HEADER APOPTOSIS 23-MAR-05 1Z6T
TITLE STRUCTURE OF THE APOPTOTIC PROTEASE-ACTIVATING FACTOR 1 BOUND TO ADP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOPTOTIC PROTEASE ACTIVATING FACTOR 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: APAF-1, RESIDUES 1-591;
COMPND 5 SYNONYM: APAF-1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-29B
KEYWDS APAF-1, CASPASE ACTIVATION, ADP, NUCLEOTIDE BINDING, CARD, APOPTOSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR S.J.RIEDL,W.LI,Y.CHAO,R.SCHWARZENBACHER,Y.SHI
REVDAT 4 14-FEB-24 1Z6T 1 REMARK
REVDAT 3 24-FEB-09 1Z6T 1 VERSN
REVDAT 2 26-APR-05 1Z6T 1 REMARK MASTER
REVDAT 1 19-APR-05 1Z6T 0
JRNL AUTH S.J.RIEDL,W.LI,Y.CHAO,R.SCHWARZENBACHER,Y.SHI
JRNL TITL STRUCTURE OF THE APOPTOTIC PROTEASE-ACTIVATING FACTOR 1
JRNL TITL 2 BOUND TO ADP
JRNL REF NATURE V. 434 926 2005
JRNL REFN ISSN 0028-0836
JRNL PMID 15829969
JRNL DOI 10.1038/NATURE03465
REMARK 2
REMARK 2 RESOLUTION. 2.21 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.2
REMARK 3 NUMBER OF REFLECTIONS : 97722
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 5211
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.21
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.27
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3661
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 46.10
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE SET COUNT : 197
REMARK 3 BIN FREE R VALUE : 0.3020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 18752
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 108
REMARK 3 SOLVENT ATOMS : 803
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.18000
REMARK 3 B22 (A**2) : 0.40000
REMARK 3 B33 (A**2) : -0.17000
REMARK 3 B12 (A**2) : 0.13000
REMARK 3 B13 (A**2) : 0.77000
REMARK 3 B23 (A**2) : -0.45000
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): 0.256
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 19376 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 17608 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 26160 ; 1.431 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 41224 ; 0.872 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2340 ; 6.191 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 888 ;36.382 ;24.730
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3676 ;16.481 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 100 ;22.503 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2904 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 21084 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 3716 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4397 ; 0.209 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 17362 ; 0.181 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 9294 ; 0.175 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 10713 ; 0.088 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 856 ; 0.213 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 5 ; 0.230 ; 0.200
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): 62 ; 0.277 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 150 ; 0.261 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 29 ; 0.306 ; 0.200
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): 15178 ; 2.190 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4724 ; 0.239 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 18904 ; 2.682 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 9001 ; 4.687 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 7256 ; 6.432 ;11.000
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 : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 106 A 350 2
REMARK 3 1 B 106 B 350 2
REMARK 3 1 C 106 C 350 2
REMARK 3 1 D 106 D 350 2
REMARK 3 2 A 360 A 586 2
REMARK 3 2 B 360 B 586 2
REMARK 3 2 C 360 C 586 2
REMARK 3 2 D 360 D 586 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 2792 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 2792 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 2792 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 2792 ; 0.05 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 4583 ; 0.46 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 4583 ; 0.46 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 4583 ; 0.42 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 D (A): 4583 ; 0.51 ; 0.50
