HEADER HYDROLASE 11-JUN-12 4FJ6
TITLE CRYSTAL STRUCTURE OF A GLYCOSIDE HYDROLASE FAMILY 33, CANDIDATE
TITLE 2 SIALIDASE (BDI_2946) FROM PARABACTEROIDES DISTASONIS ATCC 8503 AT
TITLE 3 1.90 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOSIDE HYDROLASE FAMILY 33, CANDIDATE SIALIDASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PARABACTEROIDES DISTASONIS;
SOURCE 3 ORGANISM_TAXID: 435591;
SOURCE 4 STRAIN: ATCC 8503;
SOURCE 5 GENE: BDI_2946;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: PB1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS BACTERIAL NEURAMINIDASE REPEAT, INTRAMOLECULAR TRANS-SIALIDASE, A
KEYWDS 2 CARBOHYDRATE BINDING DOMAIN, STRUCTURAL GENOMICS, JOINT CENTER FOR
KEYWDS 3 STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-
KEYWDS 4 BIOLOGY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 5 01-FEB-23 4FJ6 1 REMARK SEQADV LINK
REVDAT 4 24-JAN-18 4FJ6 1 JRNL
REVDAT 3 15-NOV-17 4FJ6 1 REMARK
REVDAT 2 01-AUG-12 4FJ6 1 AUTHOR
REVDAT 1 25-JUL-12 4FJ6 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF A GLYCOSIDE HYDROLASE FAMILY 33,
JRNL TITL 2 CANDIDATE SIALIDASE (BDI_2946) FROM PARABACTEROIDES
JRNL TITL 3 DISTASONIS ATCC 8503 AT 1.90 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 209495
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) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 10526
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 14788
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE SET COUNT : 785
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16160
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 178
REMARK 3 SOLVENT ATOMS : 2000
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.77
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.21000
REMARK 3 B22 (A**2) : 0.21000
REMARK 3 B33 (A**2) : -0.31000
REMARK 3 B12 (A**2) : 0.10000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.155
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.144
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.116
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.394
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 16905 ; 0.007 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 11325 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 23016 ; 1.531 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 27804 ; 0.999 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2155 ; 4.873 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 733 ;35.349 ;24.748
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2928 ;10.521 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 96 ;10.873 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2612 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 18667 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3221 ; 0.001 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 22 A 539 6
REMARK 3 1 B 22 B 539 6
REMARK 3 1 C 22 C 539 6
REMARK 3 1 D 22 D 539 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 1 A (A): 6506 ; 0.200 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 B (A): 6506 ; 0.220 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 C (A): 6506 ; 0.240 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 D (A): 6506 ; 0.200 ; 5.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 6506 ; 1.720 ;10.000
REMARK 3 LOOSE THERMAL 1 B (A**2): 6506 ; 1.850 ;10.000
REMARK 3 LOOSE THERMAL 1 C (A**2): 6506 ; 1.800 ;10.000
REMARK 3 LOOSE THERMAL 1 D (A**2): 6506 ; 2.070 ;10.000
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 22 A 540
REMARK 3 ORIGIN FOR THE GROUP (A): 99.6640 24.2080 275.7830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1073 T22: 0.0458
REMARK 3 T33: 0.0664 T12: 0.0349
REMARK 3 T13: -0.0388 T23: -0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 0.4293 L22: 0.1685
REMARK 3 L33: 0.3873 L12: -0.0865
REMARK 3 L13: 0.1786 L23: -0.0981
REMARK 3 S TENSOR
REMARK 3 S11: -0.0269 S12: -0.0622 S13: 0.0009
REMARK 3 S21: 0.0292 S22: 0.0637 S23: 0.0224
REMARK 3 S31: 0.0156 S32: -0.0427 S33: -0.0368
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 21 B 540
REMARK 3 ORIGIN FOR THE GROUP (A): 120.5090 27.8030 238.1000
REMARK 3 T TENSOR
REMARK 3 T11: 0.1092 T22: 0.0705
REMARK 3 T33: 0.0651 T12: 0.0260
REMARK 3 T13: -0.0197 T23: -0.0300
REMARK 3 L TENSOR
REMARK 3 L11: 0.1987 L22: 0.1324
REMARK 3 L33: 0.4798 L12: 0.1244
REMARK 3 L13: -0.0876 L23: -0.0024
REMARK 3 S TENSOR
REMARK 3 S11: -0.0309 S12: -0.0123 S13: 0.0329
REMARK 3 S21: -0.0730 S22: 0.0189 S23: 0.0040
REMARK 3 S31: 0.0374 S32: 0.1091 S33: 0.0120
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 21 C 539
REMARK 3 ORIGIN FOR THE GROUP (A): 135.4930 -20.5910 277.8870
REMARK 3 T TENSOR
REMARK 3 T11: 0.0833 T22: 0.0447
REMARK 3 T33: 0.0971 T12: 0.0272
REMARK 3 T13: -0.0205 T23: -0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 0.1242 L22: 0.5615
REMARK 3 L33: 0.6711 L12: 0.1516
REMARK 3 L13: 0.2352 L23: 0.0634
REMARK 3 S TENSOR
REMARK 3 S11: 0.0321 S12: 0.0111 S13: -0.0462
REMARK 3 S21: -0.0868 S22: 0.0096 S23: -0.0555
REMARK 3 S31: 0.0843 S32: -0.0019 S33: -0.0416
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 20 D 540
REMARK 3 ORIGIN FOR THE GROUP (A): 142.8180 -0.8550 315.6580
REMARK 3 T TENSOR
REMARK 3 T11: 0.0442 T22: 0.1037
REMARK 3 T33: 0.0676 T12: -0.0101
REMARK 3 T13: -0.0005 T23: 0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 0.1639 L22: 0.4549
REMARK 3 L33: 0.3712 L12: 0.1951
REMARK 3 L13: 0.0657 L23: 0.0256
REMARK 3 S TENSOR
REMARK 3 S11: 0.0473 S12: -0.0553 S13: -0.0168
REMARK 3 S21: 0.0047 S22: -0.0617 S23: -0.0108
REMARK 3 S31: -0.0041 S32: -0.0078 S33: 0.0143
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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. ATOM RECORD CONTAINS SUM OF TLS AND
REMARK 3 RESIDUAL B FACTORS. 3. ANISOU RECORD CONTAINS SUM OF TLS AND
REMARK 3 RESIDUAL U FACTORS. 4. WATERS WERE EXCLUDED FROM AUTOMATIC TLS
REMARK 3 ASSIGNMENT. 5. A MET-INHIBITION PROTOCOL WAS USED FOR
REMARK 3 SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE
REMARK 3 OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO
REMARK 3 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 6. PHOSPHATE IONS (PO4) AND GLYCEROL (GOL)
REMARK 3 MOLECULES FROM THE CRYSTALLIZATION/CRYOPROTECTION SOLUTION ARE
REMARK 3 MODELED. 7. CHLORIDE (CL) IONS FROM PROTEIN BUFFER HAVE BEEN
REMARK 3 MODELED.
REMARK 4
REMARK 4 4FJ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1000072964.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 10.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97922,0.91837,0.97871
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111) BENT
REMARK 200 OPTICS : FLAT MIRROR (VERTICAL FOCUSING);
REMARK 200 SINGLE CRYSTAL SI(111) BENT
REMARK 200 MONOCHROMATOR (HORIZONTAL
REMARK 200 FOCUSING)
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE DECEMBER 29, 2011
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 209534
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 29.773
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.61900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELX, SHARP, SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LITHIUM SULFATE, 1.2M SODIUM
REMARK 280 DIHYDROGEN PHOSPHATE, 0.8M DI-POTASSIUM HYDROGEN PHOSPHATE, 0.1M
REMARK 280 GLYCINE PH 10.5, VAPOR DIFFUSION,SITTING DROP,NANODROP,
REMARK 280 TEMPERATURE 277K, VAPOR DIFFUSION, SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 85.86900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 49.57649
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 81.26200
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 85.86900
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 49.57649
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 81.26200
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 85.86900
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 49.57649
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 81.26200
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 99.15298
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 162.52400
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 99.15298
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 162.52400
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 99.15298
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 162.52400
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 300 REMARK: CRYSTAL PACKING ANALYSIS SUGGESTS THE ASSIGNMENT OF A DIMER
REMARK 300 AS THE SIGNIFICANT OLIGOMERIZATION STATE.
