HEADER HYDROLASE 24-NOV-15 5FOO
TITLE 6-PHOSPHO-BETA-GLUCOSIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 6-PHOSPHO-BETA-D GLYCOSIDASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 EC: 3.2.1.21, 3.2.1.86;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PYOGENES;
SOURCE 3 ORGANISM_TAXID: 160490;
SOURCE 4 STRAIN: M1 GAS;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET30
KEYWDS HYDROLASE, GLYCOSIDE HYDROLASE, CYCLOPHELLITOL, GLUCOSE 6-PHOSPHATE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.JIN,D.H.KWAN,S.G.WITHERS,G.J.DAVIES
REVDAT 3 10-JAN-24 5FOO 1 REMARK LINK
REVDAT 2 02-MAR-16 5FOO 1 JRNL
REVDAT 1 17-FEB-16 5FOO 0
JRNL AUTH D.H.KWAN,Y.JIN,J.JIANG,H.CHEN,M.P.KOTZLER,H.S.OVERKLEEFT,
JRNL AUTH 2 G.J.DAVIES,S.G.WITHERS
JRNL TITL CHEMOENZYMATIC SYNTHESIS OF 6-PHOSPHO-CYCLOPHELLITOL AS A
JRNL TITL 2 NOVEL PROBE OF 6-PHOSPHO-BETA-GLUCOSIDASES.
JRNL REF FEBS LETT. V. 590 461 2016
JRNL REFN ISSN 0014-5793
JRNL PMID 26790390
JRNL DOI 10.1002/1873-3468.12059
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 158.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 195049
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 10459
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 14435
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE SET COUNT : 718
REMARK 3 BIN FREE R VALUE : 0.3140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 22644
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 213
REMARK 3 SOLVENT ATOMS : 981
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.99000
REMARK 3 B22 (A**2) : 0.43000
REMARK 3 B33 (A**2) : -1.41000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.15000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.182
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.164
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.128
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.019
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 23590 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 21281 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 32157 ; 1.843 ; 1.932
REMARK 3 BOND ANGLES OTHERS (DEGREES): 48843 ; 1.116 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2772 ;10.899 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1223 ;37.726 ;23.769
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3531 ;14.118 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 126 ;17.969 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3282 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 26918 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 5940 ; 0.002 ; 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): 11107 ; 2.891 ; 3.474
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 11105 ; 2.889 ; 3.474
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13872 ; 3.755 ; 5.195
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 12483 ; 3.628 ; 3.735
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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.
REMARK 4
REMARK 4 5FOO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1290065608.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-APR-14
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 205534
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 49.470
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.900
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.62000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 4B3K
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.33 MM SPY1599 WAS REACTED WITH 4.2
REMARK 280 MM 6-PHOSPHO-CYCLOPHELLITOL EPOXIDE IN THE BUFFER OF 50 MM HEPES
REMARK 280 AND 150 MM NACL, PH 7.0, BEFORE BEING MIXED WITH THE SAME VOLUME
REMARK 280 OF BUFFER OF 0.1 M BIS TRIS PROPANE PH7.5, 20% PEG 3350 AND 0.15
REMARK 280 M NABR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 54.94950
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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 464
REMARK 465 LEU A 465
REMARK 465 GLU A 466
REMARK 465 VAL A 467
REMARK 465 MET A 468
REMARK 465 GLU A 469
REMARK 465 GLU A 470
REMARK 465 PHE A 471
REMARK 465 GLY A 472
REMARK 465 GLY A 473
REMARK 465 SER A 474
REMARK 465 ALA A 475
REMARK 465 SER A 476
REMARK 465 HIS A 477
REMARK 465 LEU A 478
REMARK 465 SER A 479
REMARK 465 ASP A 480
REMARK 465 SER B 464
REMARK 465 LEU B 465
REMARK 465 GLU B 466
REMARK 465 VAL B 467
REMARK 465 MET B 468
REMARK 465 GLU B 469
REMARK 465 GLU B 470
REMARK 465 PHE B 471
REMARK 465 GLY B 472
REMARK 465 GLY B 473
REMARK 465 SER B 474
REMARK 465 ALA B 475
REMARK 465 SER B 476
REMARK 465 HIS B 477
REMARK 465 LEU B 478
REMARK 465 SER B 479
REMARK 465 ASP B 480
REMARK 465 SER C 464
REMARK 465 LEU C 465
REMARK 465 GLU C 466
REMARK 465 VAL C 467
REMARK 465 MET C 468
REMARK 465 GLU C 469
REMARK 465 GLU C 470
REMARK 465 PHE C 471
REMARK 465 GLY C 472
REMARK 465 GLY C 473
REMARK 465 SER C 474
REMARK 465 ALA C 475
REMARK 465 SER C 476
REMARK 465 HIS C 477
REMARK 465 LEU C 478
REMARK 465 SER C 479
REMARK 465 ASP C 480
REMARK 465 SER D 464
REMARK 465 LEU D 465
REMARK 465 GLU D 466
REMARK 465 VAL D 467
REMARK 465 MET D 468
REMARK 465 GLU D 469
REMARK 465 GLU D 470
REMARK 465 PHE D 471
REMARK 465 GLY D 472
REMARK 465 GLY D 473
REMARK 465 SER D 474
REMARK 465 ALA D 475
REMARK 465 SER D 476
REMARK 465 HIS D 477
REMARK 465 LEU D 478
REMARK 465 SER D 479
REMARK 465 ASP D 480
REMARK 465 SER E 464
REMARK 465 LEU E 465
REMARK 465 GLU E 466
REMARK 465 VAL E 467
REMARK 465 MET E 468
REMARK 465 GLU E 469
REMARK 465 GLU E 470