REMARK 3 TIGHT THERMAL 1 A (A**2): 2792 ; 0.13 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 2792 ; 0.13 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 2792 ; 0.13 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 2792 ; 0.13 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 4583 ; 0.72 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 4583 ; 0.71 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 4583 ; 0.73 ; 2.00
REMARK 3 MEDIUM THERMAL 1 D (A**2): 4583 ; 0.72 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 94
REMARK 3 RESIDUE RANGE : A 105 A 586
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4120 39.2170 84.2050
REMARK 3 T TENSOR
REMARK 3 T11: -0.0753 T22: 0.0163
REMARK 3 T33: -0.1035 T12: -0.0153
REMARK 3 T13: -0.0500 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 0.7802 L22: 0.6330
REMARK 3 L33: 0.4692 L12: 0.1530
REMARK 3 L13: -0.3697 L23: -0.0018
REMARK 3 S TENSOR
REMARK 3 S11: -0.0240 S12: 0.0069 S13: -0.0922
REMARK 3 S21: 0.0383 S22: -0.0563 S23: -0.0367
REMARK 3 S31: 0.0715 S32: -0.0575 S33: 0.0803
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 103
REMARK 3 RESIDUE RANGE : B 104 B 586
REMARK 3 ORIGIN FOR THE GROUP (A): -6.0090 62.5100 40.8440
REMARK 3 T TENSOR
REMARK 3 T11: -0.1076 T22: -0.0230
REMARK 3 T33: -0.1600 T12: -0.0254
REMARK 3 T13: -0.0856 T23: 0.0332
REMARK 3 L TENSOR
REMARK 3 L11: 1.4446 L22: 1.0327
REMARK 3 L33: 0.4451 L12: 0.5696
REMARK 3 L13: -0.5440 L23: -0.0899
REMARK 3 S TENSOR
REMARK 3 S11: -0.0417 S12: -0.0106 S13: 0.0104
REMARK 3 S21: -0.0531 S22: -0.0019 S23: -0.1254
REMARK 3 S31: 0.0268 S32: 0.0382 S33: 0.0436
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 103
REMARK 3 RESIDUE RANGE : C 104 C 586
REMARK 3 ORIGIN FOR THE GROUP (A): 31.9240 106.7390 41.5460
REMARK 3 T TENSOR
REMARK 3 T11: -0.0943 T22: -0.0198
REMARK 3 T33: -0.1571 T12: -0.0476
REMARK 3 T13: -0.0129 T23: 0.0346
REMARK 3 L TENSOR
REMARK 3 L11: 1.3781 L22: 1.0830
REMARK 3 L33: 0.3923 L12: -0.5424
REMARK 3 L13: 0.4549 L23: -0.1309
REMARK 3 S TENSOR
REMARK 3 S11: -0.0540 S12: 0.0054 S13: -0.0195
REMARK 3 S21: 0.0542 S22: -0.0003 S23: -0.1320
REMARK 3 S31: -0.0274 S32: 0.0470 S33: 0.0544
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 94
REMARK 3 RESIDUE RANGE : D 105 D 586
REMARK 3 ORIGIN FOR THE GROUP (A): 31.5290 80.3300 82.7890
REMARK 3 T TENSOR
REMARK 3 T11: -0.0923 T22: -0.0025
REMARK 3 T33: -0.1297 T12: -0.0595
REMARK 3 T13: -0.0376 T23: 0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 1.0170 L22: 0.8192
REMARK 3 L33: 0.5922 L12: -0.2051
REMARK 3 L13: 0.4061 L23: 0.0143
REMARK 3 S TENSOR
REMARK 3 S11: -0.0343 S12: -0.0123 S13: 0.1344
REMARK 3 S21: -0.0395 S22: -0.0782 S23: -0.0303
REMARK 3 S31: -0.0953 S32: -0.0737 S33: 0.1126
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS UNACCOUNTED DENSITY NEXT TO CYSTEINES A115, A450; B115,
REMARK 3 B450;C115,C450;D115,D450;
REMARK 4
REMARK 4 1Z6T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032370.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-04; NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0; NULL
REMARK 200 PH : 7.10
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : CHESS; CHESS
REMARK 200 BEAMLINE : A1; A1
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.954; 1.0088, 0.9500, 1.0053
REMARK 200 MONOCHROMATOR : X25; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; NULL
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 103300
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.5
REMARK 200 DATA REDUNDANCY : 1.700
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : 0.04800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 48.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.26700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, AMMONIUM ACETATE, PEG-3350, PH
REMARK 280 7.1, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 276K, PH 7.10