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: 6340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 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: 6850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 0
REMARK 465 ALA A 20
REMARK 465 ASP A 21
REMARK 465 GLN A 541
REMARK 465 GLY B 0
REMARK 465 ALA B 20
REMARK 465 GLN B 541
REMARK 465 GLY C 0
REMARK 465 ALA C 20
REMARK 465 HIS C 540
REMARK 465 GLN C 541
REMARK 465 GLY D 0
REMARK 465 GLN D 541
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 LYS A 455 CG CD CE NZ
REMARK 470 LYS A 473 CD CE NZ
REMARK 470 HIS A 540 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 136 CG CD CE NZ
REMARK 470 LYS B 381 CD CE NZ
REMARK 470 LYS B 473 CG CD CE NZ
REMARK 470 LYS C 86 CD CE NZ
REMARK 470 ASN C 172 CG OD1 ND2
REMARK 470 LYS C 381 CG CD CE NZ
REMARK 470 LYS C 455 CD CE NZ
REMARK 470 LYS C 473 CG CD CE NZ
REMARK 470 GLU C 493 CD OE1 OE2
REMARK 470 LYS D 473 CG CD CE NZ
REMARK 470 GLN D 536 CD OE1 NE2
REMARK 470 HIS D 540 CG ND1 CD2 CE1 NE2
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 ILE A 201 74.49 68.98
REMARK 500 GLU A 228 177.31 179.43
REMARK 500 LYS A 254 -112.91 31.03
REMARK 500 ASN A 264 29.93 -150.67
REMARK 500 HIS A 386 -107.67 -99.52
REMARK 500 THR A 394 -103.08 -125.80
REMARK 500 SER A 438 -56.01 -163.77
REMARK 500 VAL A 444 81.73 75.67
REMARK 500 HIS A 494 41.85 -101.41
REMARK 500 ILE B 201 74.48 69.18
REMARK 500 GLU B 228 168.50 178.96
REMARK 500 LYS B 229 97.35 -68.50
REMARK 500 LYS B 254 -118.91 36.88
REMARK 500 GLN B 255 50.00 -109.00
REMARK 500 ASN B 264 35.66 -148.48
REMARK 500 HIS B 386 -107.25 -99.96
REMARK 500 THR B 394 -101.74 -127.44
REMARK 500 SER B 438 -48.84 -162.24
REMARK 500 VAL B 444 83.06 70.51
REMARK 500 HIS B 494 41.90 -99.29
REMARK 500 ASP B 513 -158.36 -150.05
REMARK 500 ILE C 201 73.21 71.29
REMARK 500 GLU C 228 -179.91 -177.35
REMARK 500 LYS C 254 -114.11 29.76
REMARK 500 GLN C 255 57.74 -112.82
REMARK 500 ASN C 264 31.57 -145.29
REMARK 500 HIS C 386 -107.74 -103.25
REMARK 500 THR C 394 -99.31 -127.64
REMARK 500 SER C 438 -54.35 -165.82
REMARK 500 VAL C 444 81.64 76.78
REMARK 500 HIS C 494 43.22 -100.23
REMARK 500 ILE D 201 74.81 70.90
REMARK 500 LYS D 254 -116.67 31.98
REMARK 500 LYS D 254 -116.62 31.88
REMARK 500 GLN D 255 52.45 -109.28
REMARK 500 ASN D 264 34.58 -147.60
REMARK 500 HIS D 386 -105.33 -103.52
REMARK 500 THR D 394 -101.16 -125.87
REMARK 500 SER D 438 -56.35 -170.32
REMARK 500 VAL D 444 82.10 76.11
REMARK 500 HIS D 494 47.51 -102.39
REMARK 500 ALA D 526 143.42 -170.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 610
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 419091 RELATED DB: TARGETTRACK
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING
REMARK 999 ONLY A GLYCINE (0) FOLLOWED BY RESIDUES 20-541 OF THE TARGET
REMARK 999 SEQUENCE.
DBREF 4FJ6 A 20 541 UNP A6LG40 A6LG40_PARD8 20 541
DBREF 4FJ6 B 20 541 UNP A6LG40 A6LG40_PARD8 20 541
DBREF 4FJ6 C 20 541 UNP A6LG40 A6LG40_PARD8 20 541
DBREF 4FJ6 D 20 541 UNP A6LG40 A6LG40_PARD8 20 541
SEQADV 4FJ6 GLY A 0 UNP A6LG40 EXPRESSION TAG
SEQADV 4FJ6 GLY B 0 UNP A6LG40 EXPRESSION TAG
SEQADV 4FJ6 GLY C 0 UNP A6LG40 EXPRESSION TAG
SEQADV 4FJ6 GLY D 0 UNP A6LG40 EXPRESSION TAG
SEQRES 1 A 523 GLY ALA ASP SER ILE TYR VAL ARG GLU GLN GLN ILE PRO
SEQRES 2 A 523 ILE LEU ILE ASP ARG ILE ASP ASN VAL LEU TYR GLU MSE
SEQRES 3 A 523 ARG ILE PRO ALA GLN LYS GLY ASP VAL LEU ASN GLU ILE
SEQRES 4 A 523 THR ILE GLN ILE GLY ASP ASN VAL ASP LEU SER ASP ILE
SEQRES 5 A 523 GLN ALA ILE ARG LEU PHE TYR SER GLY VAL GLU ALA PRO
SEQRES 6 A 523 SER ARG LYS GLY GLU HIS PHE SER PRO VAL THR TYR ILE
SEQRES 7 A 523 SER SER HIS ILE PRO GLY ASN THR ARG LYS ALA LEU GLU
SEQRES 8 A 523 SER TYR SER VAL ARG GLN ASP GLU VAL THR ALA PRO LEU
SEQRES 9 A 523 SER ARG THR VAL LYS LEU THR SER LYS GLN PRO MSE LEU
SEQRES 10 A 523 LYS GLY ILE ASN TYR PHE TRP VAL SER ILE GLN MSE LYS
SEQRES 11 A 523 PRO GLU THR SER LEU LEU ALA LYS VAL ALA THR THR MSE
SEQRES 12 A 523 PRO ASN ALA GLN ILE ASN ASN LYS PRO ILE ASN ILE THR
SEQRES 13 A 523 TRP LYS GLY LYS VAL ASP GLU ARG HIS VAL GLY ILE GLY
SEQRES 14 A 523 VAL ARG GLN ALA GLY ASP ASP GLY SER ALA ALA PHE ARG
SEQRES 15 A 523 ILE PRO GLY LEU VAL THR THR ASN ASN GLY THR LEU LEU
SEQRES 16 A 523 GLY VAL TYR ASP ILE ARG TYR ASN SER SER VAL ASP LEU
SEQRES 17 A 523 GLN GLU LYS ILE ASP ILE GLY VAL SER ARG SER THR ASP
SEQRES 18 A 523 LYS GLY GLN THR TRP GLU PRO MSE ARG VAL ALA MSE THR
SEQRES 19 A 523 PHE LYS GLN THR ASP GLY LEU PRO HIS GLY GLN ASN GLY
SEQRES 20 A 523 VAL GLY ASP PRO SER ILE LEU VAL ASP GLU LYS THR ASN
SEQRES 21 A 523 THR ILE TRP VAL VAL ALA ALA TRP THR HIS GLY MSE GLY
SEQRES 22 A 523 ASN GLU ARG ALA TRP TRP ASN SER MSE PRO GLY MSE THR
SEQRES 23 A 523 PRO ASP GLU THR ALA GLN LEU MSE LEU VAL LYS SER GLU
SEQRES 24 A 523 ASP ASP GLY LYS THR TRP SER GLU PRO ILE ASN ILE THR
SEQRES 25 A 523 SER GLN VAL LYS ASP PRO SER TRP TYR PHE LEU LEU GLN
SEQRES 26 A 523 GLY PRO GLY ARG GLY ILE THR MSE GLN ASP GLY THR LEU
SEQRES 27 A 523 VAL PHE PRO ILE GLN PHE ILE ASP ALA THR ARG VAL PRO
SEQRES 28 A 523 ASN ALA GLY ILE MSE TYR SER LYS ASP ARG GLY LYS THR
SEQRES 29 A 523 TRP HIS LEU HIS ASN LEU ALA ARG THR ASN THR THR GLU
SEQRES 30 A 523 ALA GLN VAL ALA GLU VAL GLU PRO GLY VAL LEU MSE LEU
SEQRES 31 A 523 ASN MSE ARG ASP ASN ARG GLY GLY SER ARG ALA VAL ALA
SEQRES 32 A 523 THR THR LYS ASP LEU GLY LYS THR TRP THR GLU HIS PRO
SEQRES 33 A 523 SER SER ARG SER ALA LEU GLN GLU SER VAL CYS MSE ALA
SEQRES 34 A 523 SER LEU ILE LYS VAL ASN ALA LYS ASP ASN ILE THR GLY
SEQRES 35 A 523 LYS ASP LEU LEU LEU PHE SER ASN PRO ASN THR THR LYS