REMARK 465 PHE E 471
REMARK 465 GLY E 472
REMARK 465 GLY E 473
REMARK 465 SER E 474
REMARK 465 ALA E 475
REMARK 465 SER E 476
REMARK 465 HIS E 477
REMARK 465 LEU E 478
REMARK 465 SER E 479
REMARK 465 ASP E 480
REMARK 465 ILE F 463
REMARK 465 SER F 464
REMARK 465 LEU F 465
REMARK 465 GLU F 466
REMARK 465 VAL F 467
REMARK 465 MET F 468
REMARK 465 GLU F 469
REMARK 465 GLU F 470
REMARK 465 PHE F 471
REMARK 465 GLY F 472
REMARK 465 GLY F 473
REMARK 465 SER F 474
REMARK 465 ALA F 475
REMARK 465 SER F 476
REMARK 465 HIS F 477
REMARK 465 LEU F 478
REMARK 465 SER F 479
REMARK 465 ASP F 480
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 260 CD CE NZ
REMARK 470 LYS A 302 CD CE NZ
REMARK 470 GLU A 380 CG CD OE1 OE2
REMARK 470 LYS B 260 CD CE NZ
REMARK 470 LYS B 270 CE NZ
REMARK 470 LYS C 260 CD CE NZ
REMARK 470 LYS C 302 CD CE NZ
REMARK 470 LYS C 455 CD CE NZ
REMARK 470 LYS D 302 CE NZ
REMARK 470 LYS E 260 CG CD CE NZ
REMARK 470 LYS E 455 CD CE NZ
REMARK 470 LYS F 270 CD CE NZ
REMARK 470 LYS F 302 CG CD CE NZ
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 OH TYR B 451 O HOH B 2223 2.02
REMARK 500 O HOH B 2091 O HOH B 2092 2.02
REMARK 500 O HOH B 2016 O HOH B 2040 2.07
REMARK 500 O GLU B 320 O HOH B 2160 2.19
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 GLU A 171 CD GLU A 171 OE2 0.074
REMARK 500 GLU A 366 CD GLU A 366 OE2 0.095
REMARK 500 GLU B 366 CD GLU B 366 OE2 0.096
REMARK 500 GLU C 171 CD GLU C 171 OE2 0.072
REMARK 500 GLU C 366 CD GLU C 366 OE1 -0.070
REMARK 500 GLU C 366 CD GLU C 366 OE2 0.077
REMARK 500 GLU E 366 CD GLU E 366 OE2 0.107
REMARK 500 GLU F 366 CD GLU F 366 OE2 0.103
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 22 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 28 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP A 292 CB - CG - OD1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP A 292 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG A 332 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 378 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 PRO B 181 C - N - CD ANGL. DEV. = -14.4 DEGREES
REMARK 500 MET C 176 CG - SD - CE ANGL. DEV. = 19.1 DEGREES
REMARK 500 ASP C 292 CB - CG - OD1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP C 292 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ASP C 379 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP C 379 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP D 85 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG D 101 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG D 444 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 PRO E 181 C - N - CD ANGL. DEV. = -14.2 DEGREES
REMARK 500 ARG E 431 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 MET F 176 CG - SD - CE ANGL. DEV. = 11.2 DEGREES
REMARK 500 PRO F 181 C - N - CD ANGL. DEV. = -13.3 DEGREES
REMARK 500 ARG F 378 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG F 378 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG F 444 NE - CZ - NH2 ANGL. DEV. = -3.2 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 ALA A 51 -124.23 47.54
REMARK 500 ASP A 84 -69.18 -91.04
REMARK 500 ALA A 89 48.80 39.99
REMARK 500 LEU A 175 -47.69 -132.57
REMARK 500 TYR A 299 -9.43 -145.50
REMARK 500 GLU A 366 109.37 -160.14
REMARK 500 TRP A 424 -134.37 66.23
REMARK 500 ALA A 427 -121.47 42.93
REMARK 500 ALA B 24 13.64 58.15
REMARK 500 ALA B 51 -127.52 50.59
REMARK 500 ASP B 84 -71.42 -85.76
REMARK 500 LEU B 175 -47.53 -135.23
REMARK 500 ASP B 185 92.53 -161.34
REMARK 500 LEU B 223 -164.37 -120.79
REMARK 500 ASN B 289 78.59 -116.32
REMARK 500 TYR B 299 -10.69 -143.70
REMARK 500 TYR B 342 77.06 -156.39
REMARK 500 ASP B 379 -165.71 -78.74
REMARK 500 THR B 417 147.80 -172.02
REMARK 500 SER B 423 56.91 -94.30
REMARK 500 TRP B 424 -127.72 58.90
REMARK 500 ALA B 427 -120.35 44.27
REMARK 500 PHE C 23 119.94 -35.10
REMARK 500 ALA C 51 -132.98 53.70
REMARK 500 ASP C 84 -76.09 -81.19
REMARK 500 GLU C 165 70.65 40.10
REMARK 500 LEU C 175 -43.97 -138.13
REMARK 500 TYR C 299 -17.90 -144.73
REMARK 500 TYR C 342 78.72 -163.44
REMARK 500 GLU C 366 117.86 -160.59
REMARK 500 ASP C 420 132.61 -37.34
REMARK 500 SER C 423 56.08 -95.21
REMARK 500 TRP C 424 -133.08 61.11
REMARK 500 ALA C 427 -121.90 47.95
REMARK 500 ALA D 51 -129.75 46.31
REMARK 500 ASP D 84 -74.56 -81.87
REMARK 500 TYR D 299 -15.40 -143.74
REMARK 500 GLU D 320 1.40 -68.37
REMARK 500 TYR D 342 78.70 -160.28
REMARK 500 THR D 417 142.93 -177.18
REMARK 500 TRP D 424 -128.86 61.70
REMARK 500 ALA D 427 -121.43 43.11
REMARK 500 ALA E 24 16.31 56.78
REMARK 500 ALA E 51 -127.80 46.83
REMARK 500 ASP E 84 -73.97 -84.98
REMARK 500 LEU E 175 -44.70 -143.39
REMARK 500 TYR E 299 -23.28 -143.91
REMARK 500 GLU E 366 115.05 -162.98
REMARK 500 THR E 417 143.50 -176.71
REMARK 500 SER E 423 53.25 -94.40
REMARK 500
REMARK 500 THIS ENTRY HAS 64 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TYR A 180 PRO A 181 51.61
REMARK 500 TRP A 416 THR A 417 47.86
REMARK 500 TYR B 180 PRO B 181 48.11
REMARK 500 TRP B 416 THR B 417 53.15
REMARK 500 TYR C 180 PRO C 181 43.95
REMARK 500 LEU C 294 GLY C 295 147.65
REMARK 500 TRP C 416 THR C 417 49.99
REMARK 500 TYR D 180 PRO D 181 53.64
REMARK 500 TRP D 416 THR D 417 58.01
REMARK 500 TYR E 180 PRO E 181 54.45
REMARK 500 TYR E 299 HIS E 300 149.74
REMARK 500 TRP E 416 THR E 417 57.23
REMARK 500 TYR F 180 PRO F 181 48.83
REMARK 500 TRP F 416 THR F 417 63.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 TYR A 180 12.16
REMARK 500 TRP A 416 16.09