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 95
REMARK 465 SER A 96
REMARK 465 SER A 97
REMARK 465 SER A 98
REMARK 465 GLY A 99
REMARK 465 LYS A 100
REMARK 465 ASP A 101
REMARK 465 SER A 102
REMARK 465 VAL A 103
REMARK 465 SER A 104
REMARK 465 GLU A 587
REMARK 465 VAL A 588
REMARK 465 ASP A 589
REMARK 465 ASN A 590
REMARK 465 GLY A 591
REMARK 465 GLU B 587
REMARK 465 VAL B 588
REMARK 465 ASP B 589
REMARK 465 ASN B 590
REMARK 465 GLY B 591
REMARK 465 GLU C 587
REMARK 465 VAL C 588
REMARK 465 ASP C 589
REMARK 465 ASN C 590
REMARK 465 GLY C 591
REMARK 465 SER D 95
REMARK 465 SER D 96
REMARK 465 SER D 97
REMARK 465 SER D 98
REMARK 465 GLY D 99
REMARK 465 LYS D 100
REMARK 465 ASP D 101
REMARK 465 SER D 102
REMARK 465 VAL D 103
REMARK 465 SER D 104
REMARK 465 GLU D 587
REMARK 465 VAL D 588
REMARK 465 ASP D 589
REMARK 465 ASN D 590
REMARK 465 GLY D 591
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O PRO D 335 O HOH D 1050 1.82
REMARK 500 OE1 GLN D 121 O HOH D 912 1.84
REMARK 500 O GLN B 51 O HOH B 1008 1.99
REMARK 500 N VAL A 125 O HOH A 1019 2.00
REMARK 500 O HOH C 1004 O HOH C 1046 2.01
REMARK 500 NZ LYS A 192 O HOH A 961 2.02
REMARK 500 OE1 GLN C 579 O HOH C 945 2.03
REMARK 500 OE1 GLN B 579 O HOH B 930 2.03
REMARK 500 O HOH C 1014 O HOH C 1053 2.04
REMARK 500 OG SER C 272 O HOH C 969 2.06
REMARK 500 NE ARG B 13 O HOH B 1009 2.06
REMARK 500 O PRO A 321 O HOH A 970 2.11
REMARK 500 O HOH B 1052 O HOH B 1053 2.12
REMARK 500 CB MET B 55 O HOH B 1008 2.13
REMARK 500 OG SER C 256 O HOH C 1051 2.14
REMARK 500 OG SER D 256 O HOH D 1016 2.17
REMARK 500 OG SER A 325 O HOH A 970 2.17
REMARK 500 NZ LYS A 81 O HOH A 921 2.18
REMARK 500 OG1 THR D 573 O HOH D 934 2.18
REMARK 500 NH2 ARG A 44 O HOH A 1034 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD1 ASP D 360 O HOH C 1047 1546 1.97
REMARK 500 OD2 ASP D 360 O HOH C 1061 1546 2.10
REMARK 500 NE2 GLN A 469 O SER B 357 1546 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS B 450 CB CYS B 450 SG 0.106
REMARK 500 CYS C 450 CB CYS C 450 SG 0.151
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 205 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 205 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 PRO A 335 C - N - CA ANGL. DEV. = 10.2 DEGREES
REMARK 500 ARG D 205 NE - CZ - NH2 ANGL. DEV. = -3.4 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 LYS A 62 43.68 -94.04
REMARK 500 ASP A 64 172.61 -54.52
REMARK 500 VAL A 187 -71.67 -103.74
REMARK 500 ASP A 244 67.69 69.09
REMARK 500 LYS A 355 -79.47 -48.43
REMARK 500 SER A 357 -153.13 -163.99
REMARK 500 VAL B 187 -72.14 -104.27
REMARK 500 ASP B 244 69.38 67.43
REMARK 500 LYS C 18 -77.33 -55.96
REMARK 500 VAL C 187 -70.66 -102.85
REMARK 500 ASP C 209 -5.22 -59.96
REMARK 500 PHE C 212 -169.18 -126.63
REMARK 500 ASP C 244 68.96 65.91
REMARK 500 ASN C 347 79.29 -100.70
REMARK 500 LYS D 62 47.94 -95.83
REMARK 500 ASP D 64 177.59 -58.52
REMARK 500 TYR D 80 63.88 -103.36
REMARK 500 ASP D 89 -68.91 -17.95
REMARK 500 VAL D 187 -70.13 -105.30
REMARK 500 ASP D 244 69.50 67.95
REMARK 500 LYS D 355 85.58 -68.42
REMARK 500 SER D 356 -167.79 -104.25
REMARK 500 SER D 357 -94.49 -97.52
REMARK 500 SER D 358 -38.07 -24.88
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 ADP A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 903
DBREF 1Z6T A 1 591 UNP O14727 APAF_HUMAN 1 591
DBREF 1Z6T B 1 591 UNP O14727 APAF_HUMAN 1 591
DBREF 1Z6T C 1 591 UNP O14727 APAF_HUMAN 1 591
DBREF 1Z6T D 1 591 UNP O14727 APAF_HUMAN 1 591
SEQRES 1 A 591 MET ASP ALA LYS ALA ARG ASN CYS LEU LEU GLN HIS ARG
SEQRES 2 A 591 GLU ALA LEU GLU LYS ASP ILE LYS THR SER TYR ILE MET
SEQRES 3 A 591 ASP HIS MET ILE SER ASP GLY PHE LEU THR ILE SER GLU
SEQRES 4 A 591 GLU GLU LYS VAL ARG ASN GLU PRO THR GLN GLN GLN ARG
SEQRES 5 A 591 ALA ALA MET LEU ILE LYS MET ILE LEU LYS LYS ASP ASN
SEQRES 6 A 591 ASP SER TYR VAL SER PHE TYR ASN ALA LEU LEU HIS GLU
SEQRES 7 A 591 GLY TYR LYS ASP LEU ALA ALA LEU LEU HIS ASP GLY ILE
SEQRES 8 A 591 PRO VAL VAL SER SER SER SER GLY LYS ASP SER VAL SER
SEQRES 9 A 591 GLY ILE THR SER TYR VAL ARG THR VAL LEU CYS GLU GLY