SEQRES 36 A 523 GLY ARG ASN HIS ILE THR ILE LYS ALA SER LEU ASP GLY
SEQRES 37 A 523 GLY LEU THR TRP PRO THR GLU HIS GLN VAL LEU LEU ASP
SEQRES 38 A 523 GLU ALA GLU GLY TRP GLY TYR SER CYS LEU SER MSE ILE
SEQRES 39 A 523 ASP LYS GLU THR VAL GLY ILE PHE TYR GLU SER SER VAL
SEQRES 40 A 523 ALA HIS MSE THR PHE GLN ALA VAL LYS LEU GLN ASP LEU
SEQRES 41 A 523 ILE HIS GLN
SEQRES 1 B 523 GLY ALA ASP SER ILE TYR VAL ARG GLU GLN GLN ILE PRO
SEQRES 2 B 523 ILE LEU ILE ASP ARG ILE ASP ASN VAL LEU TYR GLU MSE
SEQRES 3 B 523 ARG ILE PRO ALA GLN LYS GLY ASP VAL LEU ASN GLU ILE
SEQRES 4 B 523 THR ILE GLN ILE GLY ASP ASN VAL ASP LEU SER ASP ILE
SEQRES 5 B 523 GLN ALA ILE ARG LEU PHE TYR SER GLY VAL GLU ALA PRO
SEQRES 6 B 523 SER ARG LYS GLY GLU HIS PHE SER PRO VAL THR TYR ILE
SEQRES 7 B 523 SER SER HIS ILE PRO GLY ASN THR ARG LYS ALA LEU GLU
SEQRES 8 B 523 SER TYR SER VAL ARG GLN ASP GLU VAL THR ALA PRO LEU
SEQRES 9 B 523 SER ARG THR VAL LYS LEU THR SER LYS GLN PRO MSE LEU
SEQRES 10 B 523 LYS GLY ILE ASN TYR PHE TRP VAL SER ILE GLN MSE LYS
SEQRES 11 B 523 PRO GLU THR SER LEU LEU ALA LYS VAL ALA THR THR MSE
SEQRES 12 B 523 PRO ASN ALA GLN ILE ASN ASN LYS PRO ILE ASN ILE THR
SEQRES 13 B 523 TRP LYS GLY LYS VAL ASP GLU ARG HIS VAL GLY ILE GLY
SEQRES 14 B 523 VAL ARG GLN ALA GLY ASP ASP GLY SER ALA ALA PHE ARG
SEQRES 15 B 523 ILE PRO GLY LEU VAL THR THR ASN ASN GLY THR LEU LEU
SEQRES 16 B 523 GLY VAL TYR ASP ILE ARG TYR ASN SER SER VAL ASP LEU
SEQRES 17 B 523 GLN GLU LYS ILE ASP ILE GLY VAL SER ARG SER THR ASP
SEQRES 18 B 523 LYS GLY GLN THR TRP GLU PRO MSE ARG VAL ALA MSE THR
SEQRES 19 B 523 PHE LYS GLN THR ASP GLY LEU PRO HIS GLY GLN ASN GLY
SEQRES 20 B 523 VAL GLY ASP PRO SER ILE LEU VAL ASP GLU LYS THR ASN
SEQRES 21 B 523 THR ILE TRP VAL VAL ALA ALA TRP THR HIS GLY MSE GLY
SEQRES 22 B 523 ASN GLU ARG ALA TRP TRP ASN SER MSE PRO GLY MSE THR
SEQRES 23 B 523 PRO ASP GLU THR ALA GLN LEU MSE LEU VAL LYS SER GLU
SEQRES 24 B 523 ASP ASP GLY LYS THR TRP SER GLU PRO ILE ASN ILE THR
SEQRES 25 B 523 SER GLN VAL LYS ASP PRO SER TRP TYR PHE LEU LEU GLN
SEQRES 26 B 523 GLY PRO GLY ARG GLY ILE THR MSE GLN ASP GLY THR LEU
SEQRES 27 B 523 VAL PHE PRO ILE GLN PHE ILE ASP ALA THR ARG VAL PRO
SEQRES 28 B 523 ASN ALA GLY ILE MSE TYR SER LYS ASP ARG GLY LYS THR
SEQRES 29 B 523 TRP HIS LEU HIS ASN LEU ALA ARG THR ASN THR THR GLU
SEQRES 30 B 523 ALA GLN VAL ALA GLU VAL GLU PRO GLY VAL LEU MSE LEU
SEQRES 31 B 523 ASN MSE ARG ASP ASN ARG GLY GLY SER ARG ALA VAL ALA
SEQRES 32 B 523 THR THR LYS ASP LEU GLY LYS THR TRP THR GLU HIS PRO
SEQRES 33 B 523 SER SER ARG SER ALA LEU GLN GLU SER VAL CYS MSE ALA
SEQRES 34 B 523 SER LEU ILE LYS VAL ASN ALA LYS ASP ASN ILE THR GLY
SEQRES 35 B 523 LYS ASP LEU LEU LEU PHE SER ASN PRO ASN THR THR LYS
SEQRES 36 B 523 GLY ARG ASN HIS ILE THR ILE LYS ALA SER LEU ASP GLY
SEQRES 37 B 523 GLY LEU THR TRP PRO THR GLU HIS GLN VAL LEU LEU ASP
SEQRES 38 B 523 GLU ALA GLU GLY TRP GLY TYR SER CYS LEU SER MSE ILE
SEQRES 39 B 523 ASP LYS GLU THR VAL GLY ILE PHE TYR GLU SER SER VAL
SEQRES 40 B 523 ALA HIS MSE THR PHE GLN ALA VAL LYS LEU GLN ASP LEU
SEQRES 41 B 523 ILE HIS GLN
SEQRES 1 C 523 GLY ALA ASP SER ILE TYR VAL ARG GLU GLN GLN ILE PRO
SEQRES 2 C 523 ILE LEU ILE ASP ARG ILE ASP ASN VAL LEU TYR GLU MSE
SEQRES 3 C 523 ARG ILE PRO ALA GLN LYS GLY ASP VAL LEU ASN GLU ILE
SEQRES 4 C 523 THR ILE GLN ILE GLY ASP ASN VAL ASP LEU SER ASP ILE
SEQRES 5 C 523 GLN ALA ILE ARG LEU PHE TYR SER GLY VAL GLU ALA PRO
SEQRES 6 C 523 SER ARG LYS GLY GLU HIS PHE SER PRO VAL THR TYR ILE
SEQRES 7 C 523 SER SER HIS ILE PRO GLY ASN THR ARG LYS ALA LEU GLU
SEQRES 8 C 523 SER TYR SER VAL ARG GLN ASP GLU VAL THR ALA PRO LEU
SEQRES 9 C 523 SER ARG THR VAL LYS LEU THR SER LYS GLN PRO MSE LEU
SEQRES 10 C 523 LYS GLY ILE ASN TYR PHE TRP VAL SER ILE GLN MSE LYS
SEQRES 11 C 523 PRO GLU THR SER LEU LEU ALA LYS VAL ALA THR THR MSE
SEQRES 12 C 523 PRO ASN ALA GLN ILE ASN ASN LYS PRO ILE ASN ILE THR
SEQRES 13 C 523 TRP LYS GLY LYS VAL ASP GLU ARG HIS VAL GLY ILE GLY
SEQRES 14 C 523 VAL ARG GLN ALA GLY ASP ASP GLY SER ALA ALA PHE ARG
SEQRES 15 C 523 ILE PRO GLY LEU VAL THR THR ASN ASN GLY THR LEU LEU
SEQRES 16 C 523 GLY VAL TYR ASP ILE ARG TYR ASN SER SER VAL ASP LEU
SEQRES 17 C 523 GLN GLU LYS ILE ASP ILE GLY VAL SER ARG SER THR ASP
SEQRES 18 C 523 LYS GLY GLN THR TRP GLU PRO MSE ARG VAL ALA MSE THR
SEQRES 19 C 523 PHE LYS GLN THR ASP GLY LEU PRO HIS GLY GLN ASN GLY
SEQRES 20 C 523 VAL GLY ASP PRO SER ILE LEU VAL ASP GLU LYS THR ASN
SEQRES 21 C 523 THR ILE TRP VAL VAL ALA ALA TRP THR HIS GLY MSE GLY
SEQRES 22 C 523 ASN GLU ARG ALA TRP TRP ASN SER MSE PRO GLY MSE THR
SEQRES 23 C 523 PRO ASP GLU THR ALA GLN LEU MSE LEU VAL LYS SER GLU
SEQRES 24 C 523 ASP ASP GLY LYS THR TRP SER GLU PRO ILE ASN ILE THR
SEQRES 25 C 523 SER GLN VAL LYS ASP PRO SER TRP TYR PHE LEU LEU GLN
SEQRES 26 C 523 GLY PRO GLY ARG GLY ILE THR MSE GLN ASP GLY THR LEU
SEQRES 27 C 523 VAL PHE PRO ILE GLN PHE ILE ASP ALA THR ARG VAL PRO
SEQRES 28 C 523 ASN ALA GLY ILE MSE TYR SER LYS ASP ARG GLY LYS THR
SEQRES 29 C 523 TRP HIS LEU HIS ASN LEU ALA ARG THR ASN THR THR GLU
SEQRES 30 C 523 ALA GLN VAL ALA GLU VAL GLU PRO GLY VAL LEU MSE LEU
SEQRES 31 C 523 ASN MSE ARG ASP ASN ARG GLY GLY SER ARG ALA VAL ALA
SEQRES 32 C 523 THR THR LYS ASP LEU GLY LYS THR TRP THR GLU HIS PRO
SEQRES 33 C 523 SER SER ARG SER ALA LEU GLN GLU SER VAL CYS MSE ALA
SEQRES 34 C 523 SER LEU ILE LYS VAL ASN ALA LYS ASP ASN ILE THR GLY
SEQRES 35 C 523 LYS ASP LEU LEU LEU PHE SER ASN PRO ASN THR THR LYS
SEQRES 36 C 523 GLY ARG ASN HIS ILE THR ILE LYS ALA SER LEU ASP GLY
SEQRES 37 C 523 GLY LEU THR TRP PRO THR GLU HIS GLN VAL LEU LEU ASP