REMARK 500 TYR B 180 12.73
REMARK 500 TRP B 416 16.49
REMARK 500 TYR C 180 15.38
REMARK 500 TRP C 416 16.89
REMARK 500 TYR D 180 11.91
REMARK 500 TRP D 416 14.07
REMARK 500 TYR E 180 10.24
REMARK 500 TRP E 416 16.71
REMARK 500 TYR F 180 13.30
REMARK 500 TRP F 416 16.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "BB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "CB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "DB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "EB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "FB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JAZ D 1464
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JAZ A 1464
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JAZ B 1464
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JAZ C 1464
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JAZ E 1464
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JAZ F 1464
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS C 1465
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 1465
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 1466
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1465
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1465
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1466
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1466
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1466
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1467
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1467
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1465
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1468
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1469
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1466
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 1465
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1468
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1467
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1467
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1469
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1468
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 1468
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1470
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 1466
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1470
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 1467
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 1469
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1471
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 1470
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1471
DBREF 5FOO A 1 480 UNP Q99YP9 Q99YP9_STRP1 1 480
DBREF 5FOO B 1 480 UNP Q99YP9 Q99YP9_STRP1 1 480
DBREF 5FOO C 1 480 UNP Q99YP9 Q99YP9_STRP1 1 480
DBREF 5FOO D 1 480 UNP Q99YP9 Q99YP9_STRP1 1 480
DBREF 5FOO E 1 480 UNP Q99YP9 Q99YP9_STRP1 1 480
DBREF 5FOO F 1 480 UNP Q99YP9 Q99YP9_STRP1 1 480
SEQADV 5FOO HIS A 331 UNP Q99YP9 ARG 331 ENGINEERED MUTATION
SEQADV 5FOO HIS B 331 UNP Q99YP9 ARG 331 ENGINEERED MUTATION
SEQADV 5FOO HIS C 331 UNP Q99YP9 ARG 331 ENGINEERED MUTATION
SEQADV 5FOO HIS D 331 UNP Q99YP9 ARG 331 ENGINEERED MUTATION
SEQADV 5FOO HIS E 331 UNP Q99YP9 ARG 331 ENGINEERED MUTATION
SEQADV 5FOO HIS F 331 UNP Q99YP9 ARG 331 ENGINEERED MUTATION
SEQRES 1 A 480 MET LEU ALA PHE PRO LYS GLU PHE TRP TRP GLY GLY ALA
SEQRES 2 A 480 THR SER GLY PRO GLN SER GLU GLY ARG PHE ALA LYS GLN
SEQRES 3 A 480 HIS ARG ASN LEU PHE ASP TYR TRP TYR GLU GLU GLU PRO
SEQRES 4 A 480 ASP LEU PHE TYR ASP TYR VAL GLY PRO ASP THR ALA SER
SEQRES 5 A 480 ASP ALA TYR HIS GLN ILE GLU SER ASP LEU THR LEU LEU
SEQRES 6 A 480 ALA SER LEU GLY HIS ASN SER TYR ARG THR SER ILE GLN
SEQRES 7 A 480 TRP THR ARG LEU ILE ASP ASP PHE GLU GLN ALA THR ILE
SEQRES 8 A 480 ASN PRO ASP GLY LEU ALA TYR TYR ASN ARG VAL ILE ASP
SEQRES 9 A 480 ALA CYS LEU ALA ASN GLY ILE ARG PRO VAL ILE ASN LEU
SEQRES 10 A 480 HIS HIS PHE ASP LEU PRO ILE ALA LEU TYR GLN ALA TYR
SEQRES 11 A 480 GLY GLY TRP GLU SER LYS HIS VAL VAL ASP LEU PHE VAL
SEQRES 12 A 480 ALA PHE SER LYS VAL CYS PHE GLU GLN PHE GLY ASP ARG
SEQRES 13 A 480 VAL LYS ASP TRP PHE VAL HIS ASN GLU PRO MET VAL VAL
SEQRES 14 A 480 VAL GLU GLY SER TYR LEU MET GLN PHE HIS TYR PRO ALA
SEQRES 15 A 480 ILE VAL ASP GLY LYS LYS ALA VAL GLN VAL ALA TYR ASN
SEQRES 16 A 480 LEU ALA LEU ALA THR ALA LYS VAL ILE GLN ALA TYR ARG
SEQRES 17 A 480 ARG GLY PRO ALA GLU LEU SER ASP GLY ARG ILE GLY THR
SEQRES 18 A 480 ILE LEU ASN LEU THR PRO ALA TYR PRO ALA SER GLN SER
SEQRES 19 A 480 GLU ALA ASP MET ALA ALA ALA HIS PHE ALA GLU LEU TRP
SEQRES 20 A 480 ASN ASN ASP LEU PHE MET GLU ALA ALA VAL HIS GLY LYS
SEQRES 21 A 480 PHE PRO GLU GLU LEU VAL ALA VAL LEU LYS LYS ASP GLY
SEQRES 22 A 480 VAL LEU TRP GLN SER THR PRO GLU GLU LEU ALA LEU ILE
SEQRES 23 A 480 ALA GLU ASN ARG VAL ASP TYR LEU GLY LEU ASN PHE TYR
SEQRES 24 A 480 HIS PRO LYS ARG VAL LYS ALA PRO ASP ALA ILE PRO VAL
SEQRES 25 A 480 ILE SER PRO SER TRP SER PRO GLU TRP TYR TYR ASP PRO
SEQRES 26 A 480 TYR LEU MET PRO GLY HIS ARG MET ASN VAL ASP LYS GLY
SEQRES 27 A 480 TRP GLU ILE TYR PRO GLU ALA VAL TYR ASP ILE ALA ILE
SEQRES 28 A 480 LYS MET ARG ASP HIS TYR ASP ASN ILE PRO TRP PHE LEU
SEQRES 29 A 480 SER GLU ASN GLY VAL GLY ILE SER GLY GLU ASP ARG TYR
SEQRES 30 A 480 ARG ASP GLU THR GLY GLN ILE GLN ASP ASP TYR ARG ILE
SEQRES 31 A 480 GLN PHE LEU LYS GLU HIS LEU THR TYR LEU HIS LYS GLY
SEQRES 32 A 480 ILE GLU ALA GLY SER ASN CYS PHE GLY TYR HIS VAL TRP
SEQRES 33 A 480 THR PRO ILE ASP GLY TRP SER TRP LEU ASN ALA TYR LYS
