HEADER HYDROLASE 14-JUL-09 3IAP
TITLE E. COLI (LACZ) BETA-GALACTOSIDASE (E416Q)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-GALACTOSIDASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: BETA-GALACTOSIDASE;
COMPND 5 EC: 3.2.1.23;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 GENE: LACZ;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: LMG194;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBAD/HIS/LACZ
KEYWDS GLU-416-GLN BETA-GALACTOSIDASE HYDROLASE TIM BARREL(ALPHA/BETA
KEYWDS 2 BARREL) JELLY-ROLL BARREL IMMUNOGLOBULIN BETA SUPERSANDWHICH,
KEYWDS 3 GLYCOSIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LO,M.L.DUGDALE,N.JEERH,T.KU,N.J.ROTH,R.E.HUBER
REVDAT 6 06-SEP-23 3IAP 1 REMARK
REVDAT 5 13-OCT-21 3IAP 1 REMARK SEQADV LINK
REVDAT 4 24-JUL-19 3IAP 1 REMARK
REVDAT 3 29-NOV-17 3IAP 1 REMARK
REVDAT 2 02-FEB-10 3IAP 1 JRNL
REVDAT 1 29-DEC-09 3IAP 0
JRNL AUTH S.LO,M.L.DUGDALE,N.JEERH,T.KU,N.J.ROTH,R.E.HUBER
JRNL TITL STUDIES OF GLU-416 VARIANTS OF BETA-GALACTOSIDASE (E. COLI)
JRNL TITL 2 SHOW THAT THE ACTIVE SITE MG(2+) IS NOT IMPORTANT FOR
JRNL TITL 3 STRUCTURE AND INDICATE THAT THE MAIN ROLE OF MG (2+) IS TO
JRNL TITL 4 MEDIATE OPTIMIZATION OF ACTIVE SITE CHEMISTRY
JRNL REF PROTEIN J. V. 29 26 2010
JRNL REFN ISSN 1572-3887
JRNL PMID 19936901
JRNL DOI 10.1007/S10930-009-9216-X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 TITL CRYSTALLOGRAPHY & NMR SYSTEM
REMARK 1 REF TO BE PUBLISHED 1998
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 120198
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.400
REMARK 3 FREE R VALUE TEST SET COUNT : 4186
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 18035
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE SET COUNT : 264
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 32500
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 580
REMARK 3 SOLVENT ATOMS : 3832
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.187
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.159
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.104
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.695
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 33895 ; 0.006 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 46099 ; 0.971 ; 1.936
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 4040 ; 5.694 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1748 ;34.823 ;23.730
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5156 ;12.425 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 264 ;14.535 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4885 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 26568 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 15494 ; 0.166 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 22104 ; 0.299 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 3593 ; 0.093 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 15 ; 0.130 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 106 ; 0.123 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 35 ; 0.105 ; 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): 20317 ; 0.903 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 32814 ; 1.585 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 14477 ; 1.993 ; 3.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 13285 ; 3.084 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 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 3IAP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1000054176.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.11589
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : KOHZU: DOUBLE CRYSTAL SI(111)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 120198
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 58.420
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.0
REMARK 200 DATA REDUNDANCY : 3.290
REMARK 200 R MERGE (I) : 0.14900
REMARK 200 R SYM (I) : 0.19800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.22
REMARK 200 R MERGE FOR SHELL (I) : 0.40800
REMARK 200 R SYM FOR SHELL (I) : 0.53900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1DP0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, NACL, MGCL2, DTT, BIS-TRIS,
REMARK 280 PH6.5, HANGING DROP AT 288K, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 75.61500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 101.03000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 81.17000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 101.03000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 75.61500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 81.17000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 139280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 1
REMARK 465 SER A 2
REMARK 465 HIS A 3
REMARK 465 MET A 4
REMARK 465 LEU A 5
REMARK 465 GLU A 6
REMARK 465 ASP A 7
REMARK 465 PRO A 8
REMARK 465 VAL A 9
REMARK 465 VAL A 10
REMARK 465 LEU A 11
REMARK 465 GLN A 12
REMARK 465 GLY B 1
REMARK 465 SER B 2
REMARK 465 HIS B 3
REMARK 465 MET B 4
REMARK 465 LEU B 5
REMARK 465 GLU B 6
REMARK 465 ASP B 7
REMARK 465 PRO B 8
REMARK 465 VAL B 9
REMARK 465 VAL B 10
REMARK 465 LEU B 11
REMARK 465 GLN B 12
REMARK 465 GLY C 1
REMARK 465 SER C 2
REMARK 465 HIS C 3
REMARK 465 MET C 4
REMARK 465 LEU C 5
REMARK 465 GLU C 6
REMARK 465 ASP C 7
REMARK 465 PRO C 8
REMARK 465 VAL C 9
REMARK 465 VAL C 10
REMARK 465 LEU C 11
REMARK 465 GLN C 12
REMARK 465 GLY D 1
REMARK 465 SER D 2
REMARK 465 HIS D 3