SEQRES 38 C 523 GLU ALA GLU GLY TRP GLY TYR SER CYS LEU SER MSE ILE
SEQRES 39 C 523 ASP LYS GLU THR VAL GLY ILE PHE TYR GLU SER SER VAL
SEQRES 40 C 523 ALA HIS MSE THR PHE GLN ALA VAL LYS LEU GLN ASP LEU
SEQRES 41 C 523 ILE HIS GLN
SEQRES 1 D 523 GLY ALA ASP SER ILE TYR VAL ARG GLU GLN GLN ILE PRO
SEQRES 2 D 523 ILE LEU ILE ASP ARG ILE ASP ASN VAL LEU TYR GLU MSE
SEQRES 3 D 523 ARG ILE PRO ALA GLN LYS GLY ASP VAL LEU ASN GLU ILE
SEQRES 4 D 523 THR ILE GLN ILE GLY ASP ASN VAL ASP LEU SER ASP ILE
SEQRES 5 D 523 GLN ALA ILE ARG LEU PHE TYR SER GLY VAL GLU ALA PRO
SEQRES 6 D 523 SER ARG LYS GLY GLU HIS PHE SER PRO VAL THR TYR ILE
SEQRES 7 D 523 SER SER HIS ILE PRO GLY ASN THR ARG LYS ALA LEU GLU
SEQRES 8 D 523 SER TYR SER VAL ARG GLN ASP GLU VAL THR ALA PRO LEU
SEQRES 9 D 523 SER ARG THR VAL LYS LEU THR SER LYS GLN PRO MSE LEU
SEQRES 10 D 523 LYS GLY ILE ASN TYR PHE TRP VAL SER ILE GLN MSE LYS
SEQRES 11 D 523 PRO GLU THR SER LEU LEU ALA LYS VAL ALA THR THR MSE
SEQRES 12 D 523 PRO ASN ALA GLN ILE ASN ASN LYS PRO ILE ASN ILE THR
SEQRES 13 D 523 TRP LYS GLY LYS VAL ASP GLU ARG HIS VAL GLY ILE GLY
SEQRES 14 D 523 VAL ARG GLN ALA GLY ASP ASP GLY SER ALA ALA PHE ARG
SEQRES 15 D 523 ILE PRO GLY LEU VAL THR THR ASN ASN GLY THR LEU LEU
SEQRES 16 D 523 GLY VAL TYR ASP ILE ARG TYR ASN SER SER VAL ASP LEU
SEQRES 17 D 523 GLN GLU LYS ILE ASP ILE GLY VAL SER ARG SER THR ASP
SEQRES 18 D 523 LYS GLY GLN THR TRP GLU PRO MSE ARG VAL ALA MSE THR
SEQRES 19 D 523 PHE LYS GLN THR ASP GLY LEU PRO HIS GLY GLN ASN GLY
SEQRES 20 D 523 VAL GLY ASP PRO SER ILE LEU VAL ASP GLU LYS THR ASN
SEQRES 21 D 523 THR ILE TRP VAL VAL ALA ALA TRP THR HIS GLY MSE GLY
SEQRES 22 D 523 ASN GLU ARG ALA TRP TRP ASN SER MSE PRO GLY MSE THR
SEQRES 23 D 523 PRO ASP GLU THR ALA GLN LEU MSE LEU VAL LYS SER GLU
SEQRES 24 D 523 ASP ASP GLY LYS THR TRP SER GLU PRO ILE ASN ILE THR
SEQRES 25 D 523 SER GLN VAL LYS ASP PRO SER TRP TYR PHE LEU LEU GLN
SEQRES 26 D 523 GLY PRO GLY ARG GLY ILE THR MSE GLN ASP GLY THR LEU
SEQRES 27 D 523 VAL PHE PRO ILE GLN PHE ILE ASP ALA THR ARG VAL PRO
SEQRES 28 D 523 ASN ALA GLY ILE MSE TYR SER LYS ASP ARG GLY LYS THR
SEQRES 29 D 523 TRP HIS LEU HIS ASN LEU ALA ARG THR ASN THR THR GLU
SEQRES 30 D 523 ALA GLN VAL ALA GLU VAL GLU PRO GLY VAL LEU MSE LEU
SEQRES 31 D 523 ASN MSE ARG ASP ASN ARG GLY GLY SER ARG ALA VAL ALA
SEQRES 32 D 523 THR THR LYS ASP LEU GLY LYS THR TRP THR GLU HIS PRO
SEQRES 33 D 523 SER SER ARG SER ALA LEU GLN GLU SER VAL CYS MSE ALA
SEQRES 34 D 523 SER LEU ILE LYS VAL ASN ALA LYS ASP ASN ILE THR GLY
SEQRES 35 D 523 LYS ASP LEU LEU LEU PHE SER ASN PRO ASN THR THR LYS
SEQRES 36 D 523 GLY ARG ASN HIS ILE THR ILE LYS ALA SER LEU ASP GLY
SEQRES 37 D 523 GLY LEU THR TRP PRO THR GLU HIS GLN VAL LEU LEU ASP
SEQRES 38 D 523 GLU ALA GLU GLY TRP GLY TYR SER CYS LEU SER MSE ILE
SEQRES 39 D 523 ASP LYS GLU THR VAL GLY ILE PHE TYR GLU SER SER VAL
SEQRES 40 D 523 ALA HIS MSE THR PHE GLN ALA VAL LYS LEU GLN ASP LEU
SEQRES 41 D 523 ILE HIS GLN
MODRES 4FJ6 MSE A 44 MET SELENOMETHIONINE
MODRES 4FJ6 MSE A 134 MET SELENOMETHIONINE
MODRES 4FJ6 MSE A 147 MET SELENOMETHIONINE
MODRES 4FJ6 MSE A 161 MET SELENOMETHIONINE
MODRES 4FJ6 MSE A 247 MET SELENOMETHIONINE
MODRES 4FJ6 MSE A 251 MET SELENOMETHIONINE
MODRES 4FJ6 MSE A 290 MET SELENOMETHIONINE
MODRES 4FJ6 MSE A 300 MET SELENOMETHIONINE
MODRES 4FJ6 MSE A 303 MET SELENOMETHIONINE
MODRES 4FJ6 MSE A 312 MET SELENOMETHIONINE
MODRES 4FJ6 MSE A 351 MET SELENOMETHIONINE
MODRES 4FJ6 MSE A 374 MET SELENOMETHIONINE
MODRES 4FJ6 MSE A 407 MET SELENOMETHIONINE
MODRES 4FJ6 MSE A 410 MET SELENOMETHIONINE
MODRES 4FJ6 MSE A 446 MET SELENOMETHIONINE
MODRES 4FJ6 MSE A 511 MET SELENOMETHIONINE
MODRES 4FJ6 MSE A 528 MET SELENOMETHIONINE
MODRES 4FJ6 MSE B 44 MET SELENOMETHIONINE
MODRES 4FJ6 MSE B 134 MET SELENOMETHIONINE
MODRES 4FJ6 MSE B 147 MET SELENOMETHIONINE
MODRES 4FJ6 MSE B 161 MET SELENOMETHIONINE
MODRES 4FJ6 MSE B 247 MET SELENOMETHIONINE
MODRES 4FJ6 MSE B 251 MET SELENOMETHIONINE
MODRES 4FJ6 MSE B 290 MET SELENOMETHIONINE
MODRES 4FJ6 MSE B 300 MET SELENOMETHIONINE
MODRES 4FJ6 MSE B 303 MET SELENOMETHIONINE
MODRES 4FJ6 MSE B 312 MET SELENOMETHIONINE
MODRES 4FJ6 MSE B 351 MET SELENOMETHIONINE
MODRES 4FJ6 MSE B 374 MET SELENOMETHIONINE
MODRES 4FJ6 MSE B 407 MET SELENOMETHIONINE
MODRES 4FJ6 MSE B 410 MET SELENOMETHIONINE
MODRES 4FJ6 MSE B 446 MET SELENOMETHIONINE
MODRES 4FJ6 MSE B 511 MET SELENOMETHIONINE
MODRES 4FJ6 MSE B 528 MET SELENOMETHIONINE
MODRES 4FJ6 MSE C 44 MET SELENOMETHIONINE
MODRES 4FJ6 MSE C 134 MET SELENOMETHIONINE
MODRES 4FJ6 MSE C 147 MET SELENOMETHIONINE
MODRES 4FJ6 MSE C 161 MET SELENOMETHIONINE
MODRES 4FJ6 MSE C 247 MET SELENOMETHIONINE
MODRES 4FJ6 MSE C 251 MET SELENOMETHIONINE
MODRES 4FJ6 MSE C 290 MET SELENOMETHIONINE
MODRES 4FJ6 MSE C 300 MET SELENOMETHIONINE
MODRES 4FJ6 MSE C 303 MET SELENOMETHIONINE
MODRES 4FJ6 MSE C 312 MET SELENOMETHIONINE
MODRES 4FJ6 MSE C 351 MET SELENOMETHIONINE
MODRES 4FJ6 MSE C 374 MET SELENOMETHIONINE
MODRES 4FJ6 MSE C 407 MET SELENOMETHIONINE
MODRES 4FJ6 MSE C 410 MET SELENOMETHIONINE
MODRES 4FJ6 MSE C 446 MET SELENOMETHIONINE
MODRES 4FJ6 MSE C 511 MET SELENOMETHIONINE
MODRES 4FJ6 MSE C 528 MET SELENOMETHIONINE
MODRES 4FJ6 MSE D 44 MET SELENOMETHIONINE
MODRES 4FJ6 MSE D 134 MET SELENOMETHIONINE
MODRES 4FJ6 MSE D 147 MET SELENOMETHIONINE
MODRES 4FJ6 MSE D 161 MET SELENOMETHIONINE
MODRES 4FJ6 MSE D 247 MET SELENOMETHIONINE
MODRES 4FJ6 MSE D 251 MET SELENOMETHIONINE
MODRES 4FJ6 MSE D 290 MET SELENOMETHIONINE
MODRES 4FJ6 MSE D 300 MET SELENOMETHIONINE
MODRES 4FJ6 MSE D 303 MET SELENOMETHIONINE
MODRES 4FJ6 MSE D 312 MET SELENOMETHIONINE