SEQRES 34 A 480 ASN ARG TYR GLY LEU VAL GLU ASN ASN ILE HIS THR GLN
SEQRES 35 A 480 VAL ARG ARG PRO LYS ALA SER ALA TYR TRP PHE LYS LYS
SEQRES 36 A 480 VAL ALA THR HIS ASN ARG LEU ILE SER LEU GLU VAL MET
SEQRES 37 A 480 GLU GLU PHE GLY GLY SER ALA SER HIS LEU SER ASP
SEQRES 1 B 480 MET LEU ALA PHE PRO LYS GLU PHE TRP TRP GLY GLY ALA
SEQRES 2 B 480 THR SER GLY PRO GLN SER GLU GLY ARG PHE ALA LYS GLN
SEQRES 3 B 480 HIS ARG ASN LEU PHE ASP TYR TRP TYR GLU GLU GLU PRO
SEQRES 4 B 480 ASP LEU PHE TYR ASP TYR VAL GLY PRO ASP THR ALA SER
SEQRES 5 B 480 ASP ALA TYR HIS GLN ILE GLU SER ASP LEU THR LEU LEU
SEQRES 6 B 480 ALA SER LEU GLY HIS ASN SER TYR ARG THR SER ILE GLN
SEQRES 7 B 480 TRP THR ARG LEU ILE ASP ASP PHE GLU GLN ALA THR ILE
SEQRES 8 B 480 ASN PRO ASP GLY LEU ALA TYR TYR ASN ARG VAL ILE ASP
SEQRES 9 B 480 ALA CYS LEU ALA ASN GLY ILE ARG PRO VAL ILE ASN LEU
SEQRES 10 B 480 HIS HIS PHE ASP LEU PRO ILE ALA LEU TYR GLN ALA TYR
SEQRES 11 B 480 GLY GLY TRP GLU SER LYS HIS VAL VAL ASP LEU PHE VAL
SEQRES 12 B 480 ALA PHE SER LYS VAL CYS PHE GLU GLN PHE GLY ASP ARG
SEQRES 13 B 480 VAL LYS ASP TRP PHE VAL HIS ASN GLU PRO MET VAL VAL
SEQRES 14 B 480 VAL GLU GLY SER TYR LEU MET GLN PHE HIS TYR PRO ALA
SEQRES 15 B 480 ILE VAL ASP GLY LYS LYS ALA VAL GLN VAL ALA TYR ASN
SEQRES 16 B 480 LEU ALA LEU ALA THR ALA LYS VAL ILE GLN ALA TYR ARG
SEQRES 17 B 480 ARG GLY PRO ALA GLU LEU SER ASP GLY ARG ILE GLY THR
SEQRES 18 B 480 ILE LEU ASN LEU THR PRO ALA TYR PRO ALA SER GLN SER
SEQRES 19 B 480 GLU ALA ASP MET ALA ALA ALA HIS PHE ALA GLU LEU TRP
SEQRES 20 B 480 ASN ASN ASP LEU PHE MET GLU ALA ALA VAL HIS GLY LYS
SEQRES 21 B 480 PHE PRO GLU GLU LEU VAL ALA VAL LEU LYS LYS ASP GLY
SEQRES 22 B 480 VAL LEU TRP GLN SER THR PRO GLU GLU LEU ALA LEU ILE
SEQRES 23 B 480 ALA GLU ASN ARG VAL ASP TYR LEU GLY LEU ASN PHE TYR
SEQRES 24 B 480 HIS PRO LYS ARG VAL LYS ALA PRO ASP ALA ILE PRO VAL
SEQRES 25 B 480 ILE SER PRO SER TRP SER PRO GLU TRP TYR TYR ASP PRO
SEQRES 26 B 480 TYR LEU MET PRO GLY HIS ARG MET ASN VAL ASP LYS GLY
SEQRES 27 B 480 TRP GLU ILE TYR PRO GLU ALA VAL TYR ASP ILE ALA ILE
SEQRES 28 B 480 LYS MET ARG ASP HIS TYR ASP ASN ILE PRO TRP PHE LEU
SEQRES 29 B 480 SER GLU ASN GLY VAL GLY ILE SER GLY GLU ASP ARG TYR
SEQRES 30 B 480 ARG ASP GLU THR GLY GLN ILE GLN ASP ASP TYR ARG ILE
SEQRES 31 B 480 GLN PHE LEU LYS GLU HIS LEU THR TYR LEU HIS LYS GLY
SEQRES 32 B 480 ILE GLU ALA GLY SER ASN CYS PHE GLY TYR HIS VAL TRP
SEQRES 33 B 480 THR PRO ILE ASP GLY TRP SER TRP LEU ASN ALA TYR LYS
SEQRES 34 B 480 ASN ARG TYR GLY LEU VAL GLU ASN ASN ILE HIS THR GLN
SEQRES 35 B 480 VAL ARG ARG PRO LYS ALA SER ALA TYR TRP PHE LYS LYS
SEQRES 36 B 480 VAL ALA THR HIS ASN ARG LEU ILE SER LEU GLU VAL MET
SEQRES 37 B 480 GLU GLU PHE GLY GLY SER ALA SER HIS LEU SER ASP
SEQRES 1 C 480 MET LEU ALA PHE PRO LYS GLU PHE TRP TRP GLY GLY ALA
SEQRES 2 C 480 THR SER GLY PRO GLN SER GLU GLY ARG PHE ALA LYS GLN
SEQRES 3 C 480 HIS ARG ASN LEU PHE ASP TYR TRP TYR GLU GLU GLU PRO
SEQRES 4 C 480 ASP LEU PHE TYR ASP TYR VAL GLY PRO ASP THR ALA SER
SEQRES 5 C 480 ASP ALA TYR HIS GLN ILE GLU SER ASP LEU THR LEU LEU
SEQRES 6 C 480 ALA SER LEU GLY HIS ASN SER TYR ARG THR SER ILE GLN
SEQRES 7 C 480 TRP THR ARG LEU ILE ASP ASP PHE GLU GLN ALA THR ILE
SEQRES 8 C 480 ASN PRO ASP GLY LEU ALA TYR TYR ASN ARG VAL ILE ASP
SEQRES 9 C 480 ALA CYS LEU ALA ASN GLY ILE ARG PRO VAL ILE ASN LEU
SEQRES 10 C 480 HIS HIS PHE ASP LEU PRO ILE ALA LEU TYR GLN ALA TYR
SEQRES 11 C 480 GLY GLY TRP GLU SER LYS HIS VAL VAL ASP LEU PHE VAL
SEQRES 12 C 480 ALA PHE SER LYS VAL CYS PHE GLU GLN PHE GLY ASP ARG
SEQRES 13 C 480 VAL LYS ASP TRP PHE VAL HIS ASN GLU PRO MET VAL VAL
SEQRES 14 C 480 VAL GLU GLY SER TYR LEU MET GLN PHE HIS TYR PRO ALA
SEQRES 15 C 480 ILE VAL ASP GLY LYS LYS ALA VAL GLN VAL ALA TYR ASN
SEQRES 16 C 480 LEU ALA LEU ALA THR ALA LYS VAL ILE GLN ALA TYR ARG
SEQRES 17 C 480 ARG GLY PRO ALA GLU LEU SER ASP GLY ARG ILE GLY THR
SEQRES 18 C 480 ILE LEU ASN LEU THR PRO ALA TYR PRO ALA SER GLN SER
SEQRES 19 C 480 GLU ALA ASP MET ALA ALA ALA HIS PHE ALA GLU LEU TRP
SEQRES 20 C 480 ASN ASN ASP LEU PHE MET GLU ALA ALA VAL HIS GLY LYS
SEQRES 21 C 480 PHE PRO GLU GLU LEU VAL ALA VAL LEU LYS LYS ASP GLY
SEQRES 22 C 480 VAL LEU TRP GLN SER THR PRO GLU GLU LEU ALA LEU ILE
SEQRES 23 C 480 ALA GLU ASN ARG VAL ASP TYR LEU GLY LEU ASN PHE TYR
SEQRES 24 C 480 HIS PRO LYS ARG VAL LYS ALA PRO ASP ALA ILE PRO VAL
SEQRES 25 C 480 ILE SER PRO SER TRP SER PRO GLU TRP TYR TYR ASP PRO
SEQRES 26 C 480 TYR LEU MET PRO GLY HIS ARG MET ASN VAL ASP LYS GLY
SEQRES 27 C 480 TRP GLU ILE TYR PRO GLU ALA VAL TYR ASP ILE ALA ILE
SEQRES 28 C 480 LYS MET ARG ASP HIS TYR ASP ASN ILE PRO TRP PHE LEU
SEQRES 29 C 480 SER GLU ASN GLY VAL GLY ILE SER GLY GLU ASP ARG TYR
SEQRES 30 C 480 ARG ASP GLU THR GLY GLN ILE GLN ASP ASP TYR ARG ILE
SEQRES 31 C 480 GLN PHE LEU LYS GLU HIS LEU THR TYR LEU HIS LYS GLY
SEQRES 32 C 480 ILE GLU ALA GLY SER ASN CYS PHE GLY TYR HIS VAL TRP
SEQRES 33 C 480 THR PRO ILE ASP GLY TRP SER TRP LEU ASN ALA TYR LYS
SEQRES 34 C 480 ASN ARG TYR GLY LEU VAL GLU ASN ASN ILE HIS THR GLN
SEQRES 35 C 480 VAL ARG ARG PRO LYS ALA SER ALA TYR TRP PHE LYS LYS
SEQRES 36 C 480 VAL ALA THR HIS ASN ARG LEU ILE SER LEU GLU VAL MET
SEQRES 37 C 480 GLU GLU PHE GLY GLY SER ALA SER HIS LEU SER ASP
SEQRES 1 D 480 MET LEU ALA PHE PRO LYS GLU PHE TRP TRP GLY GLY ALA
SEQRES 2 D 480 THR SER GLY PRO GLN SER GLU GLY ARG PHE ALA LYS GLN
SEQRES 3 D 480 HIS ARG ASN LEU PHE ASP TYR TRP TYR GLU GLU GLU PRO
SEQRES 4 D 480 ASP LEU PHE TYR ASP TYR VAL GLY PRO ASP THR ALA SER