REMARK 465 MET D 4
REMARK 465 LEU D 5
REMARK 465 GLU D 6
REMARK 465 ASP D 7
REMARK 465 PRO D 8
REMARK 465 VAL D 9
REMARK 465 VAL D 10
REMARK 465 LEU D 11
REMARK 465 GLN D 12
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 ASN A 102 -80.24 -91.38
REMARK 500 ASP A 164 104.21 72.83
REMARK 500 ASP A 199 37.42 -92.83
REMARK 500 ARG A 352 76.15 -100.39
REMARK 500 ALA A 491 -3.38 70.01
REMARK 500 ALA A 514 -41.49 69.36
REMARK 500 HIS A 540 107.11 -58.48
REMARK 500 ALA A 541 43.12 -87.85
REMARK 500 GLN A 573 55.16 -95.45
REMARK 500 TYR A 588 -167.71 -114.17
REMARK 500 ASP A 598 49.86 -104.17
REMARK 500 ARG A 599 -122.15 34.94
REMARK 500 ASN A 649 50.85 -144.85
REMARK 500 ASP A 659 50.66 38.78
REMARK 500 LEU A 722 -144.26 -102.02
REMARK 500 ASP A 916 -178.89 -172.18
REMARK 500 ASN B 102 -85.24 -89.82
REMARK 500 ASN B 110 76.69 -150.27
REMARK 500 ASP B 164 102.46 77.89
REMARK 500 ASP B 199 47.28 -96.05
REMARK 500 GLU B 461 62.44 39.17
REMARK 500 ALA B 491 -3.50 73.03
REMARK 500 ALA B 514 -38.50 72.09
REMARK 500 ALA B 541 46.50 -97.10
REMARK 500 GLN B 573 55.09 -98.04
REMARK 500 ASP B 579 -154.53 -92.16
REMARK 500 TYR B 588 -165.24 -111.97
REMARK 500 ARG B 599 -127.64 33.85
REMARK 500 ASN B 649 48.22 -148.19
REMARK 500 LEU B 722 -142.10 -100.07
REMARK 500 ARG B 909 63.68 -151.49
REMARK 500 ASP B 954 84.94 -151.09
REMARK 500 ALA C 34 -12.24 -142.94
REMARK 500 ASN C 102 -72.89 -86.93
REMARK 500 ASP C 164 99.26 72.21
REMARK 500 MET C 202 -179.77 -173.60
REMARK 500 ARG C 352 78.00 -101.42
REMARK 500 GLU C 461 62.59 39.71
REMARK 500 ALA C 491 -4.56 72.80
REMARK 500 ALA C 514 -38.46 72.60
REMARK 500 ALA C 539 70.05 49.68
REMARK 500 ALA C 541 46.86 -91.65
REMARK 500 GLN C 573 57.06 -92.56
REMARK 500 TYR C 588 -162.53 -113.89
REMARK 500 ARG C 599 -131.29 38.54
REMARK 500 ASN C 649 47.40 -150.33
REMARK 500 LEU C 722 -138.74 -100.32
REMARK 500 ARG C 909 65.84 -153.00
REMARK 500 ASN D 102 -91.49 -96.04
REMARK 500 ASP D 164 102.45 74.08
REMARK 500
REMARK 500 THIS ENTRY HAS 62 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A3001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 15 O
REMARK 620 2 ASN A 18 O 104.4
REMARK 620 3 VAL A 21 O 111.5 84.5
REMARK 620 4 GLN A 163 NE2 99.0 155.1 95.2
REMARK 620 5 ASP A 193 OD2 92.5 83.0 155.1 87.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A3101 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 556 O
REMARK 620 2 TYR A 559 O 85.9
REMARK 620 3 LEU A 562 O 91.2 92.0
REMARK 620 4 HOH A4227 O 84.2 89.7 175.0
REMARK 620 5 HOH A4649 O 115.1 154.9 100.9 79.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A3104 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 601 O
REMARK 620 2 ASN A 604 OD1 64.9
REMARK 620 3 HOH A4947 O 83.9 69.7
REMARK 620 4 BTB A6001 O3 144.6 127.8 73.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A3103 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 647 O
REMARK 620 2 GLU A 650 O 107.1
REMARK 620 3 LEU A 670 O 69.6 88.8
REMARK 620 4 HOH A4686 O 71.0 153.6 65.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A3102 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO A 932 O
REMARK 620 2 LEU A 967 O 74.3
REMARK 620 3 THR A 970 O 112.3 83.5
REMARK 620 4 HOH A4213 O 148.0 133.6 89.6
REMARK 620 5 HOH A4610 O 100.5 107.0 147.2 60.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A3002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A4192 O
REMARK 620 2 HOH A4482 O 99.0
REMARK 620 3 HOH A4941 O 122.3 98.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B3001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 15 O
REMARK 620 2 ASN B 18 O 106.0
REMARK 620 3 VAL B 21 O 111.7 84.6
REMARK 620 4 GLN B 163 NE2 100.8 152.2 92.4
REMARK 620 5 ASP B 193 OD2 94.1 83.1 153.7 87.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B3104 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 201 OD2
REMARK 620 2 PHE B 601 O 109.4
REMARK 620 3 ASN B 604 ND2 169.3 80.7
REMARK 620 4 HOH B4695 O 103.4 105.6 76.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B3101 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE B 556 O
REMARK 620 2 TYR B 559 O 90.7
REMARK 620 3 LEU B 562 O 91.0 86.0
REMARK 620 4 HOH B4437 O 84.9 86.3 171.3
REMARK 620 5 HOH B4468 O 120.0 149.2 95.7 93.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B3103 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 647 O
REMARK 620 2 GLU B 650 O 107.8
REMARK 620 3 LEU B 670 O 66.8 86.3
REMARK 620 4 DMS B7016 O 115.8 100.0 171.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B3002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 718 OE1
REMARK 620 2 HOH B4236 O 89.8
REMARK 620 3 HOH B4466 O 164.8 100.9
REMARK 620 4 HOH B4574 O 75.6 95.1 113.6
REMARK 620 5 HOH B4594 O 58.1 110.0 107.6 125.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B3102 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO B 932 O
REMARK 620 2 LEU B 967 O 72.5
REMARK 620 3 THR B 970 O 112.6 78.7
REMARK 620 4 HOH B4415 O 95.7 108.7 151.5
REMARK 620 5 HOH B4518 O 149.4 133.7 90.8 63.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C3001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 15 O
REMARK 620 2 ASN C 18 O 99.2
REMARK 620 3 VAL C 21 O 110.6 86.9
REMARK 620 4 GLN C 163 NE2 99.1 158.2 97.8
REMARK 620 5 ASP C 193 OD2 91.0 81.0 156.8 86.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C3101 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE C 556 O
REMARK 620 2 TYR C 559 O 86.0
REMARK 620 3 LEU C 562 O 90.2 83.7