MODRES 4FJ6 MSE D 351 MET SELENOMETHIONINE
MODRES 4FJ6 MSE D 374 MET SELENOMETHIONINE
MODRES 4FJ6 MSE D 407 MET SELENOMETHIONINE
MODRES 4FJ6 MSE D 410 MET SELENOMETHIONINE
MODRES 4FJ6 MSE D 446 MET SELENOMETHIONINE
MODRES 4FJ6 MSE D 511 MET SELENOMETHIONINE
MODRES 4FJ6 MSE D 528 MET SELENOMETHIONINE
HET MSE A 44 8
HET MSE A 134 8
HET MSE A 147 8
HET MSE A 161 8
HET MSE A 247 8
HET MSE A 251 8
HET MSE A 290 8
HET MSE A 300 8
HET MSE A 303 13
HET MSE A 312 8
HET MSE A 351 8
HET MSE A 374 8
HET MSE A 407 8
HET MSE A 410 8
HET MSE A 446 8
HET MSE A 511 8
HET MSE A 528 8
HET MSE B 44 8
HET MSE B 134 8
HET MSE B 147 8
HET MSE B 161 8
HET MSE B 247 8
HET MSE B 251 8
HET MSE B 290 13
HET MSE B 300 8
HET MSE B 303 13
HET MSE B 312 8
HET MSE B 351 8
HET MSE B 374 8
HET MSE B 407 8
HET MSE B 410 8
HET MSE B 446 8
HET MSE B 511 8
HET MSE B 528 8
HET MSE C 44 8
HET MSE C 134 8
HET MSE C 147 8
HET MSE C 161 8
HET MSE C 247 8
HET MSE C 251 8
HET MSE C 290 8
HET MSE C 300 8
HET MSE C 303 8
HET MSE C 312 8
HET MSE C 351 8
HET MSE C 374 8
HET MSE C 407 8
HET MSE C 410 13
HET MSE C 446 8
HET MSE C 511 8
HET MSE C 528 8
HET MSE D 44 8
HET MSE D 134 8
HET MSE D 147 8
HET MSE D 161 8
HET MSE D 247 8
HET MSE D 251 8
HET MSE D 290 8
HET MSE D 300 8
HET MSE D 303 8
HET MSE D 312 8
HET MSE D 351 8
HET MSE D 374 8
HET MSE D 407 8
HET MSE D 410 8
HET MSE D 446 8
HET MSE D 511 8
HET MSE D 528 13
HET GOL A 601 6
HET GOL A 602 6
HET GOL A 603 6
HET GOL A 604 6
HET PO4 A 605 5
HET PO4 A 606 5
HET PO4 A 607 5
HET PO4 A 608 5
HET PO4 A 609 5
HET CL B 601 1
HET CL B 602 1
HET GOL B 603 6
HET GOL B 604 6
HET GOL B 605 12
HET PO4 B 606 5
HET PO4 B 607 5
HET PO4 B 608 5
HET GOL C 601 6
HET GOL C 602 6
HET GOL C 603 6
HET PO4 C 604 5
HET PO4 C 605 5
HET PO4 C 606 5
HET PO4 C 607 5
HET PO4 C 608 5
HET CL D 601 1
HET GOL D 602 6
HET GOL D 603 6
HET GOL D 604 6
HET GOL D 605 6
HET GOL D 606 6
HET PO4 D 607 5
HET PO4 D 608 5
HET PO4 D 609 5
HET PO4 D 610 5
HETNAM MSE SELENOMETHIONINE
HETNAM GOL GLYCEROL
HETNAM PO4 PHOSPHATE ION
HETNAM CL CHLORIDE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 68(C5 H11 N O2 SE)
FORMUL 5 GOL 15(C3 H8 O3)
FORMUL 9 PO4 17(O4 P 3-)
FORMUL 14 CL 3(CL 1-)
FORMUL 40 HOH *2000(H2 O)
HELIX 1 1 ASP A 66 SER A 68 5 3
HELIX 2 2 GLY A 192 SER A 196 5 5
HELIX 3 3 GLN A 255 LEU A 259 5 5
HELIX 4 4 PRO A 260 ASN A 264 5 5
HELIX 5 5 ARG A 294 ASN A 298 5 5
HELIX 6 6 ILE A 329 LYS A 334 1 6
HELIX 7 7 ASN A 453 ASN A 457 5 5
HELIX 8 8 PRO A 491 GLU A 493 5 3
HELIX 9 9 LEU A 535 ILE A 539 1 5
HELIX 10 10 ASP B 66 SER B 68 5 3
HELIX 11 11 GLY B 192 SER B 196 5 5
HELIX 12 12 GLN B 255 LEU B 259 5 5
HELIX 13 13 PRO B 260 ASN B 264 5 5
HELIX 14 14 ARG B 294 ASN B 298 5 5
HELIX 15 15 ILE B 329 LYS B 334 1 6
HELIX 16 16 ASN B 453 ASN B 457 5 5
HELIX 17 17 PRO B 491 GLU B 493 5 3
HELIX 18 18 LEU B 535 ILE B 539 1 5
HELIX 19 19 ASP C 66 SER C 68 5 3
HELIX 20 20 GLY C 192 SER C 196 5 5
HELIX 21 21 GLN C 255 LEU C 259 5 5
HELIX 22 22 PRO C 260 ASN C 264 5 5
HELIX 23 23 ARG C 294 SER C 299 1 6
HELIX 24 24 ILE C 329 LYS C 334 1 6
HELIX 25 25 ASN C 453 ASN C 457 5 5
HELIX 26 26 PRO C 491 GLU C 493 5 3
HELIX 27 27 LEU C 535 ILE C 539 1 5
HELIX 28 28 ASP D 66 SER D 68 5 3
HELIX 29 29 GLY D 192 SER D 196 5 5
HELIX 30 30 GLN D 255 LEU D 259 5 5
HELIX 31 31 PRO D 260 ASN D 264 5 5
HELIX 32 32 ARG D 294 SER D 299 1 6
HELIX 33 33 ILE D 329 LYS D 334 1 6
HELIX 34 34 ASN D 453 ASN D 457 5 5
HELIX 35 35 PRO D 491 GLU D 493 5 3
HELIX 36 36 LEU D 535 ILE D 539 1 5
SHEET 1 A 6 VAL A 113 THR A 119 0
SHEET 2 A 6 ILE A 70 VAL A 80 -1 N LEU A 75 O GLN A 115
SHEET 3 A 6 GLY A 137 MSE A 147 -1 O GLN A 146 N ALA A 72
SHEET 4 A 6 VAL A 40 ALA A 48 -1 N ILE A 46 O ASN A 139
SHEET 5 A 6 ILE A 23 ARG A 26 -1 N TYR A 24 O ARG A 45
SHEET 6 A 6 ILE A 173 TRP A 175 1 O THR A 174 N ILE A 23
SHEET 1 B 3 ILE A 32 LEU A 33 0
SHEET 2 B 3 ARG A 182 ARG A 189 1 O HIS A 183 N ILE A 32
SHEET 3 B 3 LYS A 156 VAL A 157 -1 N VAL A 157 O ARG A 182
SHEET 1 C 5 ILE A 32 LEU A 33 0
SHEET 2 C 5 ARG A 182 ARG A 189 1 O HIS A 183 N ILE A 32
SHEET 3 C 5 MSE A 528 LYS A 534 -1 O PHE A 530 N ILE A 186
SHEET 4 C 5 THR A 516 TYR A 521 -1 N TYR A 521 O THR A 529
SHEET 5 C 5 SER A 507 MSE A 511 -1 N SER A 510 O GLY A 518
SHEET 1 D 4 THR A 125 LEU A 128 0
SHEET 2 D 4 GLU A 56 ILE A 61 -1 N ILE A 59 O VAL A 126
SHEET 3 D 4 THR A 159 ILE A 166 -1 O GLN A 165 N GLU A 56
SHEET 4 D 4 LYS A 169 PRO A 170 -1 O LYS A 169 N ILE A 166
SHEET 1 E 4 ALA A 198 THR A 206 0
SHEET 2 E 4 LEU A 212 ARG A 219 -1 O ASP A 217 N ARG A 200
SHEET 3 E 4 ILE A 230 SER A 237 -1 O ASP A 231 N ILE A 218
SHEET 4 E 4 ARG A 248 MSE A 251 -1 O ARG A 248 N VAL A 234
SHEET 1 F 5 ILE A 327 ASN A 328 0
SHEET 2 F 5 GLN A 310 SER A 316 -1 N LEU A 313 O ILE A 327
SHEET 3 F 5 ILE A 280 TRP A 286 -1 N TRP A 286 O GLN A 310
SHEET 4 F 5 VAL A 266 VAL A 273 -1 N SER A 270 O VAL A 283
SHEET 5 F 5 GLY A 346 ARG A 347 1 O GLY A 346 N PRO A 269
SHEET 1 G 4 PHE A 340 GLN A 343 0
SHEET 2 G 4 LEU A 356 ILE A 363 -1 O GLN A 361 N LEU A 342
SHEET 3 G 4 PRO A 369 SER A 376 -1 O MSE A 374 N PHE A 358
SHEET 4 G 4 HIS A 384 LEU A 385 -1 O HIS A 384 N TYR A 375
SHEET 1 H 4 ILE A 349 THR A 350 0
SHEET 2 H 4 LEU A 356 ILE A 363 -1 O VAL A 357 N ILE A 349
SHEET 3 H 4 PRO A 369 SER A 376 -1 O MSE A 374 N PHE A 358
SHEET 4 H 4 ARG A 390 THR A 391 -1 O ARG A 390 N ALA A 371
SHEET 1 I 4 THR A 393 GLU A 402 0
SHEET 2 I 4 VAL A 405 ASP A 412 -1 O ARG A 411 N GLU A 395
SHEET 3 I 4 ALA A 419 THR A 423 -1 O ALA A 419 N MSE A 410
SHEET 4 I 4 THR A 431 GLU A 432 -1 O THR A 431 N THR A 422
SHEET 1 J 4 SER A 448 VAL A 452 0
SHEET 2 J 4 LEU A 463 PRO A 469 -1 O LEU A 463 N VAL A 452