SEQRES 5 D 480 ASP ALA TYR HIS GLN ILE GLU SER ASP LEU THR LEU LEU
SEQRES 6 D 480 ALA SER LEU GLY HIS ASN SER TYR ARG THR SER ILE GLN
SEQRES 7 D 480 TRP THR ARG LEU ILE ASP ASP PHE GLU GLN ALA THR ILE
SEQRES 8 D 480 ASN PRO ASP GLY LEU ALA TYR TYR ASN ARG VAL ILE ASP
SEQRES 9 D 480 ALA CYS LEU ALA ASN GLY ILE ARG PRO VAL ILE ASN LEU
SEQRES 10 D 480 HIS HIS PHE ASP LEU PRO ILE ALA LEU TYR GLN ALA TYR
SEQRES 11 D 480 GLY GLY TRP GLU SER LYS HIS VAL VAL ASP LEU PHE VAL
SEQRES 12 D 480 ALA PHE SER LYS VAL CYS PHE GLU GLN PHE GLY ASP ARG
SEQRES 13 D 480 VAL LYS ASP TRP PHE VAL HIS ASN GLU PRO MET VAL VAL
SEQRES 14 D 480 VAL GLU GLY SER TYR LEU MET GLN PHE HIS TYR PRO ALA
SEQRES 15 D 480 ILE VAL ASP GLY LYS LYS ALA VAL GLN VAL ALA TYR ASN
SEQRES 16 D 480 LEU ALA LEU ALA THR ALA LYS VAL ILE GLN ALA TYR ARG
SEQRES 17 D 480 ARG GLY PRO ALA GLU LEU SER ASP GLY ARG ILE GLY THR
SEQRES 18 D 480 ILE LEU ASN LEU THR PRO ALA TYR PRO ALA SER GLN SER
SEQRES 19 D 480 GLU ALA ASP MET ALA ALA ALA HIS PHE ALA GLU LEU TRP
SEQRES 20 D 480 ASN ASN ASP LEU PHE MET GLU ALA ALA VAL HIS GLY LYS
SEQRES 21 D 480 PHE PRO GLU GLU LEU VAL ALA VAL LEU LYS LYS ASP GLY
SEQRES 22 D 480 VAL LEU TRP GLN SER THR PRO GLU GLU LEU ALA LEU ILE
SEQRES 23 D 480 ALA GLU ASN ARG VAL ASP TYR LEU GLY LEU ASN PHE TYR
SEQRES 24 D 480 HIS PRO LYS ARG VAL LYS ALA PRO ASP ALA ILE PRO VAL
SEQRES 25 D 480 ILE SER PRO SER TRP SER PRO GLU TRP TYR TYR ASP PRO
SEQRES 26 D 480 TYR LEU MET PRO GLY HIS ARG MET ASN VAL ASP LYS GLY
SEQRES 27 D 480 TRP GLU ILE TYR PRO GLU ALA VAL TYR ASP ILE ALA ILE
SEQRES 28 D 480 LYS MET ARG ASP HIS TYR ASP ASN ILE PRO TRP PHE LEU
SEQRES 29 D 480 SER GLU ASN GLY VAL GLY ILE SER GLY GLU ASP ARG TYR
SEQRES 30 D 480 ARG ASP GLU THR GLY GLN ILE GLN ASP ASP TYR ARG ILE
SEQRES 31 D 480 GLN PHE LEU LYS GLU HIS LEU THR TYR LEU HIS LYS GLY
SEQRES 32 D 480 ILE GLU ALA GLY SER ASN CYS PHE GLY TYR HIS VAL TRP
SEQRES 33 D 480 THR PRO ILE ASP GLY TRP SER TRP LEU ASN ALA TYR LYS
SEQRES 34 D 480 ASN ARG TYR GLY LEU VAL GLU ASN ASN ILE HIS THR GLN
SEQRES 35 D 480 VAL ARG ARG PRO LYS ALA SER ALA TYR TRP PHE LYS LYS
SEQRES 36 D 480 VAL ALA THR HIS ASN ARG LEU ILE SER LEU GLU VAL MET
SEQRES 37 D 480 GLU GLU PHE GLY GLY SER ALA SER HIS LEU SER ASP
SEQRES 1 E 480 MET LEU ALA PHE PRO LYS GLU PHE TRP TRP GLY GLY ALA
SEQRES 2 E 480 THR SER GLY PRO GLN SER GLU GLY ARG PHE ALA LYS GLN
SEQRES 3 E 480 HIS ARG ASN LEU PHE ASP TYR TRP TYR GLU GLU GLU PRO
SEQRES 4 E 480 ASP LEU PHE TYR ASP TYR VAL GLY PRO ASP THR ALA SER
SEQRES 5 E 480 ASP ALA TYR HIS GLN ILE GLU SER ASP LEU THR LEU LEU
SEQRES 6 E 480 ALA SER LEU GLY HIS ASN SER TYR ARG THR SER ILE GLN
SEQRES 7 E 480 TRP THR ARG LEU ILE ASP ASP PHE GLU GLN ALA THR ILE
SEQRES 8 E 480 ASN PRO ASP GLY LEU ALA TYR TYR ASN ARG VAL ILE ASP
SEQRES 9 E 480 ALA CYS LEU ALA ASN GLY ILE ARG PRO VAL ILE ASN LEU
SEQRES 10 E 480 HIS HIS PHE ASP LEU PRO ILE ALA LEU TYR GLN ALA TYR
SEQRES 11 E 480 GLY GLY TRP GLU SER LYS HIS VAL VAL ASP LEU PHE VAL
SEQRES 12 E 480 ALA PHE SER LYS VAL CYS PHE GLU GLN PHE GLY ASP ARG
SEQRES 13 E 480 VAL LYS ASP TRP PHE VAL HIS ASN GLU PRO MET VAL VAL
SEQRES 14 E 480 VAL GLU GLY SER TYR LEU MET GLN PHE HIS TYR PRO ALA
SEQRES 15 E 480 ILE VAL ASP GLY LYS LYS ALA VAL GLN VAL ALA TYR ASN
SEQRES 16 E 480 LEU ALA LEU ALA THR ALA LYS VAL ILE GLN ALA TYR ARG
SEQRES 17 E 480 ARG GLY PRO ALA GLU LEU SER ASP GLY ARG ILE GLY THR
SEQRES 18 E 480 ILE LEU ASN LEU THR PRO ALA TYR PRO ALA SER GLN SER
SEQRES 19 E 480 GLU ALA ASP MET ALA ALA ALA HIS PHE ALA GLU LEU TRP
SEQRES 20 E 480 ASN ASN ASP LEU PHE MET GLU ALA ALA VAL HIS GLY LYS
SEQRES 21 E 480 PHE PRO GLU GLU LEU VAL ALA VAL LEU LYS LYS ASP GLY
SEQRES 22 E 480 VAL LEU TRP GLN SER THR PRO GLU GLU LEU ALA LEU ILE
SEQRES 23 E 480 ALA GLU ASN ARG VAL ASP TYR LEU GLY LEU ASN PHE TYR
SEQRES 24 E 480 HIS PRO LYS ARG VAL LYS ALA PRO ASP ALA ILE PRO VAL
SEQRES 25 E 480 ILE SER PRO SER TRP SER PRO GLU TRP TYR TYR ASP PRO
SEQRES 26 E 480 TYR LEU MET PRO GLY HIS ARG MET ASN VAL ASP LYS GLY
SEQRES 27 E 480 TRP GLU ILE TYR PRO GLU ALA VAL TYR ASP ILE ALA ILE
SEQRES 28 E 480 LYS MET ARG ASP HIS TYR ASP ASN ILE PRO TRP PHE LEU
SEQRES 29 E 480 SER GLU ASN GLY VAL GLY ILE SER GLY GLU ASP ARG TYR
SEQRES 30 E 480 ARG ASP GLU THR GLY GLN ILE GLN ASP ASP TYR ARG ILE
SEQRES 31 E 480 GLN PHE LEU LYS GLU HIS LEU THR TYR LEU HIS LYS GLY
SEQRES 32 E 480 ILE GLU ALA GLY SER ASN CYS PHE GLY TYR HIS VAL TRP
SEQRES 33 E 480 THR PRO ILE ASP GLY TRP SER TRP LEU ASN ALA TYR LYS
SEQRES 34 E 480 ASN ARG TYR GLY LEU VAL GLU ASN ASN ILE HIS THR GLN
SEQRES 35 E 480 VAL ARG ARG PRO LYS ALA SER ALA TYR TRP PHE LYS LYS
SEQRES 36 E 480 VAL ALA THR HIS ASN ARG LEU ILE SER LEU GLU VAL MET
SEQRES 37 E 480 GLU GLU PHE GLY GLY SER ALA SER HIS LEU SER ASP
SEQRES 1 F 480 MET LEU ALA PHE PRO LYS GLU PHE TRP TRP GLY GLY ALA
SEQRES 2 F 480 THR SER GLY PRO GLN SER GLU GLY ARG PHE ALA LYS GLN
SEQRES 3 F 480 HIS ARG ASN LEU PHE ASP TYR TRP TYR GLU GLU GLU PRO
SEQRES 4 F 480 ASP LEU PHE TYR ASP TYR VAL GLY PRO ASP THR ALA SER
SEQRES 5 F 480 ASP ALA TYR HIS GLN ILE GLU SER ASP LEU THR LEU LEU
SEQRES 6 F 480 ALA SER LEU GLY HIS ASN SER TYR ARG THR SER ILE GLN
SEQRES 7 F 480 TRP THR ARG LEU ILE ASP ASP PHE GLU GLN ALA THR ILE
SEQRES 8 F 480 ASN PRO ASP GLY LEU ALA TYR TYR ASN ARG VAL ILE ASP
SEQRES 9 F 480 ALA CYS LEU ALA ASN GLY ILE ARG PRO VAL ILE ASN LEU
SEQRES 10 F 480 HIS HIS PHE ASP LEU PRO ILE ALA LEU TYR GLN ALA TYR
SEQRES 11 F 480 GLY GLY TRP GLU SER LYS HIS VAL VAL ASP LEU PHE VAL
