1 31
HELIX 75 75 PRO C 448 LEU C 474 1 27
HELIX 76 76 ASP C 479 GLY C 513 1 35
HELIX 77 77 ASP C 522 LEU C 542 1 21
SHEET 1 A 3 GLU A 25 LEU A 28 0
SHEET 2 A 3 LEU A 16 TYR A 20 -1 N VAL A 18 O LYS A 26
SHEET 3 A 3 LEU A 40 LEU A 43 -1 O ARG A 41 N GLN A 19
SHEET 1 B 2 LYS A 174 SER A 175 0
SHEET 2 B 2 LYS A 187 GLY A 188 -1 O GLY A 188 N LYS A 174
SHEET 1 C 3 GLY A 201 GLU A 205 0
SHEET 2 C 3 PHE A 376 TYR A 386 -1 O ARG A 378 N GLU A 205
SHEET 3 C 3 ILE A 393 ALA A 404 -1 O ASP A 399 N LEU A 381
SHEET 1 D 2 ARG A 266 TYR A 272 0
SHEET 2 D 2 VAL A 277 TYR A 284 -1 O GLY A 279 N HIS A 271
SHEET 1 E 2 TRP A 302 ARG A 304 0
SHEET 2 E 2 TYR A 318 PRO A 320 -1 O LEU A 319 N ARG A 303
SHEET 1 F 3 GLU B 25 LEU B 28 0
SHEET 2 F 3 LEU B 16 TYR B 20 -1 N VAL B 18 O LYS B 26
SHEET 3 F 3 LEU B 40 LEU B 43 -1 O ARG B 41 N GLN B 19
SHEET 1 G 3 LEU B 153 SER B 154 0
SHEET 2 G 3 GLY B 276 TYR B 284 -1 O VAL B 277 N LEU B 153
SHEET 3 G 3 ARG B 266 TYR B 272 -1 N ARG B 267 O ALA B 283
SHEET 1 H 2 LYS B 174 SER B 175 0
SHEET 2 H 2 LYS B 187 GLY B 188 -1 O GLY B 188 N LYS B 174
SHEET 1 I 3 GLY B 201 GLU B 205 0
SHEET 2 I 3 PHE B 376 TYR B 386 -1 O ARG B 378 N GLU B 205
SHEET 3 I 3 ILE B 393 ALA B 404 -1 O GLU B 395 N SER B 385
SHEET 1 J 2 TRP B 302 ARG B 304 0
SHEET 2 J 2 TYR B 318 PRO B 320 -1 O LEU B 319 N ARG B 303
SHEET 1 K 3 GLU C 25 LEU C 28 0
SHEET 2 K 3 LEU C 16 TYR C 20 -1 N VAL C 18 O LYS C 26
SHEET 3 K 3 LEU C 40 LEU C 43 -1 O ARG C 42 N GLN C 19
SHEET 1 L 2 LYS C 174 SER C 175 0
SHEET 2 L 2 LYS C 187 GLY C 188 -1 O GLY C 188 N LYS C 174
SHEET 1 M 3 GLY C 201 GLU C 205 0
SHEET 2 M 3 PHE C 376 TYR C 386 -1 O ARG C 378 N GLU C 205
SHEET 3 M 3 ILE C 393 ALA C 404 -1 O GLU C 395 N SER C 385
SHEET 1 N 2 ARG C 266 TYR C 272 0
SHEET 2 N 2 VAL C 277 TYR C 284 -1 O GLY C 279 N HIS C 271
SHEET 1 O 2 TRP C 302 ARG C 304 0
SHEET 2 O 2 TYR C 318 PRO C 320 -1 O LEU C 319 N ARG C 303
CISPEP 1 ARG A 253 PRO A 254 0 2.04
CISPEP 2 ARG B 253 PRO B 254 0 -5.13
CISPEP 3 ARG C 253 PRO C 254 0 4.30
CRYST1 207.304 132.529 102.962 90.00 93.75 90.00 C 1 2 1 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 0.004824 0.000000 0.000317 0.00000
SCALE2 0.000000 0.007546 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009733 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