SHEET 3 J 4 ILE A 478 SER A 483 -1 O LYS A 481 N PHE A 466
SHEET 4 J 4 GLN A 495 ASP A 499 -1 O LEU A 498 N ILE A 478
SHEET 1 K 6 VAL B 113 THR B 119 0
SHEET 2 K 6 ILE B 70 VAL B 80 -1 N LEU B 75 O GLN B 115
SHEET 3 K 6 GLY B 137 MSE B 147 -1 O GLN B 146 N ALA B 72
SHEET 4 K 6 VAL B 40 ALA B 48 -1 N ALA B 48 O GLY B 137
SHEET 5 K 6 ILE B 23 ARG B 26 -1 N TYR B 24 O ARG B 45
SHEET 6 K 6 ILE B 173 TRP B 175 1 O THR B 174 N ILE B 23
SHEET 1 L 3 ILE B 32 LEU B 33 0
SHEET 2 L 3 ARG B 182 ARG B 189 1 O HIS B 183 N ILE B 32
SHEET 3 L 3 LYS B 156 VAL B 157 -1 N VAL B 157 O ARG B 182
SHEET 1 M 5 ILE B 32 LEU B 33 0
SHEET 2 M 5 ARG B 182 ARG B 189 1 O HIS B 183 N ILE B 32
SHEET 3 M 5 MSE B 528 LYS B 534 -1 O PHE B 530 N ILE B 186
SHEET 4 M 5 THR B 516 TYR B 521 -1 N TYR B 521 O THR B 529
SHEET 5 M 5 SER B 507 MSE B 511 -1 N SER B 510 O GLY B 518
SHEET 1 N 4 THR B 125 THR B 129 0
SHEET 2 N 4 GLU B 56 ILE B 61 -1 N ILE B 59 O VAL B 126
SHEET 3 N 4 THR B 159 ILE B 166 -1 O GLN B 165 N GLU B 56
SHEET 4 N 4 LYS B 169 PRO B 170 -1 O LYS B 169 N ILE B 166
SHEET 1 O 4 ALA B 198 THR B 206 0
SHEET 2 O 4 LEU B 212 ARG B 219 -1 O ASP B 217 N ARG B 200
SHEET 3 O 4 ILE B 230 SER B 237 -1 O ASP B 231 N ILE B 218
SHEET 4 O 4 ARG B 248 MSE B 251 -1 O MSE B 251 N ILE B 232
SHEET 1 P 5 ILE B 327 ASN B 328 0
SHEET 2 P 5 GLN B 310 SER B 316 -1 N LEU B 313 O ILE B 327
SHEET 3 P 5 ILE B 280 TRP B 286 -1 N TRP B 286 O GLN B 310
SHEET 4 P 5 VAL B 266 VAL B 273 -1 N LEU B 272 O TRP B 281
SHEET 5 P 5 GLY B 346 ARG B 347 1 O GLY B 346 N ILE B 271
SHEET 1 Q 4 PHE B 340 GLN B 343 0
SHEET 2 Q 4 LEU B 356 ILE B 363 -1 O GLN B 361 N LEU B 342
SHEET 3 Q 4 PRO B 369 SER B 376 -1 O MSE B 374 N PHE B 358
SHEET 4 Q 4 HIS B 384 LEU B 385 -1 O HIS B 384 N TYR B 375
SHEET 1 R 4 ILE B 349 THR B 350 0
SHEET 2 R 4 LEU B 356 ILE B 363 -1 O VAL B 357 N ILE B 349
SHEET 3 R 4 PRO B 369 SER B 376 -1 O MSE B 374 N PHE B 358
SHEET 4 R 4 ARG B 390 THR B 391 -1 O ARG B 390 N ALA B 371
SHEET 1 S 4 THR B 393 GLU B 402 0
SHEET 2 S 4 VAL B 405 ASP B 412 -1 O MSE B 407 N ALA B 399
SHEET 3 S 4 ALA B 419 THR B 423 -1 O ALA B 419 N MSE B 410
SHEET 4 S 4 THR B 431 GLU B 432 -1 O THR B 431 N THR B 422
SHEET 1 T 2 GLY B 416 SER B 417 0
SHEET 2 T 2 GLN B 441 GLU B 442 -1 O GLU B 442 N GLY B 416
SHEET 1 U 4 SER B 448 VAL B 452 0
SHEET 2 U 4 LEU B 463 PRO B 469 -1 O LEU B 463 N VAL B 452
SHEET 3 U 4 ILE B 478 SER B 483 -1 O LYS B 481 N PHE B 466
SHEET 4 U 4 GLN B 495 ASP B 499 -1 O LEU B 498 N ILE B 478
SHEET 1 V 6 VAL C 113 THR C 119 0
SHEET 2 V 6 ILE C 70 VAL C 80 -1 N LEU C 75 O GLN C 115
SHEET 3 V 6 GLY C 137 MSE C 147 -1 O GLN C 146 N ALA C 72
SHEET 4 V 6 VAL C 40 ALA C 48 -1 N LEU C 41 O VAL C 143
SHEET 5 V 6 TYR C 24 ARG C 26 -1 N TYR C 24 O ARG C 45
SHEET 6 V 6 THR C 174 TRP C 175 1 O THR C 174 N VAL C 25
SHEET 1 W 3 ILE C 32 LEU C 33 0
SHEET 2 W 3 ARG C 182 ARG C 189 1 O HIS C 183 N ILE C 32
SHEET 3 W 3 LYS C 156 VAL C 157 -1 N VAL C 157 O ARG C 182
SHEET 1 X 5 ILE C 32 LEU C 33 0
SHEET 2 X 5 ARG C 182 ARG C 189 1 O HIS C 183 N ILE C 32
SHEET 3 X 5 MSE C 528 LYS C 534 -1 O MSE C 528 N ARG C 189
SHEET 4 X 5 THR C 516 TYR C 521 -1 N TYR C 521 O THR C 529
SHEET 5 X 5 SER C 507 MSE C 511 -1 N SER C 510 O GLY C 518
SHEET 1 Y 4 THR C 125 THR C 129 0
SHEET 2 Y 4 GLU C 56 ILE C 61 -1 N ILE C 59 O VAL C 126
SHEET 3 Y 4 THR C 159 ILE C 166 -1 O THR C 160 N GLN C 60
SHEET 4 Y 4 LYS C 169 PRO C 170 -1 O LYS C 169 N ILE C 166
SHEET 1 Z 4 ALA C 198 THR C 206 0
SHEET 2 Z 4 LEU C 212 ARG C 219 -1 O ASP C 217 N ARG C 200
SHEET 3 Z 4 ILE C 230 SER C 237 -1 O ASP C 231 N ILE C 218
SHEET 4 Z 4 ARG C 248 MSE C 251 -1 O MSE C 251 N ILE C 232
SHEET 1 AA 5 ILE C 327 ASN C 328 0
SHEET 2 AA 5 GLN C 310 SER C 316 -1 N LEU C 313 O ILE C 327
SHEET 3 AA 5 ILE C 280 TRP C 286 -1 N ALA C 284 O MSE C 312
SHEET 4 AA 5 VAL C 266 VAL C 273 -1 N LEU C 272 O TRP C 281
SHEET 5 AA 5 GLY C 346 ARG C 347 1 O GLY C 346 N ILE C 271
SHEET 1 AB 4 PHE C 340 GLN C 343 0
SHEET 2 AB 4 LEU C 356 ILE C 363 -1 O GLN C 361 N LEU C 342
SHEET 3 AB 4 PRO C 369 SER C 376 -1 O MSE C 374 N PHE C 358
SHEET 4 AB 4 HIS C 384 LEU C 385 -1 O HIS C 384 N TYR C 375
SHEET 1 AC 4 ILE C 349 THR C 350 0
SHEET 2 AC 4 LEU C 356 ILE C 363 -1 O VAL C 357 N ILE C 349
SHEET 3 AC 4 PRO C 369 SER C 376 -1 O MSE C 374 N PHE C 358
SHEET 4 AC 4 ARG C 390 THR C 391 -1 O ARG C 390 N ALA C 371
SHEET 1 AD 4 THR C 393 GLU C 402 0
SHEET 2 AD 4 VAL C 405 ASP C 412 -1 O MSE C 407 N ALA C 399
SHEET 3 AD 4 ALA C 419 THR C 423 -1 O ALA C 419 N MSE C 410
SHEET 4 AD 4 THR C 431 GLU C 432 -1 O THR C 431 N THR C 422
SHEET 1 AE 4 SER C 448 VAL C 452 0
SHEET 2 AE 4 LEU C 463 PRO C 469 -1 O LEU C 463 N VAL C 452
SHEET 3 AE 4 ILE C 478 SER C 483 -1 O LYS C 481 N PHE C 466
SHEET 4 AE 4 GLN C 495 ASP C 499 -1 O LEU C 498 N ILE C 478
SHEET 1 AF 6 VAL D 113 THR D 119 0
SHEET 2 AF 6 ILE D 70 VAL D 80 -1 N LEU D 75 O GLN D 115
SHEET 3 AF 6 GLY D 137 MSE D 147 -1 O GLN D 146 N ALA D 72
SHEET 4 AF 6 VAL D 40 ALA D 48 -1 N ILE D 46 O ASN D 139
SHEET 5 AF 6 ILE D 23 ARG D 26 -1 N TYR D 24 O ARG D 45
SHEET 6 AF 6 ILE D 173 TRP D 175 1 O THR D 174 N ILE D 23
SHEET 1 AG 3 ILE D 32 LEU D 33 0
SHEET 2 AG 3 ARG D 182 ARG D 189 1 O HIS D 183 N ILE D 32
SHEET 3 AG 3 LYS D 156 VAL D 157 -1 N VAL D 157 O ARG D 182
SHEET 1 AH 5 ILE D 32 LEU D 33 0
SHEET 2 AH 5 ARG D 182 ARG D 189 1 O HIS D 183 N ILE D 32
SHEET 3 AH 5 MSE D 528 LYS D 534 -1 O PHE D 530 N ILE D 186
SHEET 4 AH 5 THR D 516 TYR D 521 -1 N TYR D 521 O THR D 529
SHEET 5 AH 5 SER D 507 ASP D 513 -1 N SER D 510 O GLY D 518
SHEET 1 AI 4 THR D 125 THR D 129 0
SHEET 2 AI 4 GLU D 56 ILE D 61 -1 N ILE D 59 O VAL D 126