SEQRES 10 A 591 GLY VAL PRO GLN ARG PRO VAL VAL PHE VAL THR ARG LYS
SEQRES 11 A 591 LYS LEU VAL ASN ALA ILE GLN GLN LYS LEU SER LYS LEU
SEQRES 12 A 591 LYS GLY GLU PRO GLY TRP VAL THR ILE HIS GLY MET ALA
SEQRES 13 A 591 GLY CYS GLY LYS SER VAL LEU ALA ALA GLU ALA VAL ARG
SEQRES 14 A 591 ASP HIS SER LEU LEU GLU GLY CYS PHE PRO GLY GLY VAL
SEQRES 15 A 591 HIS TRP VAL SER VAL GLY LYS GLN ASP LYS SER GLY LEU
SEQRES 16 A 591 LEU MET LYS LEU GLN ASN LEU CYS THR ARG LEU ASP GLN
SEQRES 17 A 591 ASP GLU SER PHE SER GLN ARG LEU PRO LEU ASN ILE GLU
SEQRES 18 A 591 GLU ALA LYS ASP ARG LEU ARG ILE LEU MET LEU ARG LYS
SEQRES 19 A 591 HIS PRO ARG SER LEU LEU ILE LEU ASP ASP VAL TRP ASP
SEQRES 20 A 591 SER TRP VAL LEU LYS ALA PHE ASP SER GLN CYS GLN ILE
SEQRES 21 A 591 LEU LEU THR THR ARG ASP LYS SER VAL THR ASP SER VAL
SEQRES 22 A 591 MET GLY PRO LYS TYR VAL VAL PRO VAL GLU SER SER LEU
SEQRES 23 A 591 GLY LYS GLU LYS GLY LEU GLU ILE LEU SER LEU PHE VAL
SEQRES 24 A 591 ASN MET LYS LYS ALA ASP LEU PRO GLU GLN ALA HIS SER
SEQRES 25 A 591 ILE ILE LYS GLU CYS LYS GLY SER PRO LEU VAL VAL SER
SEQRES 26 A 591 LEU ILE GLY ALA LEU LEU ARG ASP PHE PRO ASN ARG TRP
SEQRES 27 A 591 GLU TYR TYR LEU LYS GLN LEU GLN ASN LYS GLN PHE LYS
SEQRES 28 A 591 ARG ILE ARG LYS SER SER SER TYR ASP TYR GLU ALA LEU
SEQRES 29 A 591 ASP GLU ALA MET SER ILE SER VAL GLU MET LEU ARG GLU
SEQRES 30 A 591 ASP ILE LYS ASP TYR TYR THR ASP LEU SER ILE LEU GLN
SEQRES 31 A 591 LYS ASP VAL LYS VAL PRO THR LYS VAL LEU CYS ILE LEU
SEQRES 32 A 591 TRP ASP MET GLU THR GLU GLU VAL GLU ASP ILE LEU GLN
SEQRES 33 A 591 GLU PHE VAL ASN LYS SER LEU LEU PHE CYS ASP ARG ASN
SEQRES 34 A 591 GLY LYS SER PHE ARG TYR TYR LEU HIS ASP LEU GLN VAL
SEQRES 35 A 591 ASP PHE LEU THR GLU LYS ASN CYS SER GLN LEU GLN ASP
SEQRES 36 A 591 LEU HIS LYS LYS ILE ILE THR GLN PHE GLN ARG TYR HIS
SEQRES 37 A 591 GLN PRO HIS THR LEU SER PRO ASP GLN GLU ASP CYS MET
SEQRES 38 A 591 TYR TRP TYR ASN PHE LEU ALA TYR HIS MET ALA SER ALA
SEQRES 39 A 591 LYS MET HIS LYS GLU LEU CYS ALA LEU MET PHE SER LEU
SEQRES 40 A 591 ASP TRP ILE LYS ALA LYS THR GLU LEU VAL GLY PRO ALA
SEQRES 41 A 591 HIS LEU ILE HIS GLU PHE VAL GLU TYR ARG HIS ILE LEU
SEQRES 42 A 591 ASP GLU LYS ASP CYS ALA VAL SER GLU ASN PHE GLN GLU
SEQRES 43 A 591 PHE LEU SER LEU ASN GLY HIS LEU LEU GLY ARG GLN PRO
SEQRES 44 A 591 PHE PRO ASN ILE VAL GLN LEU GLY LEU CYS GLU PRO GLU
SEQRES 45 A 591 THR SER GLU VAL TYR GLN GLN ALA LYS LEU GLN ALA LYS
SEQRES 46 A 591 GLN GLU VAL ASP ASN GLY
SEQRES 1 B 591 MET ASP ALA LYS ALA ARG ASN CYS LEU LEU GLN HIS ARG
SEQRES 2 B 591 GLU ALA LEU GLU LYS ASP ILE LYS THR SER TYR ILE MET
SEQRES 3 B 591 ASP HIS MET ILE SER ASP GLY PHE LEU THR ILE SER GLU
SEQRES 4 B 591 GLU GLU LYS VAL ARG ASN GLU PRO THR GLN GLN GLN ARG
SEQRES 5 B 591 ALA ALA MET LEU ILE LYS MET ILE LEU LYS LYS ASP ASN
SEQRES 6 B 591 ASP SER TYR VAL SER PHE TYR ASN ALA LEU LEU HIS GLU
SEQRES 7 B 591 GLY TYR LYS ASP LEU ALA ALA LEU LEU HIS ASP GLY ILE
SEQRES 8 B 591 PRO VAL VAL SER SER SER SER GLY LYS ASP SER VAL SER
SEQRES 9 B 591 GLY ILE THR SER TYR VAL ARG THR VAL LEU CYS GLU GLY
SEQRES 10 B 591 GLY VAL PRO GLN ARG PRO VAL VAL PHE VAL THR ARG LYS
SEQRES 11 B 591 LYS LEU VAL ASN ALA ILE GLN GLN LYS LEU SER LYS LEU
SEQRES 12 B 591 LYS GLY GLU PRO GLY TRP VAL THR ILE HIS GLY MET ALA
SEQRES 13 B 591 GLY CYS GLY LYS SER VAL LEU ALA ALA GLU ALA VAL ARG
SEQRES 14 B 591 ASP HIS SER LEU LEU GLU GLY CYS PHE PRO GLY GLY VAL
SEQRES 15 B 591 HIS TRP VAL SER VAL GLY LYS GLN ASP LYS SER GLY LEU
SEQRES 16 B 591 LEU MET LYS LEU GLN ASN LEU CYS THR ARG LEU ASP GLN
SEQRES 17 B 591 ASP GLU SER PHE SER GLN ARG LEU PRO LEU ASN ILE GLU
SEQRES 18 B 591 GLU ALA LYS ASP ARG LEU ARG ILE LEU MET LEU ARG LYS
SEQRES 19 B 591 HIS PRO ARG SER LEU LEU ILE LEU ASP ASP VAL TRP ASP
SEQRES 20 B 591 SER TRP VAL LEU LYS ALA PHE ASP SER GLN CYS GLN ILE
SEQRES 21 B 591 LEU LEU THR THR ARG ASP LYS SER VAL THR ASP SER VAL
SEQRES 22 B 591 MET GLY PRO LYS TYR VAL VAL PRO VAL GLU SER SER LEU
SEQRES 23 B 591 GLY LYS GLU LYS GLY LEU GLU ILE LEU SER LEU PHE VAL