SEQRES 12 F 480 ALA PHE SER LYS VAL CYS PHE GLU GLN PHE GLY ASP ARG
SEQRES 13 F 480 VAL LYS ASP TRP PHE VAL HIS ASN GLU PRO MET VAL VAL
SEQRES 14 F 480 VAL GLU GLY SER TYR LEU MET GLN PHE HIS TYR PRO ALA
SEQRES 15 F 480 ILE VAL ASP GLY LYS LYS ALA VAL GLN VAL ALA TYR ASN
SEQRES 16 F 480 LEU ALA LEU ALA THR ALA LYS VAL ILE GLN ALA TYR ARG
SEQRES 17 F 480 ARG GLY PRO ALA GLU LEU SER ASP GLY ARG ILE GLY THR
SEQRES 18 F 480 ILE LEU ASN LEU THR PRO ALA TYR PRO ALA SER GLN SER
SEQRES 19 F 480 GLU ALA ASP MET ALA ALA ALA HIS PHE ALA GLU LEU TRP
SEQRES 20 F 480 ASN ASN ASP LEU PHE MET GLU ALA ALA VAL HIS GLY LYS
SEQRES 21 F 480 PHE PRO GLU GLU LEU VAL ALA VAL LEU LYS LYS ASP GLY
SEQRES 22 F 480 VAL LEU TRP GLN SER THR PRO GLU GLU LEU ALA LEU ILE
SEQRES 23 F 480 ALA GLU ASN ARG VAL ASP TYR LEU GLY LEU ASN PHE TYR
SEQRES 24 F 480 HIS PRO LYS ARG VAL LYS ALA PRO ASP ALA ILE PRO VAL
SEQRES 25 F 480 ILE SER PRO SER TRP SER PRO GLU TRP TYR TYR ASP PRO
SEQRES 26 F 480 TYR LEU MET PRO GLY HIS ARG MET ASN VAL ASP LYS GLY
SEQRES 27 F 480 TRP GLU ILE TYR PRO GLU ALA VAL TYR ASP ILE ALA ILE
SEQRES 28 F 480 LYS MET ARG ASP HIS TYR ASP ASN ILE PRO TRP PHE LEU
SEQRES 29 F 480 SER GLU ASN GLY VAL GLY ILE SER GLY GLU ASP ARG TYR
SEQRES 30 F 480 ARG ASP GLU THR GLY GLN ILE GLN ASP ASP TYR ARG ILE
SEQRES 31 F 480 GLN PHE LEU LYS GLU HIS LEU THR TYR LEU HIS LYS GLY
SEQRES 32 F 480 ILE GLU ALA GLY SER ASN CYS PHE GLY TYR HIS VAL TRP
SEQRES 33 F 480 THR PRO ILE ASP GLY TRP SER TRP LEU ASN ALA TYR LYS
SEQRES 34 F 480 ASN ARG TYR GLY LEU VAL GLU ASN ASN ILE HIS THR GLN
SEQRES 35 F 480 VAL ARG ARG PRO LYS ALA SER ALA TYR TRP PHE LYS LYS
SEQRES 36 F 480 VAL ALA THR HIS ASN ARG LEU ILE SER LEU GLU VAL MET
SEQRES 37 F 480 GLU GLU PHE GLY GLY SER ALA SER HIS LEU SER ASP
HET JAZ A1464 16
HET EDO A1465 4
HET EDO A1466 4
HET EDO A1467 4
HET EDO A1468 4
HET EDO A1469 4
HET PO4 A1470 5
HET CL A1471 1
HET JAZ B1464 16
HET EDO B1465 4
HET EDO B1466 4
HET EDO B1467 4
HET EDO B1468 4
HET EDO B1469 4
HET PO4 B1470 5
HET CL B1471 1
HET JAZ C1464 16
HET TRS C1465 8
HET EDO C1466 4
HET EDO C1467 4
HET PO4 C1468 5
HET JAZ D1464 16
HET EDO D1465 4
HET EDO D1466 4
HET EDO D1467 4
HET EDO D1468 4
HET PO4 D1469 5
HET CL D1470 1
HET JAZ E1464 16
HET EDO E1465 4
HET PO4 E1466 5
HET JAZ F1464 16
HET EDO F1465 4
HET EDO F1466 4
HET PO4 F1467 5
HETNAM JAZ 6-PHOSPHOCYCLOPHELLITOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PO4 PHOSPHATE ION
HETNAM CL CHLORIDE ION
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN EDO ETHYLENE GLYCOL
HETSYN TRS TRIS BUFFER
FORMUL 7 JAZ 6(C7 H15 O9 P)
FORMUL 8 EDO 19(C2 H6 O2)
FORMUL 13 PO4 6(O4 P 3-)
FORMUL 14 CL 3(CL 1-)
FORMUL 24 TRS C4 H12 N O3 1+
FORMUL 42 HOH *981(H2 O)
HELIX 1 1 SER A 15 GLU A 20 1 6
HELIX 2 2 ASN A 29 GLU A 38 1 10
HELIX 3 3 PRO A 39 VAL A 46 5 8
HELIX 4 4 ASP A 53 LEU A 68 1 16
HELIX 5 5 GLN A 78 ILE A 83 1 6
HELIX 6 6 ASN A 92 ASN A 109 1 18
HELIX 7 7 PRO A 123 GLY A 131 1 9
HELIX 8 8 GLY A 132 GLU A 134 5 3
HELIX 9 9 SER A 135 GLY A 154 1 20
HELIX 10 10 GLU A 165 LEU A 175 1 11
HELIX 11 11 ASP A 185 ARG A 209 1 25
HELIX 12 12 SER A 234 ASN A 249 1 16
HELIX 13 13 ASN A 249 GLY A 259 1 11
HELIX 14 14 PRO A 262 ASP A 272 1 11
HELIX 15 15 THR A 279 ASN A 289 1 11
HELIX 16 16 SER A 318 TYR A 322 5 5
HELIX 17 17 PRO A 343 TYR A 357 1 15
HELIX 18 18 GLY A 373 TYR A 377 5 5
HELIX 19 19 ASP A 386 ALA A 406 1 21
HELIX 20 20 SER A 423 ALA A 427 5 5
HELIX 21 21 LYS A 447 ASN A 460 1 14
HELIX 22 22 SER B 15 GLU B 20 1 6
HELIX 23 23 ASN B 29 GLU B 38 1 10
HELIX 24 24 PRO B 39 VAL B 46 5 8
HELIX 25 25 ASP B 53 LEU B 68 1 16
HELIX 26 26 GLN B 78 ILE B 83 1 6
HELIX 27 27 ASN B 92 ASN B 109 1 18
HELIX 28 28 PRO B 123 GLY B 131 1 9
HELIX 29 29 GLY B 132 GLU B 134 5 3
HELIX 30 30 SER B 135 GLY B 154 1 20
HELIX 31 31 GLU B 165 LEU B 175 1 11
HELIX 32 32 ASP B 185 ARG B 209 1 25
HELIX 33 33 SER B 234 ASN B 249 1 16
HELIX 34 34 ASN B 249 GLY B 259 1 11
HELIX 35 35 PRO B 262 ASP B 272 1 11
HELIX 36 36 THR B 279 ASN B 289 1 11
HELIX 37 37 SER B 318 TYR B 322 5 5
HELIX 38 38 GLU B 344 TYR B 357 1 14
HELIX 39 39 GLY B 373 TYR B 377 5 5
HELIX 40 40 ASP B 386 ALA B 406 1 21
HELIX 41 41 SER B 423 ALA B 427 5 5
HELIX 42 42 LYS B 447 ASN B 460 1 14
HELIX 43 43 SER C 15 GLU C 20 1 6
HELIX 44 44 ASN C 29 GLU C 38 1 10
HELIX 45 45 PRO C 39 VAL C 46 5 8
HELIX 46 46 ASP C 53 LEU C 68 1 16
HELIX 47 47 GLN C 78 ILE C 83 1 6
HELIX 48 48 ASN C 92 ASN C 109 1 18
HELIX 49 49 PRO C 123 GLY C 131 1 9
HELIX 50 50 GLY C 132 GLU C 134 5 3
HELIX 51 51 SER C 135 GLY C 154 1 20
HELIX 52 52 GLU C 165 LEU C 175 1 11
HELIX 53 53 ASP C 185 ARG C 209 1 25
HELIX 54 54 SER C 234 ASN C 249 1 16
HELIX 55 55 ASN C 249 GLY C 259 1 11
HELIX 56 56 PRO C 262 ASP C 272 1 11
HELIX 57 57 THR C 279 ASN C 289 1 11
HELIX 58 58 SER C 318 TYR C 322 5 5
HELIX 59 59 GLU C 344 TYR C 357 1 14
HELIX 60 60 GLY C 373 TYR C 377 5 5
HELIX 61 61 ASP C 386 ALA C 406 1 21
HELIX 62 62 SER C 423 ALA C 427 5 5
HELIX 63 63 LYS C 447 ASN C 460 1 14
HELIX 64 64 SER D 15 GLU D 20 1 6
HELIX 65 65 ASN D 29 GLU D 38 1 10
HELIX 66 66 PRO D 39 VAL D 46 5 8
HELIX 67 67 ASP D 53 LEU D 68 1 16
HELIX 68 68 GLN D 78 ILE D 83 1 6
HELIX 69 69 ASN D 92 ASN D 109 1 18
HELIX 70 70 PRO D 123 GLY D 131 1 9
HELIX 71 71 GLY D 132 GLU D 134 5 3
HELIX 72 72 SER D 135 GLY D 154 1 20
HELIX 73 73 GLU D 165 LEU D 175 1 11
HELIX 74 74 ASP D 185 GLY D 210 1 26
HELIX 75 75 PRO D 211 SER D 215 5 5
HELIX 76 76 SER D 234 ASN D 249 1 16
HELIX 77 77 ASN D 249 GLY D 259 1 11
HELIX 78 78 PRO D 262 ASP D 272 1 11
HELIX 79 79 THR D 279 ASN D 289 1 11