REMARK 620 4 HOH C4337 O 85.5 88.8 171.5
REMARK 620 5 HOH C4485 O 117.3 156.2 99.8 88.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C3104 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE C 601 O
REMARK 620 2 ASN C 604 OD1 66.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C3103 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER C 647 O
REMARK 620 2 GLU C 650 O 107.4
REMARK 620 3 LEU C 670 O 69.4 85.2
REMARK 620 4 DMS C7017 O 130.2 113.9 138.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C3002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN C 718 OE1
REMARK 620 2 HOH C4235 O 86.5
REMARK 620 3 HOH C4324 O 164.1 109.2
REMARK 620 4 HOH C4519 O 56.8 100.5 120.0
REMARK 620 5 HOH C4636 O 63.2 87.0 114.0 118.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C3102 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO C 932 O
REMARK 620 2 LEU C 967 O 72.9
REMARK 620 3 THR C 970 O 113.1 81.8
REMARK 620 4 HOH C4434 O 97.9 103.2 148.5
REMARK 620 5 HOH C4538 O 152.5 130.1 87.7 65.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D3001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 15 O
REMARK 620 2 ASN D 18 O 99.2
REMARK 620 3 VAL D 21 O 108.2 86.2
REMARK 620 4 GLN D 163 NE2 98.9 160.3 95.4
REMARK 620 5 ASP D 193 OD2 89.3 85.6 161.7 87.0
REMARK 620 6 ASP D 193 OD1 136.7 80.5 114.9 81.1 47.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D3103 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 201 OD2
REMARK 620 2 PHE D 601 O 106.7
REMARK 620 3 ASN D 604 ND2 167.0 83.4
REMARK 620 4 BTB D6001 O1 55.6 158.9 116.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D3101 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE D 556 O
REMARK 620 2 TYR D 559 O 86.9
REMARK 620 3 LEU D 562 O 89.3 90.9
REMARK 620 4 HOH D4357 O 82.1 82.5 169.4
REMARK 620 5 HOH D4494 O 116.7 155.8 94.8 94.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D3104 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER D 647 O
REMARK 620 2 GLU D 650 O 105.6
REMARK 620 3 LEU D 670 O 67.2 84.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D3002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN D 718 OE1
REMARK 620 2 HOH D4247 O 90.9
REMARK 620 3 HOH D4520 O 59.1 115.2
REMARK 620 4 HOH D4894 O 67.1 97.2 115.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D3102 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO D 932 O
REMARK 620 2 LEU D 967 O 72.6
REMARK 620 3 THR D 970 O 112.1 84.0
REMARK 620 4 HOH D4440 O 102.3 109.0 145.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 3101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 3102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 3103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 3104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB A 6001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7002
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7004
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7005
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7006
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7007
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7008
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7009
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7010
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7011
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7012
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7013
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7014
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7015
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7016
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7017
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7018
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7019
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7020
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7021
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7022
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7023
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7024
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7025
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7026
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7027
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7028
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7029
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7030
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7031
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 7032
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 3101
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 3102
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 3103
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 3104
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB B 6001
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7001
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7002
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7003
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7004
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7005
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7006
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7007
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7008
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7009
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7010
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7011