SEQRES 24 B 591 ASN MET LYS LYS ALA ASP LEU PRO GLU GLN ALA HIS SER
SEQRES 25 B 591 ILE ILE LYS GLU CYS LYS GLY SER PRO LEU VAL VAL SER
SEQRES 26 B 591 LEU ILE GLY ALA LEU LEU ARG ASP PHE PRO ASN ARG TRP
SEQRES 27 B 591 GLU TYR TYR LEU LYS GLN LEU GLN ASN LYS GLN PHE LYS
SEQRES 28 B 591 ARG ILE ARG LYS SER SER SER TYR ASP TYR GLU ALA LEU
SEQRES 29 B 591 ASP GLU ALA MET SER ILE SER VAL GLU MET LEU ARG GLU
SEQRES 30 B 591 ASP ILE LYS ASP TYR TYR THR ASP LEU SER ILE LEU GLN
SEQRES 31 B 591 LYS ASP VAL LYS VAL PRO THR LYS VAL LEU CYS ILE LEU
SEQRES 32 B 591 TRP ASP MET GLU THR GLU GLU VAL GLU ASP ILE LEU GLN
SEQRES 33 B 591 GLU PHE VAL ASN LYS SER LEU LEU PHE CYS ASP ARG ASN
SEQRES 34 B 591 GLY LYS SER PHE ARG TYR TYR LEU HIS ASP LEU GLN VAL
SEQRES 35 B 591 ASP PHE LEU THR GLU LYS ASN CYS SER GLN LEU GLN ASP
SEQRES 36 B 591 LEU HIS LYS LYS ILE ILE THR GLN PHE GLN ARG TYR HIS
SEQRES 37 B 591 GLN PRO HIS THR LEU SER PRO ASP GLN GLU ASP CYS MET
SEQRES 38 B 591 TYR TRP TYR ASN PHE LEU ALA TYR HIS MET ALA SER ALA
SEQRES 39 B 591 LYS MET HIS LYS GLU LEU CYS ALA LEU MET PHE SER LEU
SEQRES 40 B 591 ASP TRP ILE LYS ALA LYS THR GLU LEU VAL GLY PRO ALA
SEQRES 41 B 591 HIS LEU ILE HIS GLU PHE VAL GLU TYR ARG HIS ILE LEU
SEQRES 42 B 591 ASP GLU LYS ASP CYS ALA VAL SER GLU ASN PHE GLN GLU
SEQRES 43 B 591 PHE LEU SER LEU ASN GLY HIS LEU LEU GLY ARG GLN PRO
SEQRES 44 B 591 PHE PRO ASN ILE VAL GLN LEU GLY LEU CYS GLU PRO GLU
SEQRES 45 B 591 THR SER GLU VAL TYR GLN GLN ALA LYS LEU GLN ALA LYS
SEQRES 46 B 591 GLN GLU VAL ASP ASN GLY
SEQRES 1 C 591 MET ASP ALA LYS ALA ARG ASN CYS LEU LEU GLN HIS ARG
SEQRES 2 C 591 GLU ALA LEU GLU LYS ASP ILE LYS THR SER TYR ILE MET
SEQRES 3 C 591 ASP HIS MET ILE SER ASP GLY PHE LEU THR ILE SER GLU
SEQRES 4 C 591 GLU GLU LYS VAL ARG ASN GLU PRO THR GLN GLN GLN ARG
SEQRES 5 C 591 ALA ALA MET LEU ILE LYS MET ILE LEU LYS LYS ASP ASN
SEQRES 6 C 591 ASP SER TYR VAL SER PHE TYR ASN ALA LEU LEU HIS GLU
SEQRES 7 C 591 GLY TYR LYS ASP LEU ALA ALA LEU LEU HIS ASP GLY ILE
SEQRES 8 C 591 PRO VAL VAL SER SER SER SER GLY LYS ASP SER VAL SER
SEQRES 9 C 591 GLY ILE THR SER TYR VAL ARG THR VAL LEU CYS GLU GLY
SEQRES 10 C 591 GLY VAL PRO GLN ARG PRO VAL VAL PHE VAL THR ARG LYS
SEQRES 11 C 591 LYS LEU VAL ASN ALA ILE GLN GLN LYS LEU SER LYS LEU
SEQRES 12 C 591 LYS GLY GLU PRO GLY TRP VAL THR ILE HIS GLY MET ALA
SEQRES 13 C 591 GLY CYS GLY LYS SER VAL LEU ALA ALA GLU ALA VAL ARG
SEQRES 14 C 591 ASP HIS SER LEU LEU GLU GLY CYS PHE PRO GLY GLY VAL
SEQRES 15 C 591 HIS TRP VAL SER VAL GLY LYS GLN ASP LYS SER GLY LEU
SEQRES 16 C 591 LEU MET LYS LEU GLN ASN LEU CYS THR ARG LEU ASP GLN
SEQRES 17 C 591 ASP GLU SER PHE SER GLN ARG LEU PRO LEU ASN ILE GLU
SEQRES 18 C 591 GLU ALA LYS ASP ARG LEU ARG ILE LEU MET LEU ARG LYS
SEQRES 19 C 591 HIS PRO ARG SER LEU LEU ILE LEU ASP ASP VAL TRP ASP
SEQRES 20 C 591 SER TRP VAL LEU LYS ALA PHE ASP SER GLN CYS GLN ILE
SEQRES 21 C 591 LEU LEU THR THR ARG ASP LYS SER VAL THR ASP SER VAL
SEQRES 22 C 591 MET GLY PRO LYS TYR VAL VAL PRO VAL GLU SER SER LEU
SEQRES 23 C 591 GLY LYS GLU LYS GLY LEU GLU ILE LEU SER LEU PHE VAL
SEQRES 24 C 591 ASN MET LYS LYS ALA ASP LEU PRO GLU GLN ALA HIS SER
SEQRES 25 C 591 ILE ILE LYS GLU CYS LYS GLY SER PRO LEU VAL VAL SER
SEQRES 26 C 591 LEU ILE GLY ALA LEU LEU ARG ASP PHE PRO ASN ARG TRP
SEQRES 27 C 591 GLU TYR TYR LEU LYS GLN LEU GLN ASN LYS GLN PHE LYS
SEQRES 28 C 591 ARG ILE ARG LYS SER SER SER TYR ASP TYR GLU ALA LEU
SEQRES 29 C 591 ASP GLU ALA MET SER ILE SER VAL GLU MET LEU ARG GLU
SEQRES 30 C 591 ASP ILE LYS ASP TYR TYR THR ASP LEU SER ILE LEU GLN
SEQRES 31 C 591 LYS ASP VAL LYS VAL PRO THR LYS VAL LEU CYS ILE LEU
SEQRES 32 C 591 TRP ASP MET GLU THR GLU GLU VAL GLU ASP ILE LEU GLN
SEQRES 33 C 591 GLU PHE VAL ASN LYS SER LEU LEU PHE CYS ASP ARG ASN
SEQRES 34 C 591 GLY LYS SER PHE ARG TYR TYR LEU HIS ASP LEU GLN VAL
SEQRES 35 C 591 ASP PHE LEU THR GLU LYS ASN CYS SER GLN LEU GLN ASP
SEQRES 36 C 591 LEU HIS LYS LYS ILE ILE THR GLN PHE GLN ARG TYR HIS
SEQRES 37 C 591 GLN PRO HIS THR LEU SER PRO ASP GLN GLU ASP CYS MET
SEQRES 38 C 591 TYR TRP TYR ASN PHE LEU ALA TYR HIS MET ALA SER ALA