SHEET 3 AI 4 THR D 159 ILE D 166 -1 O GLN D 165 N GLU D 56
SHEET 4 AI 4 LYS D 169 PRO D 170 -1 O LYS D 169 N ILE D 166
SHEET 1 AJ 4 ALA D 198 THR D 206 0
SHEET 2 AJ 4 LEU D 212 ARG D 219 -1 O ASP D 217 N ARG D 200
SHEET 3 AJ 4 ILE D 230 SER D 237 -1 O ASP D 231 N ILE D 218
SHEET 4 AJ 4 ARG D 248 MSE D 251 -1 O MSE D 251 N ILE D 232
SHEET 1 AK 5 ILE D 327 ASN D 328 0
SHEET 2 AK 5 GLN D 310 SER D 316 -1 N LEU D 313 O ILE D 327
SHEET 3 AK 5 ILE D 280 TRP D 286 -1 N TRP D 286 O GLN D 310
SHEET 4 AK 5 VAL D 266 VAL D 273 -1 N LEU D 272 O TRP D 281
SHEET 5 AK 5 GLY D 346 ARG D 347 1 O GLY D 346 N ILE D 271
SHEET 1 AL 4 PHE D 340 GLN D 343 0
SHEET 2 AL 4 LEU D 356 ILE D 363 -1 O GLN D 361 N LEU D 342
SHEET 3 AL 4 PRO D 369 SER D 376 -1 O MSE D 374 N PHE D 358
SHEET 4 AL 4 HIS D 384 LEU D 385 -1 O HIS D 384 N TYR D 375
SHEET 1 AM 4 ILE D 349 THR D 350 0
SHEET 2 AM 4 LEU D 356 ILE D 363 -1 O VAL D 357 N ILE D 349
SHEET 3 AM 4 PRO D 369 SER D 376 -1 O MSE D 374 N PHE D 358
SHEET 4 AM 4 ARG D 390 THR D 391 -1 O ARG D 390 N ALA D 371
SHEET 1 AN 4 THR D 393 GLU D 402 0
SHEET 2 AN 4 VAL D 405 ASP D 412 -1 O MSE D 407 N ALA D 399
SHEET 3 AN 4 ALA D 419 THR D 423 -1 O ALA D 419 N MSE D 410
SHEET 4 AN 4 THR D 431 GLU D 432 -1 O THR D 431 N THR D 422
SHEET 1 AO 2 GLY D 416 SER D 417 0
SHEET 2 AO 2 GLN D 441 GLU D 442 -1 O GLU D 442 N GLY D 416
SHEET 1 AP 4 SER D 448 VAL D 452 0
SHEET 2 AP 4 LEU D 463 PRO D 469 -1 O LEU D 463 N VAL D 452
SHEET 3 AP 4 ILE D 478 SER D 483 -1 O LYS D 481 N PHE D 466
SHEET 4 AP 4 GLN D 495 ASP D 499 -1 O LEU D 498 N ILE D 478
LINK C GLU A 43 N MSE A 44 1555 1555 1.33
LINK C MSE A 44 N ARG A 45 1555 1555 1.33
LINK C PRO A 133 N MSE A 134 1555 1555 1.33
LINK C MSE A 134 N LEU A 135 1555 1555 1.33
LINK C GLN A 146 N MSE A 147 1555 1555 1.33
LINK C MSE A 147 N LYS A 148 1555 1555 1.33
LINK C THR A 160 N MSE A 161 1555 1555 1.33
LINK C MSE A 161 N PRO A 162 1555 1555 1.35
LINK C PRO A 246 N MSE A 247 1555 1555 1.33
LINK C MSE A 247 N ARG A 248 1555 1555 1.33
LINK C ALA A 250 N MSE A 251 1555 1555 1.34
LINK C MSE A 251 N THR A 252 1555 1555 1.33
LINK C GLY A 289 N MSE A 290 1555 1555 1.34
LINK C MSE A 290 N GLY A 291 1555 1555 1.33
LINK C SER A 299 N MSE A 300 1555 1555 1.33
LINK C MSE A 300 N PRO A 301 1555 1555 1.36
LINK C GLY A 302 N MSE A 303 1555 1555 1.34
LINK C MSE A 303 N THR A 304 1555 1555 1.33
LINK C LEU A 311 N MSE A 312 1555 1555 1.34
LINK C MSE A 312 N LEU A 313 1555 1555 1.34
LINK C THR A 350 N MSE A 351 1555 1555 1.33
LINK C MSE A 351 N GLN A 352 1555 1555 1.33
LINK C ILE A 373 N MSE A 374 1555 1555 1.33
LINK C MSE A 374 N TYR A 375 1555 1555 1.33
LINK C LEU A 406 N MSE A 407 1555 1555 1.33
LINK C MSE A 407 N LEU A 408 1555 1555 1.33
LINK C ASN A 409 N MSE A 410 1555 1555 1.33
LINK C MSE A 410 N ARG A 411 1555 1555 1.33
LINK C CYS A 445 N MSE A 446 1555 1555 1.33
LINK C MSE A 446 N ALA A 447 1555 1555 1.33
LINK C SER A 510 N MSE A 511 1555 1555 1.33
LINK C MSE A 511 N ILE A 512 1555 1555 1.33
LINK C HIS A 527 N MSE A 528 1555 1555 1.34
LINK C MSE A 528 N THR A 529 1555 1555 1.33
LINK C GLU B 43 N MSE B 44 1555 1555 1.33
LINK C MSE B 44 N ARG B 45 1555 1555 1.33
LINK C PRO B 133 N MSE B 134 1555 1555 1.33
LINK C MSE B 134 N LEU B 135 1555 1555 1.33
LINK C GLN B 146 N MSE B 147 1555 1555 1.33
LINK C MSE B 147 N LYS B 148 1555 1555 1.33
LINK C THR B 160 N MSE B 161 1555 1555 1.33
LINK C MSE B 161 N PRO B 162 1555 1555 1.35
LINK C PRO B 246 N MSE B 247 1555 1555 1.33
LINK C MSE B 247 N ARG B 248 1555 1555 1.33
LINK C ALA B 250 N MSE B 251 1555 1555 1.33
LINK C MSE B 251 N THR B 252 1555 1555 1.33
LINK C GLY B 289 N MSE B 290 1555 1555 1.34
LINK C MSE B 290 N GLY B 291 1555 1555 1.34
LINK C SER B 299 N MSE B 300 1555 1555 1.33
LINK C MSE B 300 N PRO B 301 1555 1555 1.36
LINK C GLY B 302 N MSE B 303 1555 1555 1.34
LINK C MSE B 303 N THR B 304 1555 1555 1.34
LINK C LEU B 311 N MSE B 312 1555 1555 1.33
LINK C MSE B 312 N LEU B 313 1555 1555 1.34
LINK C THR B 350 N MSE B 351 1555 1555 1.33
LINK C MSE B 351 N GLN B 352 1555 1555 1.33
LINK C ILE B 373 N MSE B 374 1555 1555 1.33
LINK C MSE B 374 N TYR B 375 1555 1555 1.33
LINK C LEU B 406 N MSE B 407 1555 1555 1.33
LINK C MSE B 407 N LEU B 408 1555 1555 1.34
LINK C ASN B 409 N MSE B 410 1555 1555 1.33
LINK C MSE B 410 N ARG B 411 1555 1555 1.33
LINK C CYS B 445 N MSE B 446 1555 1555 1.33
LINK C MSE B 446 N ALA B 447 1555 1555 1.33
LINK C SER B 510 N MSE B 511 1555 1555 1.33
LINK C MSE B 511 N ILE B 512 1555 1555 1.33
LINK C HIS B 527 N MSE B 528 1555 1555 1.33
LINK C MSE B 528 N THR B 529 1555 1555 1.33
LINK C GLU C 43 N MSE C 44 1555 1555 1.33
LINK C MSE C 44 N ARG C 45 1555 1555 1.33
LINK C PRO C 133 N MSE C 134 1555 1555 1.33
LINK C MSE C 134 N LEU C 135 1555 1555 1.33
LINK C GLN C 146 N MSE C 147 1555 1555 1.33
LINK C MSE C 147 N LYS C 148 1555 1555 1.33
LINK C THR C 160 N MSE C 161 1555 1555 1.33
LINK C MSE C 161 N PRO C 162 1555 1555 1.35
LINK C PRO C 246 N MSE C 247 1555 1555 1.33
LINK C MSE C 247 N ARG C 248 1555 1555 1.33
LINK C ALA C 250 N MSE C 251 1555 1555 1.34
LINK C MSE C 251 N THR C 252 1555 1555 1.33
LINK C GLY C 289 N MSE C 290 1555 1555 1.33
LINK C MSE C 290 N GLY C 291 1555 1555 1.33
LINK C SER C 299 N MSE C 300 1555 1555 1.33
LINK C MSE C 300 N PRO C 301 1555 1555 1.36
LINK C GLY C 302 N MSE C 303 1555 1555 1.33
LINK C MSE C 303 N THR C 304 1555 1555 1.34
LINK C LEU C 311 N MSE C 312 1555 1555 1.34
LINK C MSE C 312 N LEU C 313 1555 1555 1.34
LINK C THR C 350 N MSE C 351 1555 1555 1.33
LINK C MSE C 351 N GLN C 352 1555 1555 1.33
LINK C ILE C 373 N MSE C 374 1555 1555 1.33
LINK C MSE C 374 N TYR C 375 1555 1555 1.33