HELIX 80 80 SER D 318 TYR D 322 5 5
HELIX 81 81 GLU D 344 TYR D 357 1 14
HELIX 82 82 GLY D 373 TYR D 377 5 5
HELIX 83 83 ASP D 386 ALA D 406 1 21
HELIX 84 84 SER D 423 ALA D 427 5 5
HELIX 85 85 LYS D 447 ASN D 460 1 14
HELIX 86 86 SER E 15 GLU E 20 1 6
HELIX 87 87 ASN E 29 GLU E 38 1 10
HELIX 88 88 PRO E 39 VAL E 46 5 8
HELIX 89 89 ASP E 53 LEU E 68 1 16
HELIX 90 90 GLN E 78 ILE E 83 1 6
HELIX 91 91 ASN E 92 ASN E 109 1 18
HELIX 92 92 PRO E 123 GLY E 131 1 9
HELIX 93 93 GLY E 132 GLU E 134 5 3
HELIX 94 94 SER E 135 GLY E 154 1 20
HELIX 95 95 GLU E 165 LEU E 175 1 11
HELIX 96 96 ASP E 185 ARG E 209 1 25
HELIX 97 97 PRO E 211 SER E 215 5 5
HELIX 98 98 SER E 234 ASN E 249 1 16
HELIX 99 99 ASN E 249 GLY E 259 1 11
HELIX 100 100 PRO E 262 ASP E 272 1 11
HELIX 101 101 THR E 279 ASN E 289 1 11
HELIX 102 102 SER E 318 TYR E 322 5 5
HELIX 103 103 PRO E 343 TYR E 357 1 15
HELIX 104 104 GLY E 373 TYR E 377 5 5
HELIX 105 105 ASP E 386 ALA E 406 1 21
HELIX 106 106 SER E 423 ALA E 427 5 5
HELIX 107 107 LYS E 447 ASN E 460 1 14
HELIX 108 108 SER F 15 GLU F 20 1 6
HELIX 109 109 ASN F 29 GLU F 38 1 10
HELIX 110 110 PRO F 39 VAL F 46 5 8
HELIX 111 111 ASP F 53 LEU F 68 1 16
HELIX 112 112 GLN F 78 ILE F 83 1 6
HELIX 113 113 ASN F 92 ASN F 109 1 18
HELIX 114 114 PRO F 123 GLY F 131 1 9
HELIX 115 115 GLY F 132 GLU F 134 5 3
HELIX 116 116 SER F 135 GLY F 154 1 20
HELIX 117 117 GLU F 165 LEU F 175 1 11
HELIX 118 118 ASP F 185 ARG F 209 1 25
HELIX 119 119 SER F 234 ASN F 249 1 16
HELIX 120 120 ASN F 249 HIS F 258 1 10
HELIX 121 121 PRO F 262 ASP F 272 1 11
HELIX 122 122 THR F 279 ASN F 289 1 11
HELIX 123 123 SER F 318 TYR F 322 5 5
HELIX 124 124 PRO F 343 TYR F 357 1 15
HELIX 125 125 GLY F 373 TYR F 377 5 5
HELIX 126 126 ASP F 386 ALA F 406 1 21
HELIX 127 127 SER F 423 ALA F 427 5 5
HELIX 128 128 LYS F 447 ASN F 460 1 14
SHEET 1 AA 2 LEU A 2 ALA A 3 0
SHEET 2 AA 2 ARG A 461 LEU A 462 -1 O LEU A 462 N LEU A 2
SHEET 1 AB 9 TRP A 9 ALA A 13 0
SHEET 2 AB 9 CYS A 410 TRP A 416 1 O PHE A 411 N TRP A 9
SHEET 3 AB 9 TRP A 362 ASN A 367 1 O TRP A 362 N PHE A 411
SHEET 4 AB 9 TYR A 293 ASN A 297 1 O LEU A 294 N PHE A 363
SHEET 5 AB 9 ARG A 218 ASN A 224 1 O THR A 221 N GLY A 295
SHEET 6 AB 9 ASP A 159 ASN A 164 1 O TRP A 160 N GLY A 220
SHEET 7 AB 9 ARG A 112 ASN A 116 1 O ILE A 115 N PHE A 161
SHEET 8 AB 9 SER A 72 SER A 76 1 O TYR A 73 N VAL A 114
SHEET 9 AB 9 TRP A 9 ALA A 13 1 O GLY A 12 N ARG A 74
SHEET 1 AC 3 ALA A 228 PRO A 230 0
SHEET 2 AC 3 LYS A 302 LYS A 305 1 O LYS A 302 N TYR A 229
SHEET 3 AC 3 ASP A 324 PRO A 325 -1 O ASP A 324 N LYS A 305
SHEET 1 AD 3 TRP A 339 ILE A 341 0
SHEET 2 AD 3 HIS A 331 ASN A 334 -1 O ARG A 332 N ILE A 341
SHEET 3 AD 3 ALA E 309 ILE E 313 1 O ILE E 310 N MET A 333
SHEET 1 AE 2 VAL A 435 ASN A 437 0
SHEET 2 AE 2 ARG A 444 PRO A 446 -1 O ARG A 445 N GLU A 436
SHEET 1 BA 2 LEU B 2 ALA B 3 0
SHEET 2 BA 2 ARG B 461 LEU B 462 -1 O LEU B 462 N LEU B 2
SHEET 1 BB 9 TRP B 9 ALA B 13 0
SHEET 2 BB 9 CYS B 410 TRP B 416 1 O PHE B 411 N TRP B 9
SHEET 3 BB 9 TRP B 362 ASN B 367 1 O TRP B 362 N PHE B 411
SHEET 4 BB 9 TYR B 293 ASN B 297 1 O LEU B 294 N PHE B 363
SHEET 5 BB 9 ARG B 218 LEU B 223 1 O THR B 221 N GLY B 295
SHEET 6 BB 9 ASP B 159 ASN B 164 1 O TRP B 160 N GLY B 220
SHEET 7 BB 9 ARG B 112 ASN B 116 1 O ILE B 115 N PHE B 161
SHEET 8 BB 9 SER B 72 SER B 76 1 O TYR B 73 N VAL B 114
SHEET 9 BB 9 TRP B 9 ALA B 13 1 O GLY B 12 N ARG B 74
SHEET 1 BC 3 ALA B 228 PRO B 230 0
SHEET 2 BC 3 LYS B 302 LYS B 305 1 O LYS B 302 N TYR B 229
SHEET 3 BC 3 ASP B 324 PRO B 325 -1 O ASP B 324 N LYS B 305
SHEET 1 BD 2 ARG B 332 ASN B 334 0
SHEET 2 BD 2 TRP B 339 ILE B 341 -1 O TRP B 339 N ASN B 334
SHEET 1 BE 2 VAL B 435 ASN B 437 0
SHEET 2 BE 2 ARG B 444 PRO B 446 -1 O ARG B 445 N GLU B 436
SHEET 1 CA 2 LEU C 2 ALA C 3 0
SHEET 2 CA 2 ARG C 461 LEU C 462 -1 O LEU C 462 N LEU C 2
SHEET 1 CB 9 TRP C 9 ALA C 13 0
SHEET 2 CB 9 CYS C 410 TRP C 416 1 O PHE C 411 N TRP C 9
SHEET 3 CB 9 TRP C 362 ASN C 367 1 O TRP C 362 N PHE C 411
SHEET 4 CB 9 TYR C 293 ASN C 297 1 O LEU C 294 N PHE C 363
SHEET 5 CB 9 ARG C 218 ASN C 224 1 O THR C 221 N GLY C 295
SHEET 6 CB 9 ASP C 159 ASN C 164 1 O TRP C 160 N GLY C 220
SHEET 7 CB 9 ARG C 112 ASN C 116 1 O ILE C 115 N PHE C 161
SHEET 8 CB 9 SER C 72 SER C 76 1 O TYR C 73 N VAL C 114
SHEET 9 CB 9 TRP C 9 ALA C 13 1 O GLY C 12 N ARG C 74
SHEET 1 CC 3 ALA C 228 PRO C 230 0
SHEET 2 CC 3 LYS C 302 LYS C 305 1 O LYS C 302 N TYR C 229
SHEET 3 CC 3 ASP C 324 PRO C 325 -1 O ASP C 324 N LYS C 305
SHEET 1 CD 3 ALA C 309 PRO C 311 0
SHEET 2 CD 3 HIS D 331 ASN D 334 1 O HIS D 331 N ILE C 310
SHEET 3 CD 3 TRP D 339 ILE D 341 -1 O TRP D 339 N ASN D 334
SHEET 1 CE 2 ARG C 332 ASN C 334 0
SHEET 2 CE 2 TRP C 339 ILE C 341 -1 O TRP C 339 N ASN C 334
SHEET 1 CF 2 VAL C 435 ASN C 437 0
SHEET 2 CF 2 ARG C 444 PRO C 446 -1 O ARG C 445 N GLU C 436
SHEET 1 DA 2 LEU D 2 ALA D 3 0
SHEET 2 DA 2 ARG D 461 LEU D 462 -1 O LEU D 462 N LEU D 2
SHEET 1 DB 9 TRP D 9 ALA D 13 0
SHEET 2 DB 9 CYS D 410 TRP D 416 1 O PHE D 411 N TRP D 9
SHEET 3 DB 9 TRP D 362 ASN D 367 1 O TRP D 362 N PHE D 411
SHEET 4 DB 9 TYR D 293 ASN D 297 1 O LEU D 294 N PHE D 363
SHEET 5 DB 9 ARG D 218 LEU D 223 1 O THR D 221 N GLY D 295
SHEET 6 DB 9 ASP D 159 ASN D 164 1 O TRP D 160 N GLY D 220
SHEET 7 DB 9 ARG D 112 ASN D 116 1 O ILE D 115 N PHE D 161
SHEET 8 DB 9 SER D 72 SER D 76 1 O TYR D 73 N VAL D 114
SHEET 9 DB 9 TRP D 9 ALA D 13 1 O GLY D 12 N ARG D 74
SHEET 1 DC 3 ALA D 228 PRO D 230 0
SHEET 2 DC 3 LYS D 302 LYS D 305 1 O LYS D 302 N TYR D 229