SEQRES 39 C 591 LYS MET HIS LYS GLU LEU CYS ALA LEU MET PHE SER LEU
SEQRES 40 C 591 ASP TRP ILE LYS ALA LYS THR GLU LEU VAL GLY PRO ALA
SEQRES 41 C 591 HIS LEU ILE HIS GLU PHE VAL GLU TYR ARG HIS ILE LEU
SEQRES 42 C 591 ASP GLU LYS ASP CYS ALA VAL SER GLU ASN PHE GLN GLU
SEQRES 43 C 591 PHE LEU SER LEU ASN GLY HIS LEU LEU GLY ARG GLN PRO
SEQRES 44 C 591 PHE PRO ASN ILE VAL GLN LEU GLY LEU CYS GLU PRO GLU
SEQRES 45 C 591 THR SER GLU VAL TYR GLN GLN ALA LYS LEU GLN ALA LYS
SEQRES 46 C 591 GLN GLU VAL ASP ASN GLY
SEQRES 1 D 591 MET ASP ALA LYS ALA ARG ASN CYS LEU LEU GLN HIS ARG
SEQRES 2 D 591 GLU ALA LEU GLU LYS ASP ILE LYS THR SER TYR ILE MET
SEQRES 3 D 591 ASP HIS MET ILE SER ASP GLY PHE LEU THR ILE SER GLU
SEQRES 4 D 591 GLU GLU LYS VAL ARG ASN GLU PRO THR GLN GLN GLN ARG
SEQRES 5 D 591 ALA ALA MET LEU ILE LYS MET ILE LEU LYS LYS ASP ASN
SEQRES 6 D 591 ASP SER TYR VAL SER PHE TYR ASN ALA LEU LEU HIS GLU
SEQRES 7 D 591 GLY TYR LYS ASP LEU ALA ALA LEU LEU HIS ASP GLY ILE
SEQRES 8 D 591 PRO VAL VAL SER SER SER SER GLY LYS ASP SER VAL SER
SEQRES 9 D 591 GLY ILE THR SER TYR VAL ARG THR VAL LEU CYS GLU GLY
SEQRES 10 D 591 GLY VAL PRO GLN ARG PRO VAL VAL PHE VAL THR ARG LYS
SEQRES 11 D 591 LYS LEU VAL ASN ALA ILE GLN GLN LYS LEU SER LYS LEU
SEQRES 12 D 591 LYS GLY GLU PRO GLY TRP VAL THR ILE HIS GLY MET ALA
SEQRES 13 D 591 GLY CYS GLY LYS SER VAL LEU ALA ALA GLU ALA VAL ARG
SEQRES 14 D 591 ASP HIS SER LEU LEU GLU GLY CYS PHE PRO GLY GLY VAL
SEQRES 15 D 591 HIS TRP VAL SER VAL GLY LYS GLN ASP LYS SER GLY LEU
SEQRES 16 D 591 LEU MET LYS LEU GLN ASN LEU CYS THR ARG LEU ASP GLN
SEQRES 17 D 591 ASP GLU SER PHE SER GLN ARG LEU PRO LEU ASN ILE GLU
SEQRES 18 D 591 GLU ALA LYS ASP ARG LEU ARG ILE LEU MET LEU ARG LYS
SEQRES 19 D 591 HIS PRO ARG SER LEU LEU ILE LEU ASP ASP VAL TRP ASP
SEQRES 20 D 591 SER TRP VAL LEU LYS ALA PHE ASP SER GLN CYS GLN ILE
SEQRES 21 D 591 LEU LEU THR THR ARG ASP LYS SER VAL THR ASP SER VAL
SEQRES 22 D 591 MET GLY PRO LYS TYR VAL VAL PRO VAL GLU SER SER LEU
SEQRES 23 D 591 GLY LYS GLU LYS GLY LEU GLU ILE LEU SER LEU PHE VAL
SEQRES 24 D 591 ASN MET LYS LYS ALA ASP LEU PRO GLU GLN ALA HIS SER
SEQRES 25 D 591 ILE ILE LYS GLU CYS LYS GLY SER PRO LEU VAL VAL SER
SEQRES 26 D 591 LEU ILE GLY ALA LEU LEU ARG ASP PHE PRO ASN ARG TRP
SEQRES 27 D 591 GLU TYR TYR LEU LYS GLN LEU GLN ASN LYS GLN PHE LYS
SEQRES 28 D 591 ARG ILE ARG LYS SER SER SER TYR ASP TYR GLU ALA LEU
SEQRES 29 D 591 ASP GLU ALA MET SER ILE SER VAL GLU MET LEU ARG GLU
SEQRES 30 D 591 ASP ILE LYS ASP TYR TYR THR ASP LEU SER ILE LEU GLN
SEQRES 31 D 591 LYS ASP VAL LYS VAL PRO THR LYS VAL LEU CYS ILE LEU
SEQRES 32 D 591 TRP ASP MET GLU THR GLU GLU VAL GLU ASP ILE LEU GLN
SEQRES 33 D 591 GLU PHE VAL ASN LYS SER LEU LEU PHE CYS ASP ARG ASN
SEQRES 34 D 591 GLY LYS SER PHE ARG TYR TYR LEU HIS ASP LEU GLN VAL
SEQRES 35 D 591 ASP PHE LEU THR GLU LYS ASN CYS SER GLN LEU GLN ASP
SEQRES 36 D 591 LEU HIS LYS LYS ILE ILE THR GLN PHE GLN ARG TYR HIS
SEQRES 37 D 591 GLN PRO HIS THR LEU SER PRO ASP GLN GLU ASP CYS MET
SEQRES 38 D 591 TYR TRP TYR ASN PHE LEU ALA TYR HIS MET ALA SER ALA
SEQRES 39 D 591 LYS MET HIS LYS GLU LEU CYS ALA LEU MET PHE SER LEU
SEQRES 40 D 591 ASP TRP ILE LYS ALA LYS THR GLU LEU VAL GLY PRO ALA
SEQRES 41 D 591 HIS LEU ILE HIS GLU PHE VAL GLU TYR ARG HIS ILE LEU
SEQRES 42 D 591 ASP GLU LYS ASP CYS ALA VAL SER GLU ASN PHE GLN GLU
SEQRES 43 D 591 PHE LEU SER LEU ASN GLY HIS LEU LEU GLY ARG GLN PRO
SEQRES 44 D 591 PHE PRO ASN ILE VAL GLN LEU GLY LEU CYS GLU PRO GLU
SEQRES 45 D 591 THR SER GLU VAL TYR GLN GLN ALA LYS LEU GLN ALA LYS
SEQRES 46 D 591 GLN GLU VAL ASP ASN GLY
HET ADP A 900 27
HET ADP B 901 27
HET ADP C 902 27
HET ADP D 903 27
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL 5 ADP 4(C10 H15 N5 O10 P2)
FORMUL 9 HOH *803(H2 O)
HELIX 1 1 ASP A 2 HIS A 12 1 11
HELIX 2 2 HIS A 12 ILE A 20 1 9
HELIX 3 3 LYS A 21 ASP A 32 1 12
HELIX 4 4 THR A 36 ASN A 45 1 10
HELIX 5 5 THR A 48 LYS A 62 1 15
HELIX 6 6 ASP A 64 GLY A 79 1 16
HELIX 7 7 TYR A 80 ASP A 89 1 10
HELIX 8 8 THR A 107 GLY A 117 1 11
HELIX 9 9 ARG A 129 SER A 141 1 13
HELIX 10 10 GLY A 159 ARG A 169 1 11