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7012
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7013
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7014
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7015
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7016
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7017
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7018
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7019
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7020
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7021
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7022
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7023
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7024
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7025
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7026
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7027
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7028
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7029
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7030
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7031
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7032
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 7033
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7034
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 3101
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 3102
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 3103
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 3104
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB C 6001
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7001
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7002
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7003
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7004
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7005
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7006
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7007
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7008
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7009
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7010
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7011
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7012
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7013
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7014
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7015
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7016
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7017
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7018
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7019
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7020
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7021
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7022
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7023
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7024
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7025
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7026
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7027
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7028
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7029
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7030
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 7031
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 3101
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 3102
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 3103
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 3104
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB D 6001
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7001
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7002
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7003
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7004
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7005
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7006
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7007
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7009
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7010
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7011
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7012
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7013
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7014
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7015
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7016
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7017
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7018
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7019
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7020
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7021
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7022
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7023
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7024
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7025
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7026
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7027
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7028
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 7029
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DP0 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN BUT WILD TYPE
REMARK 900 RELATED ID: 3DYP RELATED DB: PDB
REMARK 900 THE SAME PROTEIN BUT WITH H418N MUTATION INSTEAD OF E416Q
REMARK 900 RELATED ID: 3DYM RELATED DB: PDB
REMARK 900 THE SAME PROTEIN BUT WITH H418E MUTATION INSTEAD OF E416Q
REMARK 900 RELATED ID: 3IAQ RELATED DB: PDB
DBREF 3IAP A 9 1023 UNP B8LFD6 B8LFD6_ECOLI 10 1024
DBREF 3IAP B 9 1023 UNP B8LFD6 B8LFD6_ECOLI 10 1024
DBREF 3IAP C 9 1023 UNP B8LFD6 B8LFD6_ECOLI 10 1024
DBREF 3IAP D 9 1023 UNP B8LFD6 B8LFD6_ECOLI 10 1024
SEQADV 3IAP GLY A 1 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP SER A 2 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP HIS A 3 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP MET A 4 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP LEU A 5 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP GLU A 6 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP ASP A 7 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP PRO A 8 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP GLN A 416 UNP B8LFD6 GLU 417 ENGINEERED MUTATION
SEQADV 3IAP GLY B 1 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP SER B 2 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP HIS B 3 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP MET B 4 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP LEU B 5 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP GLU B 6 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP ASP B 7 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP PRO B 8 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP GLN B 416 UNP B8LFD6 GLU 417 ENGINEERED MUTATION
SEQADV 3IAP GLY C 1 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP SER C 2 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP HIS C 3 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP MET C 4 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP LEU C 5 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP GLU C 6 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP ASP C 7 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP PRO C 8 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP GLN C 416 UNP B8LFD6 GLU 417 ENGINEERED MUTATION
SEQADV 3IAP GLY D 1 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP SER D 2 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP HIS D 3 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP MET D 4 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP LEU D 5 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP GLU D 6 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP ASP D 7 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP PRO D 8 UNP B8LFD6 EXPRESSION TAG
SEQADV 3IAP GLN D 416 UNP B8LFD6 GLU 417 ENGINEERED MUTATION
SEQRES 1 A 1023 GLY SER HIS MET LEU GLU ASP PRO VAL VAL LEU GLN ARG
SEQRES 2 A 1023 ARG ASP TRP GLU ASN PRO GLY VAL THR GLN LEU ASN ARG
SEQRES 3 A 1023 LEU ALA ALA HIS PRO PRO PHE ALA SER TRP ARG ASN SER
SEQRES 4 A 1023 GLU GLU ALA ARG THR ASP ARG PRO SER GLN GLN LEU ARG
SEQRES 5 A 1023 SER LEU ASN GLY GLU TRP ARG PHE ALA TRP PHE PRO ALA
SEQRES 6 A 1023 PRO GLU ALA VAL PRO GLU SER TRP LEU GLU CYS ASP LEU
SEQRES 7 A 1023 PRO GLU ALA ASP THR VAL VAL VAL PRO SER ASN TRP GLN
SEQRES 8 A 1023 MET HIS GLY TYR ASP ALA PRO ILE TYR THR ASN VAL THR
SEQRES 9 A 1023 TYR PRO ILE THR VAL ASN PRO PRO PHE VAL PRO THR GLU
SEQRES 10 A 1023 ASN PRO THR GLY CYS TYR SER LEU THR PHE ASN VAL ASP
SEQRES 11 A 1023 GLU SER TRP LEU GLN GLU GLY GLN THR ARG ILE ILE PHE
SEQRES 12 A 1023 ASP GLY VAL ASN SER ALA PHE HIS LEU TRP CYS ASN GLY
SEQRES 13 A 1023 ARG TRP VAL GLY TYR GLY GLN ASP SER ARG LEU PRO SER
SEQRES 14 A 1023 GLU PHE ASP LEU SER ALA PHE LEU ARG ALA GLY GLU ASN
SEQRES 15 A 1023 ARG LEU ALA VAL MET VAL LEU ARG TRP SER ASP GLY SER
SEQRES 16 A 1023 TYR LEU GLU ASP GLN ASP MET TRP ARG MET SER GLY ILE
SEQRES 17 A 1023 PHE ARG ASP VAL SER LEU LEU HIS LYS PRO THR THR GLN
SEQRES 18 A 1023 ILE SER ASP PHE HIS VAL ALA THR ARG PHE ASN ASP ASP
SEQRES 19 A 1023 PHE SER ARG ALA VAL LEU GLU ALA GLU VAL GLN MET CYS
SEQRES 20 A 1023 GLY GLU LEU ARG ASP TYR LEU ARG VAL THR VAL SER LEU
SEQRES 21 A 1023 TRP GLN GLY GLU THR GLN VAL ALA SER GLY THR ALA PRO
SEQRES 22 A 1023 PHE GLY GLY GLU ILE ILE ASP GLU ARG GLY GLY TYR ALA
SEQRES 23 A 1023 ASP ARG VAL THR LEU ARG LEU ASN VAL GLU ASN PRO LYS
SEQRES 24 A 1023 LEU TRP SER ALA GLU ILE PRO ASN LEU TYR ARG ALA VAL
SEQRES 25 A 1023 VAL GLU LEU HIS THR ALA ASP GLY THR LEU ILE GLU ALA
SEQRES 26 A 1023 GLU ALA CYS ASP VAL GLY PHE ARG GLU VAL ARG ILE GLU
SEQRES 27 A 1023 ASN GLY LEU LEU LEU LEU ASN GLY LYS PRO LEU LEU ILE
SEQRES 28 A 1023 ARG GLY VAL ASN ARG HIS GLU HIS HIS PRO LEU HIS GLY
SEQRES 29 A 1023 GLN VAL MET ASP GLU GLN THR MET VAL GLN ASP ILE LEU
SEQRES 30 A 1023 LEU MET LYS GLN ASN ASN PHE ASN ALA VAL ARG CYS SER
SEQRES 31 A 1023 HIS TYR PRO ASN HIS PRO LEU TRP TYR THR LEU CYS ASP
SEQRES 32 A 1023 ARG TYR GLY LEU TYR VAL VAL ASP GLU ALA ASN ILE GLN
SEQRES 33 A 1023 THR HIS GLY MET VAL PRO MET ASN ARG LEU THR ASP ASP
SEQRES 34 A 1023 PRO ARG TRP LEU PRO ALA MET SER GLU ARG VAL THR ARG
SEQRES 35 A 1023 MET VAL GLN ARG ASP ARG ASN HIS PRO SER VAL ILE ILE
SEQRES 36 A 1023 TRP SER LEU GLY ASN GLU SER GLY HIS GLY ALA ASN HIS
SEQRES 37 A 1023 ASP ALA LEU TYR ARG TRP ILE LYS SER VAL ASP PRO SER
SEQRES 38 A 1023 ARG PRO VAL GLN TYR GLU GLY GLY GLY ALA ASP THR THR
SEQRES 39 A 1023 ALA THR ASP ILE ILE CYS PRO MET TYR ALA ARG VAL ASP
SEQRES 40 A 1023 GLU ASP GLN PRO PHE PRO ALA VAL PRO LYS TRP SER ILE