SHEET 3 DC 3 ASP D 324 PRO D 325 -1 O ASP D 324 N LYS D 305
SHEET 1 DD 2 VAL D 435 ASN D 437 0
SHEET 2 DD 2 ARG D 444 PRO D 446 -1 O ARG D 445 N GLU D 436
SHEET 1 EA 2 LEU E 2 ALA E 3 0
SHEET 2 EA 2 ARG E 461 LEU E 462 -1 O LEU E 462 N LEU E 2
SHEET 1 EB 9 TRP E 9 ALA E 13 0
SHEET 2 EB 9 CYS E 410 TRP E 416 1 O PHE E 411 N TRP E 9
SHEET 3 EB 9 TRP E 362 ASN E 367 1 O TRP E 362 N PHE E 411
SHEET 4 EB 9 LEU E 294 ASN E 297 1 O LEU E 294 N PHE E 363
SHEET 5 EB 9 ARG E 218 LEU E 223 1 O THR E 221 N GLY E 295
SHEET 6 EB 9 ASP E 159 ASN E 164 1 O TRP E 160 N GLY E 220
SHEET 7 EB 9 ARG E 112 ASN E 116 1 O ILE E 115 N PHE E 161
SHEET 8 EB 9 SER E 72 SER E 76 1 O TYR E 73 N VAL E 114
SHEET 9 EB 9 TRP E 9 ALA E 13 1 O GLY E 12 N ARG E 74
SHEET 1 EC 3 ALA E 228 PRO E 230 0
SHEET 2 EC 3 LYS E 302 LYS E 305 1 O LYS E 302 N TYR E 229
SHEET 3 EC 3 ASP E 324 PRO E 325 -1 O ASP E 324 N LYS E 305
SHEET 1 ED 2 MET E 333 ASN E 334 0
SHEET 2 ED 2 TRP E 339 GLU E 340 -1 O TRP E 339 N ASN E 334
SHEET 1 EE 2 VAL E 435 ASN E 437 0
SHEET 2 EE 2 ARG E 444 PRO E 446 -1 O ARG E 445 N GLU E 436
SHEET 1 FA 2 LEU F 2 ALA F 3 0
SHEET 2 FA 2 ARG F 461 LEU F 462 -1 O LEU F 462 N LEU F 2
SHEET 1 FB 9 TRP F 9 ALA F 13 0
SHEET 2 FB 9 CYS F 410 TRP F 416 1 O PHE F 411 N TRP F 9
SHEET 3 FB 9 TRP F 362 ASN F 367 1 O TRP F 362 N PHE F 411
SHEET 4 FB 9 TYR F 293 ASN F 297 1 O LEU F 294 N PHE F 363
SHEET 5 FB 9 ARG F 218 ASN F 224 1 O THR F 221 N GLY F 295
SHEET 6 FB 9 ASP F 159 ASN F 164 1 O TRP F 160 N GLY F 220
SHEET 7 FB 9 ARG F 112 ASN F 116 1 O ILE F 115 N PHE F 161
SHEET 8 FB 9 SER F 72 SER F 76 1 O TYR F 73 N VAL F 114
SHEET 9 FB 9 TRP F 9 ALA F 13 1 O GLY F 12 N ARG F 74
SHEET 1 FC 3 ALA F 228 PRO F 230 0
SHEET 2 FC 3 LYS F 302 LYS F 305 1 O LYS F 302 N TYR F 229
SHEET 3 FC 3 ASP F 324 PRO F 325 -1 O ASP F 324 N LYS F 305
SHEET 1 FD 2 ARG F 332 ASN F 334 0
SHEET 2 FD 2 TRP F 339 ILE F 341 -1 O TRP F 339 N ASN F 334
SHEET 1 FE 2 VAL F 435 ASN F 437 0
SHEET 2 FE 2 ARG F 444 PRO F 446 -1 O ARG F 445 N GLU F 436
LINK OE2 GLU A 366 C5 JAZ A1464 1555 1555 1.47
LINK OE2 GLU B 366 C5 JAZ B1464 1555 1555 1.45
LINK OE2 GLU C 366 C5 JAZ C1464 1555 1555 1.42
LINK OE2 GLU D 366 C5 JAZ D1464 1555 1555 1.45
LINK OE2 GLU E 366 C5 JAZ E1464 1555 1555 1.43
LINK OE2 GLU F 366 C5 JAZ F1464 1555 1555 1.41
SITE 1 AC1 16 GLN D 18 HIS D 119 ASN D 164 TYR D 299
SITE 2 AC1 16 LYS D 337 GLU D 366 TRP D 416 SER D 423
SITE 3 AC1 16 TRP D 424 TYR D 432 HOH D2050 HOH D2067
SITE 4 AC1 16 HOH D2095 HOH D2103 HOH D2121 HOH D2130
SITE 1 AC2 16 GLN A 18 HIS A 119 ASN A 164 GLU A 165
SITE 2 AC2 16 TYR A 299 LYS A 337 GLU A 366 TRP A 416
SITE 3 AC2 16 SER A 423 TRP A 424 TYR A 432 HOH A2060
SITE 4 AC2 16 HOH A2092 HOH A2175 HOH A2195 HOH A2213
SITE 1 AC3 17 GLN B 18 HIS B 119 ASN B 164 TYR B 299
SITE 2 AC3 17 LYS B 337 TRP B 339 GLU B 366 TRP B 416
SITE 3 AC3 17 SER B 423 TRP B 424 TYR B 432 EDO B1468
SITE 4 AC3 17 HOH B2061 HOH B2090 HOH B2146 HOH B2177
SITE 5 AC3 17 HOH B2208
SITE 1 AC4 17 GLN C 18 HIS C 119 ASN C 164 TYR C 299
SITE 2 AC4 17 LYS C 337 TRP C 339 GLU C 366 TRP C 416
SITE 3 AC4 17 SER C 423 TRP C 424 TYR C 432 HOH C2033
SITE 4 AC4 17 HOH C2058 HOH C2111 HOH C2138 HOH C2156
SITE 5 AC4 17 HOH C2172
SITE 1 AC5 16 GLN E 18 HIS E 119 ASN E 164 TYR E 299
SITE 2 AC5 16 LYS E 337 TRP E 339 GLU E 366 TRP E 416
SITE 3 AC5 16 SER E 423 TRP E 424 TYR E 432 HOH E2050
SITE 4 AC5 16 HOH E2068 HOH E2098 HOH E2129 HOH E2134
SITE 1 AC6 16 GLN F 18 HIS F 119 ASN F 164 TYR F 299
SITE 2 AC6 16 LYS F 337 TRP F 339 GLU F 366 TRP F 416
SITE 3 AC6 16 SER F 423 TRP F 424 TYR F 432 HOH F2036
SITE 4 AC6 16 HOH F2048 HOH F2068 HOH F2077 HOH F2088
SITE 1 AC7 5 GLU C 235 MET C 238 HIS C 242 HOH C2095
SITE 2 AC7 5 HOH C2173
SITE 1 AC8 4 GLU F 436 ASN F 438 VAL F 443 ARG F 445
SITE 1 AC9 6 ARG F 431 GLU F 436 ASN F 437 HOH F2081
SITE 2 AC9 6 HOH F2083 HOH F2092
SITE 1 BC1 3 ARG A 112 ASP A 159 ARG A 218
SITE 1 BC2 3 GLU B 7 ASN B 71 ARG B 112
SITE 1 BC3 4 ASP B 40 PHE B 42 TYR B 43 ASP B 44
SITE 1 BC4 4 GLU A 7 ASN A 71 ARG A 112 HOH A2056
SITE 1 BC5 2 ARG C 303 TYR C 342
SITE 1 BC6 6 TYR A 35 TYR A 45 GLY A 47 HOH A2038
SITE 2 BC6 6 TYR C 35 TYR C 45
SITE 1 BC7 5 TRP B 9 ARG B 112 LYS B 158 ASP B 159
SITE 2 BC7 5 ARG B 218
SITE 1 BC8 5 GLU D 7 TRP D 9 ASN D 71 ARG D 112
SITE 2 BC8 5 HOH D2048
SITE 1 BC9 6 PRO A 307 ALA A 309 PRO A 311 GLU A 320
SITE 2 BC9 6 TRP A 321 EDO A1469
SITE 1 CC1 5 GLU A 320 TYR A 323 ASP A 324 PRO A 325
SITE 2 CC1 5 EDO A1468
SITE 1 CC2 5 ARG D 112 LYS D 158 ASP D 159 GLY D 217
SITE 2 CC2 5 ARG D 218
SITE 1 CC3 3 TYR E 229 ARG E 303 TYR E 342
SITE 1 CC4 5 HIS B 179 TRP B 424 JAZ B1464 HOH B2100
SITE 2 CC4 5 HOH B2224
SITE 1 CC5 5 ASP C 40 PHE C 42 TYR C 43 ASP C 44
SITE 2 CC5 5 TYR C 45
SITE 1 CC6 4 ASP D 40 PHE D 42 ASP D 44 TYR D 45
SITE 1 CC7 3 ALA B 24 ASN B 92 ASP B 94
SITE 1 CC8 4 GLU D 436 ASN D 438 VAL D 443 ARG D 445
SITE 1 CC9 3 HIS C 27 ARG C 28 HOH C2017
SITE 1 DC1 3 HIS A 27 ARG A 28 HOH A2025
SITE 1 DC2 3 HIS E 27 ARG E 28 HOH E2025
SITE 1 DC3 4 HIS B 27 ARG B 28 HOH B2026 HOH B2027
SITE 1 DC4 3 HIS F 27 ARG F 28 HOH F2015
SITE 1 DC5 3 HIS D 27 ARG D 28 HOH D2023
SITE 1 DC6 3 GLU A 165 MET A 167 HOH A2130
SITE 1 DC7 3 LYS D 394 TRP D 452 ILE D 463
SITE 1 DC8 3 LYS B 394 TRP B 452 ILE B 463
CRYST1 103.017 109.899 158.500 90.00 92.02 90.00 P 1 21 1 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009707 0.000000 0.000342 0.00000
SCALE2 0.000000 0.009099 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006313 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