LINK C LEU C 406 N MSE C 407 1555 1555 1.33
LINK C MSE C 407 N LEU C 408 1555 1555 1.33
LINK C ASN C 409 N MSE C 410 1555 1555 1.34
LINK C MSE C 410 N ARG C 411 1555 1555 1.34
LINK C CYS C 445 N MSE C 446 1555 1555 1.33
LINK C MSE C 446 N ALA C 447 1555 1555 1.33
LINK C SER C 510 N MSE C 511 1555 1555 1.33
LINK C MSE C 511 N ILE C 512 1555 1555 1.33
LINK C HIS C 527 N MSE C 528 1555 1555 1.33
LINK C MSE C 528 N THR C 529 1555 1555 1.33
LINK C GLU D 43 N MSE D 44 1555 1555 1.33
LINK C MSE D 44 N ARG D 45 1555 1555 1.34
LINK C PRO D 133 N MSE D 134 1555 1555 1.33
LINK C MSE D 134 N LEU D 135 1555 1555 1.33
LINK C GLN D 146 N MSE D 147 1555 1555 1.33
LINK C MSE D 147 N LYS D 148 1555 1555 1.32
LINK C THR D 160 N MSE D 161 1555 1555 1.33
LINK C MSE D 161 N PRO D 162 1555 1555 1.35
LINK C PRO D 246 N MSE D 247 1555 1555 1.33
LINK C MSE D 247 N ARG D 248 1555 1555 1.33
LINK C ALA D 250 N MSE D 251 1555 1555 1.34
LINK C MSE D 251 N THR D 252 1555 1555 1.34
LINK C GLY D 289 N MSE D 290 1555 1555 1.34
LINK C MSE D 290 N GLY D 291 1555 1555 1.33
LINK C SER D 299 N MSE D 300 1555 1555 1.33
LINK C MSE D 300 N PRO D 301 1555 1555 1.35
LINK C GLY D 302 N MSE D 303 1555 1555 1.34
LINK C MSE D 303 N THR D 304 1555 1555 1.33
LINK C LEU D 311 N MSE D 312 1555 1555 1.34
LINK C MSE D 312 N LEU D 313 1555 1555 1.34
LINK C THR D 350 N MSE D 351 1555 1555 1.33
LINK C MSE D 351 N GLN D 352 1555 1555 1.33
LINK C ILE D 373 N MSE D 374 1555 1555 1.33
LINK C MSE D 374 N TYR D 375 1555 1555 1.33
LINK C LEU D 406 N MSE D 407 1555 1555 1.33
LINK C MSE D 407 N LEU D 408 1555 1555 1.33
LINK C ASN D 409 N MSE D 410 1555 1555 1.33
LINK C MSE D 410 N ARG D 411 1555 1555 1.34
LINK C CYS D 445 N MSE D 446 1555 1555 1.32
LINK C MSE D 446 N ALA D 447 1555 1555 1.33
LINK C SER D 510 N MSE D 511 1555 1555 1.33
LINK C MSE D 511 N ILE D 512 1555 1555 1.33
LINK C HIS D 527 N MSE D 528 1555 1555 1.34
LINK C MSE D 528 N THR D 529 1555 1555 1.33
CISPEP 1 ALA A 120 PRO A 121 0 -1.61
CISPEP 2 LEU A 226 GLN A 227 0 2.54
CISPEP 3 ALA B 120 PRO B 121 0 -0.74
CISPEP 4 LEU B 226 GLN B 227 0 2.37
CISPEP 5 ALA C 120 PRO C 121 0 -1.78
CISPEP 6 LEU C 226 GLN C 227 0 1.76
CISPEP 7 ALA D 120 PRO D 121 0 0.22
CISPEP 8 LEU D 226 GLN D 227 0 1.35
SITE 1 AC1 7 SER A 98 HIS A 99 GLY A 503 TRP A 504
SITE 2 AC1 7 GLU A 522 SER A 523 HIS A 527
SITE 1 AC2 9 GLU A 275 ARG A 347 ILE A 349 ILE A 450
SITE 2 AC2 9 LYS A 451 HOH A 752 HOH A 861 HOH A 871
SITE 3 AC2 9 HOH A 900
SITE 1 AC3 9 ASP A 35 ARG A 105 GLY A 187 VAL A 188
SITE 2 AC3 9 GLN A 190 HOH A 725 HOH A 859 HOH A 885
SITE 3 AC3 9 HOH A1165
SITE 1 AC4 5 ARG A 200 SER A 223 VAL A 224 TRP A 504
SITE 2 AC4 5 HOH A 902
SITE 1 AC5 5 LYS A 229 LYS A 254 HIS A 261 HOH A 983
SITE 2 AC5 5 HOH A1065
SITE 1 AC6 7 ARG A 26 HIS A 89 PHE A 90 SER A 91
SITE 2 AC6 7 HOH A 727 HOH A 960 HOH A1167
SITE 1 AC7 5 ARG A 200 ARG A 411 ARG A 475 TYR A 506
SITE 2 AC7 5 HOH A 902
SITE 1 AC8 5 HIS A 384 HIS A 386 HOH A1016 HOH A1103
SITE 2 AC8 5 HOH A1155
SITE 1 AC9 6 ARG A 236 GLU A 245 LYS A 321 HOH A1097
SITE 2 AC9 6 HOH A1119 HOH A1159
SITE 1 BC1 3 LYS B 50 GLN D 49 LYS D 50
SITE 1 BC2 1 GLU B 109
SITE 1 BC3 8 GLU A 109 SER A 110 LYS B 229 LYS B 254
SITE 2 BC3 8 HIS B 261 HOH B1062 HOH B1173 HOH B1174
SITE 1 BC4 7 GLU B 275 ILE B 450 LYS B 451 HOH B 737
SITE 2 BC4 7 HOH B 741 HOH B1017 HOH B1026
SITE 1 BC5 10 ASN A 168 ASP B 35 ARG B 105 ILE B 186
SITE 2 BC5 10 GLY B 187 VAL B 188 GLN B 190 HOH B 789
SITE 3 BC5 10 HOH B 905 HOH B 962
SITE 1 BC6 5 ARG B 200 ARG B 411 ARG B 475 TYR B 506
SITE 2 BC6 5 HOH B 835
SITE 1 BC7 9 ARG B 26 HIS B 89 PHE B 90 SER B 91
SITE 2 BC7 9 HOH B 780 HOH B 850 HOH B 920 HOH B 936
SITE 3 BC7 9 HOH B1127
SITE 1 BC8 4 ARG B 236 THR B 238 GLU B 245 LYS B 321
SITE 1 BC9 6 ASN C 103 GLU C 109 SER C 110 HOH C 759
SITE 2 BC9 6 HOH C1069 HOH C1070
SITE 1 CC1 8 GLU C 275 ILE C 349 ILE C 450 LYS C 451
SITE 2 CC1 8 HOH C 792 HOH C 910 HOH C 988 HOH C1065
SITE 1 CC2 7 VAL C 93 THR C 94 LEU C 108 TYR C 111
SITE 2 CC2 7 HOH C 962 HOH C1179 ASN D 292
SITE 1 CC3 3 HIS C 261 HOH C 768 HOH C1128
SITE 1 CC4 7 ARG C 200 ASP C 225 ARG C 411 ARG C 475
SITE 2 CC4 7 TYR C 506 HOH C 779 HOH C 975
SITE 1 CC5 8 ARG C 26 HIS C 89 PHE C 90 SER C 91
SITE 2 CC5 8 HOH C 744 HOH C 790 HOH C1002 HOH C1059
SITE 1 CC6 5 HIS C 384 HIS C 386 HOH C 832 HOH C 871
SITE 2 CC6 5 HOH C1110
SITE 1 CC7 4 ARG C 390 ARG C 414 ARG C 437 HOH C1190
SITE 1 CC8 1 ARG D 236
SITE 1 CC9 8 GLU D 275 ILE D 349 ILE D 450 LYS D 451
SITE 2 CC9 8 HOH D 735 HOH D 843 HOH D 844 HOH D1008
SITE 1 DC1 6 ASN C 292 VAL D 93 THR D 94 LEU D 108
SITE 2 DC1 6 TYR D 111 HOH D 834
SITE 1 DC2 9 ASP D 35 ARG D 105 GLY D 187 VAL D 188
SITE 2 DC2 9 ARG D 189 ASP D 193 HOH D 756 HOH D 870
SITE 3 DC2 9 HOH D 927
SITE 1 DC3 9 SER D 98 HIS D 99 GLY D 503 TRP D 504
SITE 2 DC3 9 GLU D 522 SER D 523 SER D 524 ALA D 526
SITE 3 DC3 9 HOH D1162
SITE 1 DC4 7 HOH C1068 ASN D 103 ALA D 107 LEU D 108
SITE 2 DC4 7 GLU D 109 SER D 110 HOH D 732
SITE 1 DC5 6 HOH C 718 LYS D 229 LYS D 254 HIS D 261
SITE 2 DC5 6 HOH D 709 HOH D 712
SITE 1 DC6 10 ARG D 26 HIS D 89 PHE D 90 SER D 91
SITE 2 DC6 10 HOH D 771 HOH D 880 HOH D1005 HOH D1056
SITE 3 DC6 10 HOH D1109 HOH D1129
SITE 1 DC7 5 ARG D 200 ARG D 411 ARG D 475 TYR D 506
SITE 2 DC7 5 HOH D1153
SITE 1 DC8 5 HIS D 384 HIS D 386 HOH D 818 HOH D 937
SITE 2 DC8 5 HOH D1155
CRYST1 171.738 171.738 243.786 90.00 90.00 120.00 H 3 36
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 0.005823 0.003362 0.000000 0.00000
SCALE2 0.000000 0.006724 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004102 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