SEQRES 41 A 1023 LYS LYS TRP LEU SER LEU PRO GLY GLU THR ARG PRO LEU
SEQRES 42 A 1023 ILE LEU CYS GLU TYR ALA HIS ALA MET GLY ASN SER LEU
SEQRES 43 A 1023 GLY GLY PHE ALA LYS TYR TRP GLN ALA PHE ARG GLN TYR
SEQRES 44 A 1023 PRO ARG LEU GLN GLY GLY PHE VAL TRP ASP TRP VAL ASP
SEQRES 45 A 1023 GLN SER LEU ILE LYS TYR ASP GLU ASN GLY ASN PRO TRP
SEQRES 46 A 1023 SER ALA TYR GLY GLY ASP PHE GLY ASP THR PRO ASN ASP
SEQRES 47 A 1023 ARG GLN PHE CYS MET ASN GLY LEU VAL PHE ALA ASP ARG
SEQRES 48 A 1023 THR PRO HIS PRO ALA LEU THR GLU ALA LYS HIS GLN GLN
SEQRES 49 A 1023 GLN PHE PHE GLN PHE ARG LEU SER GLY GLN THR ILE GLU
SEQRES 50 A 1023 VAL THR SER GLU TYR LEU PHE ARG HIS SER ASP ASN GLU
SEQRES 51 A 1023 LEU LEU HIS TRP MET VAL ALA LEU ASP GLY LYS PRO LEU
SEQRES 52 A 1023 ALA SER GLY GLU VAL PRO LEU ASP VAL ALA PRO GLN GLY
SEQRES 53 A 1023 LYS GLN LEU ILE GLU LEU PRO GLU LEU PRO GLN PRO GLU
SEQRES 54 A 1023 SER ALA GLY GLN LEU TRP LEU THR VAL ARG VAL VAL GLN
SEQRES 55 A 1023 PRO ASN ALA THR ALA TRP SER GLU ALA GLY HIS ILE SER
SEQRES 56 A 1023 ALA TRP GLN GLN TRP ARG LEU ALA GLU ASN LEU SER VAL
SEQRES 57 A 1023 THR LEU PRO ALA ALA SER HIS ALA ILE PRO HIS LEU THR
SEQRES 58 A 1023 THR SER GLU MET ASP PHE CYS ILE GLU LEU GLY ASN LYS
SEQRES 59 A 1023 ARG TRP GLN PHE ASN ARG GLN SER GLY PHE LEU SER GLN
SEQRES 60 A 1023 MET TRP ILE GLY ASP LYS LYS GLN LEU LEU THR PRO LEU
SEQRES 61 A 1023 ARG ASP GLN PHE THR ARG ALA PRO LEU ASP ASN ASP ILE
SEQRES 62 A 1023 GLY VAL SER GLU ALA THR ARG ILE ASP PRO ASN ALA TRP
SEQRES 63 A 1023 VAL GLU ARG TRP LYS ALA ALA GLY HIS TYR GLN ALA GLU
SEQRES 64 A 1023 ALA ALA LEU LEU GLN CYS THR ALA ASP THR LEU ALA ASP
SEQRES 65 A 1023 ALA VAL LEU ILE THR THR ALA HIS ALA TRP GLN HIS GLN
SEQRES 66 A 1023 GLY LYS THR LEU PHE ILE SER ARG LYS THR TYR ARG ILE
SEQRES 67 A 1023 ASP GLY SER GLY GLN MET ALA ILE THR VAL ASP VAL GLU
SEQRES 68 A 1023 VAL ALA SER ASP THR PRO HIS PRO ALA ARG ILE GLY LEU
SEQRES 69 A 1023 ASN CYS GLN LEU ALA GLN VAL ALA GLU ARG VAL ASN TRP
SEQRES 70 A 1023 LEU GLY LEU GLY PRO GLN GLU ASN TYR PRO ASP ARG LEU
SEQRES 71 A 1023 THR ALA ALA CYS PHE ASP ARG TRP ASP LEU PRO LEU SER
SEQRES 72 A 1023 ASP MET TYR THR PRO TYR VAL PHE PRO SER GLU ASN GLY
SEQRES 73 A 1023 LEU ARG CYS GLY THR ARG GLU LEU ASN TYR GLY PRO HIS
SEQRES 74 A 1023 GLN TRP ARG GLY ASP PHE GLN PHE ASN ILE SER ARG TYR
SEQRES 75 A 1023 SER GLN GLN GLN LEU MET GLU THR SER HIS ARG HIS LEU
SEQRES 76 A 1023 LEU HIS ALA GLU GLU GLY THR TRP LEU ASN ILE ASP GLY
SEQRES 77 A 1023 PHE HIS MET GLY ILE GLY GLY ASP ASP SER TRP SER PRO
SEQRES 78 A 1023 SER VAL SER ALA GLU PHE GLN LEU SER ALA GLY ARG TYR
SEQRES 79 A 1023 HIS TYR GLN LEU VAL TRP CYS GLN LYS
SEQRES 1 B 1023 GLY SER HIS MET LEU GLU ASP PRO VAL VAL LEU GLN ARG
SEQRES 2 B 1023 ARG ASP TRP GLU ASN PRO GLY VAL THR GLN LEU ASN ARG
SEQRES 3 B 1023 LEU ALA ALA HIS PRO PRO PHE ALA SER TRP ARG ASN SER
SEQRES 4 B 1023 GLU GLU ALA ARG THR ASP ARG PRO SER GLN GLN LEU ARG
SEQRES 5 B 1023 SER LEU ASN GLY GLU TRP ARG PHE ALA TRP PHE PRO ALA
SEQRES 6 B 1023 PRO GLU ALA VAL PRO GLU SER TRP LEU GLU CYS ASP LEU
SEQRES 7 B 1023 PRO GLU ALA ASP THR VAL VAL VAL PRO SER ASN TRP GLN
SEQRES 8 B 1023 MET HIS GLY TYR ASP ALA PRO ILE TYR THR ASN VAL THR
SEQRES 9 B 1023 TYR PRO ILE THR VAL ASN PRO PRO PHE VAL PRO THR GLU
SEQRES 10 B 1023 ASN PRO THR GLY CYS TYR SER LEU THR PHE ASN VAL ASP
SEQRES 11 B 1023 GLU SER TRP LEU GLN GLU GLY GLN THR ARG ILE ILE PHE
SEQRES 12 B 1023 ASP GLY VAL ASN SER ALA PHE HIS LEU TRP CYS ASN GLY
SEQRES 13 B 1023 ARG TRP VAL GLY TYR GLY GLN ASP SER ARG LEU PRO SER
SEQRES 14 B 1023 GLU PHE ASP LEU SER ALA PHE LEU ARG ALA GLY GLU ASN
SEQRES 15 B 1023 ARG LEU ALA VAL MET VAL LEU ARG TRP SER ASP GLY SER
SEQRES 16 B 1023 TYR LEU GLU ASP GLN ASP MET TRP ARG MET SER GLY ILE
SEQRES 17 B 1023 PHE ARG ASP VAL SER LEU LEU HIS LYS PRO THR THR GLN
SEQRES 18 B 1023 ILE SER ASP PHE HIS VAL ALA THR ARG PHE ASN ASP ASP
SEQRES 19 B 1023 PHE SER ARG ALA VAL LEU GLU ALA GLU VAL GLN MET CYS
SEQRES 20 B 1023 GLY GLU LEU ARG ASP TYR LEU ARG VAL THR VAL SER LEU
SEQRES 21 B 1023 TRP GLN GLY GLU THR GLN VAL ALA SER GLY THR ALA PRO
SEQRES 22 B 1023 PHE GLY GLY GLU ILE ILE ASP GLU ARG GLY GLY TYR ALA
SEQRES 23 B 1023 ASP ARG VAL THR LEU ARG LEU ASN VAL GLU ASN PRO LYS
SEQRES 24 B 1023 LEU TRP SER ALA GLU ILE PRO ASN LEU TYR ARG ALA VAL
SEQRES 25 B 1023 VAL GLU LEU HIS THR ALA ASP GLY THR LEU ILE GLU ALA
SEQRES 26 B 1023 GLU ALA CYS ASP VAL GLY PHE ARG GLU VAL ARG ILE GLU
SEQRES 27 B 1023 ASN GLY LEU LEU LEU LEU ASN GLY LYS PRO LEU LEU ILE
SEQRES 28 B 1023 ARG GLY VAL ASN ARG HIS GLU HIS HIS PRO LEU HIS GLY
SEQRES 29 B 1023 GLN VAL MET ASP GLU GLN THR MET VAL GLN ASP ILE LEU
SEQRES 30 B 1023 LEU MET LYS GLN ASN ASN PHE ASN ALA VAL ARG CYS SER
SEQRES 31 B 1023 HIS TYR PRO ASN HIS PRO LEU TRP TYR THR LEU CYS ASP
SEQRES 32 B 1023 ARG TYR GLY LEU TYR VAL VAL ASP GLU ALA ASN ILE GLN
SEQRES 33 B 1023 THR HIS GLY MET VAL PRO MET ASN ARG LEU THR ASP ASP
SEQRES 34 B 1023 PRO ARG TRP LEU PRO ALA MET SER GLU ARG VAL THR ARG
SEQRES 35 B 1023 MET VAL GLN ARG ASP ARG ASN HIS PRO SER VAL ILE ILE
SEQRES 36 B 1023 TRP SER LEU GLY ASN GLU SER GLY HIS GLY ALA ASN HIS
SEQRES 37 B 1023 ASP ALA LEU TYR ARG TRP ILE LYS SER VAL ASP PRO SER
SEQRES 38 B 1023 ARG PRO VAL GLN TYR GLU GLY GLY GLY ALA ASP THR THR
SEQRES 39 B 1023 ALA THR ASP ILE ILE CYS PRO MET TYR ALA ARG VAL ASP
SEQRES 40 B 1023 GLU ASP GLN PRO PHE PRO ALA VAL PRO LYS TRP SER ILE