HELIX 11 11 ASP A 170 PHE A 178 1 9
HELIX 12 12 ASP A 191 ASP A 207 1 17
HELIX 13 13 ASN A 219 LYS A 234 1 16
HELIX 14 14 ASP A 247 ALA A 253 1 7
HELIX 15 15 ASP A 266 ASP A 271 5 6
HELIX 16 16 GLY A 287 ASN A 300 1 14
HELIX 17 17 LYS A 302 PRO A 307 5 6
HELIX 18 18 GLU A 308 CYS A 317 1 10
HELIX 19 19 SER A 320 PHE A 334 1 15
HELIX 20 20 ARG A 337 ASN A 347 1 11
HELIX 21 21 TYR A 361 MET A 374 1 14
HELIX 22 22 ILE A 379 LEU A 386 1 8
HELIX 23 23 SER A 387 LEU A 389 5 3
HELIX 24 24 THR A 397 ASP A 405 1 9
HELIX 25 25 GLU A 407 LYS A 421 1 15
HELIX 26 26 HIS A 438 ASN A 449 1 12
HELIX 27 27 GLN A 452 GLN A 465 1 14
HELIX 28 28 GLN A 469 LEU A 473 5 5
HELIX 29 29 ASP A 479 ALA A 494 1 16
HELIX 30 30 MET A 496 PHE A 505 1 10
HELIX 31 31 SER A 506 GLY A 518 1 13
HELIX 32 32 PRO A 519 TYR A 529 1 11
HELIX 33 33 ARG A 530 LEU A 533 5 4
HELIX 34 34 ASP A 534 ASN A 551 1 18
HELIX 35 35 ASN A 562 LEU A 568 1 7
HELIX 36 36 SER A 574 GLN A 586 1 13
HELIX 37 37 ASP B 2 ILE B 20 1 19
HELIX 38 38 THR B 22 GLY B 33 1 12
HELIX 39 39 THR B 36 ASN B 45 1 10
HELIX 40 40 THR B 48 LEU B 61 1 14
HELIX 41 41 ASP B 64 GLU B 78 1 15
HELIX 42 42 TYR B 80 ASP B 89 1 10
HELIX 43 43 GLY B 90 ILE B 91 5 2
HELIX 44 44 PRO B 92 SER B 96 5 5
HELIX 45 45 SER B 98 GLY B 105 1 8
HELIX 46 46 THR B 107 GLY B 118 1 12
HELIX 47 47 ARG B 129 SER B 141 1 13
HELIX 48 48 GLY B 159 VAL B 168 1 10
HELIX 49 49 ASP B 170 PHE B 178 1 9
HELIX 50 50 ASP B 191 ASP B 207 1 17
HELIX 51 51 ASN B 219 LYS B 234 1 16
HELIX 52 52 ASP B 247 ALA B 253 1 7
HELIX 53 53 ASP B 266 ASP B 271 5 6
HELIX 54 54 GLY B 287 ASN B 300 1 14
HELIX 55 55 LYS B 302 PRO B 307 5 6
HELIX 56 56 GLU B 308 LYS B 318 1 11
HELIX 57 57 SER B 320 PHE B 334 1 15
HELIX 58 58 ARG B 337 ASN B 347 1 11
HELIX 59 59 TYR B 361 MET B 374 1 14
HELIX 60 60 ARG B 376 LEU B 386 1 11
HELIX 61 61 SER B 387 LEU B 389 5 3
HELIX 62 62 THR B 397 ASP B 405 1 9
HELIX 63 63 GLU B 407 LYS B 421 1 15
HELIX 64 64 HIS B 438 ASN B 449 1 12
HELIX 65 65 GLN B 452 GLN B 465 1 14
HELIX 66 66 GLN B 469 LEU B 473 5 5
HELIX 67 67 ASP B 479 ALA B 494 1 16
HELIX 68 68 MET B 496 PHE B 505 1 10
HELIX 69 69 SER B 506 GLY B 518 1 13
HELIX 70 70 PRO B 519 ARG B 530 1 12
HELIX 71 71 HIS B 531 LEU B 533 5 3
HELIX 72 72 ASP B 534 ASN B 551 1 18
HELIX 73 73 ASN B 562 LEU B 568 1 7
HELIX 74 74 SER B 574 GLN B 586 1 13
HELIX 75 75 ASP C 2 ILE C 20 1 19
HELIX 76 76 THR C 22 GLY C 33 1 12
HELIX 77 77 THR C 36 ASN C 45 1 10
HELIX 78 78 THR C 48 LEU C 61 1 14
HELIX 79 79 ASP C 64 GLU C 78 1 15
HELIX 80 80 TYR C 80 HIS C 88 1 9
HELIX 81 81 ASP C 89 ILE C 91 5 3
HELIX 82 82 PRO C 92 SER C 96 5 5
HELIX 83 83 SER C 98 GLY C 105 1 8
HELIX 84 84 THR C 107 GLY C 117 1 11
HELIX 85 85 ARG C 129 SER C 141 1 13
HELIX 86 86 GLY C 159 ARG C 169 1 11
HELIX 87 87 ASP C 170 PHE C 178 1 9
HELIX 88 88 ASP C 191 ASP C 207 1 17
HELIX 89 89 ASN C 219 LYS C 234 1 16
HELIX 90 90 ASP C 247 ALA C 253 1 7
HELIX 91 91 ASP C 266 ASP C 271 5 6
HELIX 92 92 GLY C 287 ASN C 300 1 14
HELIX 93 93 LYS C 302 PRO C 307 5 6
HELIX 94 94 GLU C 308 LYS C 318 1 11
HELIX 95 95 SER C 320 PHE C 334 1 15
HELIX 96 96 ARG C 337 ASN C 347 1 11
HELIX 97 97 TYR C 361 MET C 374 1 14
HELIX 98 98 ARG C 376 LEU C 386 1 11
HELIX 99 99 SER C 387 LEU C 389 5 3
HELIX 100 100 THR C 397 ASP C 405 1 9
HELIX 101 101 GLU C 407 LYS C 421 1 15
HELIX 102 102 HIS C 438 ASN C 449 1 12
HELIX 103 103 GLN C 452 GLN C 465 1 14
HELIX 104 104 GLN C 469 LEU C 473 5 5
HELIX 105 105 ASP C 479 ALA C 494 1 16
HELIX 106 106 MET C 496 PHE C 505 1 10
HELIX 107 107 SER C 506 GLY C 518 1 13
HELIX 108 108 PRO C 519 ARG C 530 1 12
HELIX 109 109 HIS C 531 LEU C 533 5 3
HELIX 110 110 ASP C 534 ASN C 551 1 18
HELIX 111 111 ASN C 562 LEU C 568 1 7
HELIX 112 112 SER C 574 GLN C 586 1 13
HELIX 113 113 ASP D 2 ILE D 20 1 19
HELIX 114 114 THR D 22 ASP D 32 1 11
HELIX 115 115 THR D 36 GLU D 46 1 11
HELIX 116 116 THR D 48 LEU D 61 1 14
HELIX 117 117 ASP D 64 GLU D 78 1 15
HELIX 118 118 TYR D 80 ASP D 89 1 10
HELIX 119 119 THR D 107 GLY D 117 1 11
HELIX 120 120 ARG D 129 SER D 141 1 13
HELIX 121 121 GLY D 159 ARG D 169 1 11
HELIX 122 122 ASP D 170 PHE D 178 1 9