SEQRES 41 B 1023 LYS LYS TRP LEU SER LEU PRO GLY GLU THR ARG PRO LEU
SEQRES 42 B 1023 ILE LEU CYS GLU TYR ALA HIS ALA MET GLY ASN SER LEU
SEQRES 43 B 1023 GLY GLY PHE ALA LYS TYR TRP GLN ALA PHE ARG GLN TYR
SEQRES 44 B 1023 PRO ARG LEU GLN GLY GLY PHE VAL TRP ASP TRP VAL ASP
SEQRES 45 B 1023 GLN SER LEU ILE LYS TYR ASP GLU ASN GLY ASN PRO TRP
SEQRES 46 B 1023 SER ALA TYR GLY GLY ASP PHE GLY ASP THR PRO ASN ASP
SEQRES 47 B 1023 ARG GLN PHE CYS MET ASN GLY LEU VAL PHE ALA ASP ARG
SEQRES 48 B 1023 THR PRO HIS PRO ALA LEU THR GLU ALA LYS HIS GLN GLN
SEQRES 49 B 1023 GLN PHE PHE GLN PHE ARG LEU SER GLY GLN THR ILE GLU
SEQRES 50 B 1023 VAL THR SER GLU TYR LEU PHE ARG HIS SER ASP ASN GLU
SEQRES 51 B 1023 LEU LEU HIS TRP MET VAL ALA LEU ASP GLY LYS PRO LEU
SEQRES 52 B 1023 ALA SER GLY GLU VAL PRO LEU ASP VAL ALA PRO GLN GLY
SEQRES 53 B 1023 LYS GLN LEU ILE GLU LEU PRO GLU LEU PRO GLN PRO GLU
SEQRES 54 B 1023 SER ALA GLY GLN LEU TRP LEU THR VAL ARG VAL VAL GLN
SEQRES 55 B 1023 PRO ASN ALA THR ALA TRP SER GLU ALA GLY HIS ILE SER
SEQRES 56 B 1023 ALA TRP GLN GLN TRP ARG LEU ALA GLU ASN LEU SER VAL
SEQRES 57 B 1023 THR LEU PRO ALA ALA SER HIS ALA ILE PRO HIS LEU THR
SEQRES 58 B 1023 THR SER GLU MET ASP PHE CYS ILE GLU LEU GLY ASN LYS
SEQRES 59 B 1023 ARG TRP GLN PHE ASN ARG GLN SER GLY PHE LEU SER GLN
SEQRES 60 B 1023 MET TRP ILE GLY ASP LYS LYS GLN LEU LEU THR PRO LEU
SEQRES 61 B 1023 ARG ASP GLN PHE THR ARG ALA PRO LEU ASP ASN ASP ILE
SEQRES 62 B 1023 GLY VAL SER GLU ALA THR ARG ILE ASP PRO ASN ALA TRP
SEQRES 63 B 1023 VAL GLU ARG TRP LYS ALA ALA GLY HIS TYR GLN ALA GLU
SEQRES 64 B 1023 ALA ALA LEU LEU GLN CYS THR ALA ASP THR LEU ALA ASP
SEQRES 65 B 1023 ALA VAL LEU ILE THR THR ALA HIS ALA TRP GLN HIS GLN
SEQRES 66 B 1023 GLY LYS THR LEU PHE ILE SER ARG LYS THR TYR ARG ILE
SEQRES 67 B 1023 ASP GLY SER GLY GLN MET ALA ILE THR VAL ASP VAL GLU
SEQRES 68 B 1023 VAL ALA SER ASP THR PRO HIS PRO ALA ARG ILE GLY LEU
SEQRES 69 B 1023 ASN CYS GLN LEU ALA GLN VAL ALA GLU ARG VAL ASN TRP
SEQRES 70 B 1023 LEU GLY LEU GLY PRO GLN GLU ASN TYR PRO ASP ARG LEU
SEQRES 71 B 1023 THR ALA ALA CYS PHE ASP ARG TRP ASP LEU PRO LEU SER
SEQRES 72 B 1023 ASP MET TYR THR PRO TYR VAL PHE PRO SER GLU ASN GLY
SEQRES 73 B 1023 LEU ARG CYS GLY THR ARG GLU LEU ASN TYR GLY PRO HIS
SEQRES 74 B 1023 GLN TRP ARG GLY ASP PHE GLN PHE ASN ILE SER ARG TYR
SEQRES 75 B 1023 SER GLN GLN GLN LEU MET GLU THR SER HIS ARG HIS LEU
SEQRES 76 B 1023 LEU HIS ALA GLU GLU GLY THR TRP LEU ASN ILE ASP GLY
SEQRES 77 B 1023 PHE HIS MET GLY ILE GLY GLY ASP ASP SER TRP SER PRO
SEQRES 78 B 1023 SER VAL SER ALA GLU PHE GLN LEU SER ALA GLY ARG TYR
SEQRES 79 B 1023 HIS TYR GLN LEU VAL TRP CYS GLN LYS
SEQRES 1 C 1023 GLY SER HIS MET LEU GLU ASP PRO VAL VAL LEU GLN ARG
SEQRES 2 C 1023 ARG ASP TRP GLU ASN PRO GLY VAL THR GLN LEU ASN ARG
SEQRES 3 C 1023 LEU ALA ALA HIS PRO PRO PHE ALA SER TRP ARG ASN SER
SEQRES 4 C 1023 GLU GLU ALA ARG THR ASP ARG PRO SER GLN GLN LEU ARG
SEQRES 5 C 1023 SER LEU ASN GLY GLU TRP ARG PHE ALA TRP PHE PRO ALA
SEQRES 6 C 1023 PRO GLU ALA VAL PRO GLU SER TRP LEU GLU CYS ASP LEU
SEQRES 7 C 1023 PRO GLU ALA ASP THR VAL VAL VAL PRO SER ASN TRP GLN
SEQRES 8 C 1023 MET HIS GLY TYR ASP ALA PRO ILE TYR THR ASN VAL THR
SEQRES 9 C 1023 TYR PRO ILE THR VAL ASN PRO PRO PHE VAL PRO THR GLU
SEQRES 10 C 1023 ASN PRO THR GLY CYS TYR SER LEU THR PHE ASN VAL ASP
SEQRES 11 C 1023 GLU SER TRP LEU GLN GLU GLY GLN THR ARG ILE ILE PHE
SEQRES 12 C 1023 ASP GLY VAL ASN SER ALA PHE HIS LEU TRP CYS ASN GLY
SEQRES 13 C 1023 ARG TRP VAL GLY TYR GLY GLN ASP SER ARG LEU PRO SER
SEQRES 14 C 1023 GLU PHE ASP LEU SER ALA PHE LEU ARG ALA GLY GLU ASN
SEQRES 15 C 1023 ARG LEU ALA VAL MET VAL LEU ARG TRP SER ASP GLY SER
SEQRES 16 C 1023 TYR LEU GLU ASP GLN ASP MET TRP ARG MET SER GLY ILE
SEQRES 17 C 1023 PHE ARG ASP VAL SER LEU LEU HIS LYS PRO THR THR GLN
SEQRES 18 C 1023 ILE SER ASP PHE HIS VAL ALA THR ARG PHE ASN ASP ASP
SEQRES 19 C 1023 PHE SER ARG ALA VAL LEU GLU ALA GLU VAL GLN MET CYS
SEQRES 20 C 1023 GLY GLU LEU ARG ASP TYR LEU ARG VAL THR VAL SER LEU
SEQRES 21 C 1023 TRP GLN GLY GLU THR GLN VAL ALA SER GLY THR ALA PRO
SEQRES 22 C 1023 PHE GLY GLY GLU ILE ILE ASP GLU ARG GLY GLY TYR ALA
SEQRES 23 C 1023 ASP ARG VAL THR LEU ARG LEU ASN VAL GLU ASN PRO LYS
SEQRES 24 C 1023 LEU TRP SER ALA GLU ILE PRO ASN LEU TYR ARG ALA VAL
SEQRES 25 C 1023 VAL GLU LEU HIS THR ALA ASP GLY THR LEU ILE GLU ALA
SEQRES 26 C 1023 GLU ALA CYS ASP VAL GLY PHE ARG GLU VAL ARG ILE GLU
SEQRES 27 C 1023 ASN GLY LEU LEU LEU LEU ASN GLY LYS PRO LEU LEU ILE
SEQRES 28 C 1023 ARG GLY VAL ASN ARG HIS GLU HIS HIS PRO LEU HIS GLY
SEQRES 29 C 1023 GLN VAL MET ASP GLU GLN THR MET VAL GLN ASP ILE LEU
SEQRES 30 C 1023 LEU MET LYS GLN ASN ASN PHE ASN ALA VAL ARG CYS SER
SEQRES 31 C 1023 HIS TYR PRO ASN HIS PRO LEU TRP TYR THR LEU CYS ASP
SEQRES 32 C 1023 ARG TYR GLY LEU TYR VAL VAL ASP GLU ALA ASN ILE GLN
SEQRES 33 C 1023 THR HIS GLY MET VAL PRO MET ASN ARG LEU THR ASP ASP
SEQRES 34 C 1023 PRO ARG TRP LEU PRO ALA MET SER GLU ARG VAL THR ARG
SEQRES 35 C 1023 MET VAL GLN ARG ASP ARG ASN HIS PRO SER VAL ILE ILE
SEQRES 36 C 1023 TRP SER LEU GLY ASN GLU SER GLY HIS GLY ALA ASN HIS
SEQRES 37 C 1023 ASP ALA LEU TYR ARG TRP ILE LYS SER VAL ASP PRO SER
SEQRES 38 C 1023 ARG PRO VAL GLN TYR GLU GLY GLY GLY ALA ASP THR THR
SEQRES 39 C 1023 ALA THR ASP ILE ILE CYS PRO MET TYR ALA ARG VAL ASP
SEQRES 40 C 1023 GLU ASP GLN PRO PHE PRO ALA VAL PRO LYS TRP SER ILE
SEQRES 41 C 1023 LYS LYS TRP LEU SER LEU PRO GLY GLU THR ARG PRO LEU