HELIX 123 123 ASP D 191 ASP D 207 1 17
HELIX 124 124 ASN D 219 LYS D 234 1 16
HELIX 125 125 ASP D 247 ALA D 253 1 7
HELIX 126 126 ASP D 266 ASP D 271 5 6
HELIX 127 127 GLY D 287 ASN D 300 1 14
HELIX 128 128 LYS D 302 PRO D 307 5 6
HELIX 129 129 GLU D 308 CYS D 317 1 10
HELIX 130 130 SER D 320 PHE D 334 1 15
HELIX 131 131 ARG D 337 ASN D 347 1 11
HELIX 132 132 TYR D 361 MET D 374 1 14
HELIX 133 133 ILE D 379 LEU D 386 1 8
HELIX 134 134 SER D 387 LEU D 389 5 3
HELIX 135 135 THR D 397 ASP D 405 1 9
HELIX 136 136 GLU D 407 LYS D 421 1 15
HELIX 137 137 HIS D 438 ASN D 449 1 12
HELIX 138 138 GLN D 452 GLN D 465 1 14
HELIX 139 139 GLN D 469 LEU D 473 5 5
HELIX 140 140 ASP D 479 ALA D 494 1 16
HELIX 141 141 MET D 496 PHE D 505 1 10
HELIX 142 142 SER D 506 GLY D 518 1 13
HELIX 143 143 PRO D 519 ARG D 530 1 12
HELIX 144 144 HIS D 531 LEU D 533 5 3
HELIX 145 145 ASP D 534 ASN D 551 1 18
HELIX 146 146 ASN D 562 LEU D 568 1 7
HELIX 147 147 SER D 574 GLN D 586 1 13
SHEET 1 A 5 VAL A 182 GLY A 188 0
SHEET 2 A 5 LEU A 239 VAL A 245 1 O ILE A 241 N VAL A 185
SHEET 3 A 5 GLN A 259 THR A 264 1 O LEU A 261 N LEU A 242
SHEET 4 A 5 GLY A 148 HIS A 153 1 N ILE A 152 O LEU A 262
SHEET 5 A 5 LYS A 277 PRO A 281 1 O VAL A 280 N THR A 151
SHEET 1 B 3 VAL A 395 PRO A 396 0
SHEET 2 B 3 SER A 432 TYR A 436 -1 O TYR A 435 N VAL A 395
SHEET 3 B 3 PHE A 425 ASN A 429 -1 N ASP A 427 O ARG A 434
SHEET 1 C 5 VAL B 182 SER B 186 0
SHEET 2 C 5 LEU B 239 ASP B 243 1 O ILE B 241 N VAL B 185
SHEET 3 C 5 GLN B 259 THR B 264 1 O LEU B 261 N LEU B 242
SHEET 4 C 5 GLY B 148 HIS B 153 1 N ILE B 152 O LEU B 262
SHEET 5 C 5 LYS B 277 PRO B 281 1 O TYR B 278 N THR B 151
SHEET 1 D 3 VAL B 395 PRO B 396 0
SHEET 2 D 3 SER B 432 TYR B 436 -1 O TYR B 435 N VAL B 395
SHEET 3 D 3 PHE B 425 ASN B 429 -1 N PHE B 425 O TYR B 436
SHEET 1 E 5 VAL C 182 GLY C 188 0
SHEET 2 E 5 LEU C 239 VAL C 245 1 O ILE C 241 N VAL C 185
SHEET 3 E 5 GLN C 259 THR C 264 1 O LEU C 261 N LEU C 240
SHEET 4 E 5 GLY C 148 HIS C 153 1 N ILE C 152 O LEU C 262
SHEET 5 E 5 LYS C 277 PRO C 281 1 O VAL C 280 N THR C 151
SHEET 1 F 3 VAL C 395 PRO C 396 0
SHEET 2 F 3 SER C 432 TYR C 436 -1 O TYR C 435 N VAL C 395
SHEET 3 F 3 PHE C 425 ASN C 429 -1 N PHE C 425 O TYR C 436
SHEET 1 G 5 VAL D 182 SER D 186 0
SHEET 2 G 5 LEU D 239 ASP D 243 1 O ILE D 241 N VAL D 185
SHEET 3 G 5 GLN D 259 THR D 264 1 O LEU D 261 N LEU D 242
SHEET 4 G 5 GLY D 148 HIS D 153 1 N ILE D 152 O LEU D 262
SHEET 5 G 5 LYS D 277 PRO D 281 1 O VAL D 280 N THR D 151
SHEET 1 H 3 VAL D 395 PRO D 396 0
SHEET 2 H 3 SER D 432 TYR D 436 -1 O TYR D 435 N VAL D 395
SHEET 3 H 3 PHE D 425 ASN D 429 -1 N PHE D 425 O TYR D 436
CISPEP 1 GLN A 558 PRO A 559 0 -6.31
CISPEP 2 GLN B 558 PRO B 559 0 -4.59
CISPEP 3 GLN C 558 PRO C 559 0 -2.10
CISPEP 4 GLN D 558 PRO D 559 0 -8.47
SITE 1 AC1 22 VAL A 125 PHE A 126 VAL A 127 ARG A 129
SITE 2 AC1 22 GLY A 157 CYS A 158 GLY A 159 LYS A 160
SITE 3 AC1 22 SER A 161 VAL A 162 PRO A 321 LEU A 322
SITE 4 AC1 22 PHE A 425 HIS A 438 HOH A 928 HOH A 970
SITE 5 AC1 22 HOH A1074 HOH A1075 HOH A1076 HOH A1077
SITE 6 AC1 22 HOH A1078 HOH A1079
SITE 1 AC2 17 VAL B 125 PHE B 126 VAL B 127 GLY B 157
SITE 2 AC2 17 CYS B 158 GLY B 159 LYS B 160 SER B 161
SITE 3 AC2 17 VAL B 162 PRO B 321 LEU B 322 PHE B 425
SITE 4 AC2 17 HIS B 438 HOH B 986 HOH B1017 HOH B1059
SITE 5 AC2 17 HOH B1093
SITE 1 AC3 16 VAL C 125 PHE C 126 VAL C 127 GLY C 157
SITE 2 AC3 16 CYS C 158 GLY C 159 LYS C 160 SER C 161
SITE 3 AC3 16 VAL C 162 PRO C 321 LEU C 322 PHE C 425
SITE 4 AC3 16 HIS C 438 HOH C 937 HOH C1009 HOH C1081
SITE 1 AC4 20 VAL D 125 PHE D 126 VAL D 127 ARG D 129
SITE 2 AC4 20 GLY D 157 CYS D 158 GLY D 159 LYS D 160
SITE 3 AC4 20 SER D 161 VAL D 162 PRO D 321 LEU D 322
SITE 4 AC4 20 PHE D 425 HIS D 438 HOH D 965 HOH D 977
SITE 5 AC4 20 HOH D 978 HOH D1007 HOH D1032 HOH D1036
CRYST1 75.955 92.883 94.988 62.96 89.99 90.05 P 1 4
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 0.013166 0.000011 -0.000009 0.00000
SCALE2 0.000000 0.010766 -0.005496 0.00000
SCALE3 0.000000 0.000000 0.011820 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