SEQRES 42 C 1023 ILE LEU CYS GLU TYR ALA HIS ALA MET GLY ASN SER LEU
SEQRES 43 C 1023 GLY GLY PHE ALA LYS TYR TRP GLN ALA PHE ARG GLN TYR
SEQRES 44 C 1023 PRO ARG LEU GLN GLY GLY PHE VAL TRP ASP TRP VAL ASP
SEQRES 45 C 1023 GLN SER LEU ILE LYS TYR ASP GLU ASN GLY ASN PRO TRP
SEQRES 46 C 1023 SER ALA TYR GLY GLY ASP PHE GLY ASP THR PRO ASN ASP
SEQRES 47 C 1023 ARG GLN PHE CYS MET ASN GLY LEU VAL PHE ALA ASP ARG
SEQRES 48 C 1023 THR PRO HIS PRO ALA LEU THR GLU ALA LYS HIS GLN GLN
SEQRES 49 C 1023 GLN PHE PHE GLN PHE ARG LEU SER GLY GLN THR ILE GLU
SEQRES 50 C 1023 VAL THR SER GLU TYR LEU PHE ARG HIS SER ASP ASN GLU
SEQRES 51 C 1023 LEU LEU HIS TRP MET VAL ALA LEU ASP GLY LYS PRO LEU
SEQRES 52 C 1023 ALA SER GLY GLU VAL PRO LEU ASP VAL ALA PRO GLN GLY
SEQRES 53 C 1023 LYS GLN LEU ILE GLU LEU PRO GLU LEU PRO GLN PRO GLU
SEQRES 54 C 1023 SER ALA GLY GLN LEU TRP LEU THR VAL ARG VAL VAL GLN
SEQRES 55 C 1023 PRO ASN ALA THR ALA TRP SER GLU ALA GLY HIS ILE SER
SEQRES 56 C 1023 ALA TRP GLN GLN TRP ARG LEU ALA GLU ASN LEU SER VAL
SEQRES 57 C 1023 THR LEU PRO ALA ALA SER HIS ALA ILE PRO HIS LEU THR
SEQRES 58 C 1023 THR SER GLU MET ASP PHE CYS ILE GLU LEU GLY ASN LYS
SEQRES 59 C 1023 ARG TRP GLN PHE ASN ARG GLN SER GLY PHE LEU SER GLN
SEQRES 60 C 1023 MET TRP ILE GLY ASP LYS LYS GLN LEU LEU THR PRO LEU
SEQRES 61 C 1023 ARG ASP GLN PHE THR ARG ALA PRO LEU ASP ASN ASP ILE
SEQRES 62 C 1023 GLY VAL SER GLU ALA THR ARG ILE ASP PRO ASN ALA TRP
SEQRES 63 C 1023 VAL GLU ARG TRP LYS ALA ALA GLY HIS TYR GLN ALA GLU
SEQRES 64 C 1023 ALA ALA LEU LEU GLN CYS THR ALA ASP THR LEU ALA ASP
SEQRES 65 C 1023 ALA VAL LEU ILE THR THR ALA HIS ALA TRP GLN HIS GLN
SEQRES 66 C 1023 GLY LYS THR LEU PHE ILE SER ARG LYS THR TYR ARG ILE
SEQRES 67 C 1023 ASP GLY SER GLY GLN MET ALA ILE THR VAL ASP VAL GLU
SEQRES 68 C 1023 VAL ALA SER ASP THR PRO HIS PRO ALA ARG ILE GLY LEU
SEQRES 69 C 1023 ASN CYS GLN LEU ALA GLN VAL ALA GLU ARG VAL ASN TRP
SEQRES 70 C 1023 LEU GLY LEU GLY PRO GLN GLU ASN TYR PRO ASP ARG LEU
SEQRES 71 C 1023 THR ALA ALA CYS PHE ASP ARG TRP ASP LEU PRO LEU SER
SEQRES 72 C 1023 ASP MET TYR THR PRO TYR VAL PHE PRO SER GLU ASN GLY
SEQRES 73 C 1023 LEU ARG CYS GLY THR ARG GLU LEU ASN TYR GLY PRO HIS
SEQRES 74 C 1023 GLN TRP ARG GLY ASP PHE GLN PHE ASN ILE SER ARG TYR
SEQRES 75 C 1023 SER GLN GLN GLN LEU MET GLU THR SER HIS ARG HIS LEU
SEQRES 76 C 1023 LEU HIS ALA GLU GLU GLY THR TRP LEU ASN ILE ASP GLY
SEQRES 77 C 1023 PHE HIS MET GLY ILE GLY GLY ASP ASP SER TRP SER PRO
SEQRES 78 C 1023 SER VAL SER ALA GLU PHE GLN LEU SER ALA GLY ARG TYR
SEQRES 79 C 1023 HIS TYR GLN LEU VAL TRP CYS GLN LYS
SEQRES 1 D 1023 GLY SER HIS MET LEU GLU ASP PRO VAL VAL LEU GLN ARG
SEQRES 2 D 1023 ARG ASP TRP GLU ASN PRO GLY VAL THR GLN LEU ASN ARG
SEQRES 3 D 1023 LEU ALA ALA HIS PRO PRO PHE ALA SER TRP ARG ASN SER
SEQRES 4 D 1023 GLU GLU ALA ARG THR ASP ARG PRO SER GLN GLN LEU ARG
SEQRES 5 D 1023 SER LEU ASN GLY GLU TRP ARG PHE ALA TRP PHE PRO ALA
SEQRES 6 D 1023 PRO GLU ALA VAL PRO GLU SER TRP LEU GLU CYS ASP LEU
SEQRES 7 D 1023 PRO GLU ALA ASP THR VAL VAL VAL PRO SER ASN TRP GLN
SEQRES 8 D 1023 MET HIS GLY TYR ASP ALA PRO ILE TYR THR ASN VAL THR
SEQRES 9 D 1023 TYR PRO ILE THR VAL ASN PRO PRO PHE VAL PRO THR GLU
SEQRES 10 D 1023 ASN PRO THR GLY CYS TYR SER LEU THR PHE ASN VAL ASP
SEQRES 11 D 1023 GLU SER TRP LEU GLN GLU GLY GLN THR ARG ILE ILE PHE
SEQRES 12 D 1023 ASP GLY VAL ASN SER ALA PHE HIS LEU TRP CYS ASN GLY
SEQRES 13 D 1023 ARG TRP VAL GLY TYR GLY GLN ASP SER ARG LEU PRO SER
SEQRES 14 D 1023 GLU PHE ASP LEU SER ALA PHE LEU ARG ALA GLY GLU ASN
SEQRES 15 D 1023 ARG LEU ALA VAL MET VAL LEU ARG TRP SER ASP GLY SER
SEQRES 16 D 1023 TYR LEU GLU ASP GLN ASP MET TRP ARG MET SER GLY ILE
SEQRES 17 D 1023 PHE ARG ASP VAL SER LEU LEU HIS LYS PRO THR THR GLN
SEQRES 18 D 1023 ILE SER ASP PHE HIS VAL ALA THR ARG PHE ASN ASP ASP
SEQRES 19 D 1023 PHE SER ARG ALA VAL LEU GLU ALA GLU VAL GLN MET CYS
SEQRES 20 D 1023 GLY GLU LEU ARG ASP TYR LEU ARG VAL THR VAL SER LEU
SEQRES 21 D 1023 TRP GLN GLY GLU THR GLN VAL ALA SER GLY THR ALA PRO
SEQRES 22 D 1023 PHE GLY GLY GLU ILE ILE ASP GLU ARG GLY GLY TYR ALA
SEQRES 23 D 1023 ASP ARG VAL THR LEU ARG LEU ASN VAL GLU ASN PRO LYS
SEQRES 24 D 1023 LEU TRP SER ALA GLU ILE PRO ASN LEU TYR ARG ALA VAL
SEQRES 25 D 1023 VAL GLU LEU HIS THR ALA ASP GLY THR LEU ILE GLU ALA
SEQRES 26 D 1023 GLU ALA CYS ASP VAL GLY PHE ARG GLU VAL ARG ILE GLU
SEQRES 27 D 1023 ASN GLY LEU LEU LEU LEU ASN GLY LYS PRO LEU LEU ILE
SEQRES 28 D 1023 ARG GLY VAL ASN ARG HIS GLU HIS HIS PRO LEU HIS GLY
SEQRES 29 D 1023 GLN VAL MET ASP GLU GLN THR MET VAL GLN ASP ILE LEU
SEQRES 30 D 1023 LEU MET LYS GLN ASN ASN PHE ASN ALA VAL ARG CYS SER
SEQRES 31 D 1023 HIS TYR PRO ASN HIS PRO LEU TRP TYR THR LEU CYS ASP
SEQRES 32 D 1023 ARG TYR GLY LEU TYR VAL VAL ASP GLU ALA ASN ILE GLN
SEQRES 33 D 1023 THR HIS GLY MET VAL PRO MET ASN ARG LEU THR ASP ASP
SEQRES 34 D 1023 PRO ARG TRP LEU PRO ALA MET SER GLU ARG VAL THR ARG
SEQRES 35 D 1023 MET VAL GLN ARG ASP ARG ASN HIS PRO SER VAL ILE ILE
SEQRES 36 D 1023 TRP SER LEU GLY ASN GLU SER GLY HIS GLY ALA ASN HIS
SEQRES 37 D 1023 ASP ALA LEU TYR ARG TRP ILE LYS SER VAL ASP PRO SER
SEQRES 38 D 1023 ARG PRO VAL GLN TYR GLU GLY GLY GLY ALA ASP THR THR
SEQRES 39 D 1023 ALA THR ASP ILE ILE CYS PRO MET TYR ALA ARG VAL ASP
SEQRES 40 D 1023 GLU ASP GLN PRO PHE PRO ALA VAL PRO LYS TRP SER ILE
SEQRES 41 D 1023 LYS LYS TRP LEU SER LEU PRO GLY GLU THR ARG PRO LEU
SEQRES 42 D 1023 ILE LEU CYS GLU TYR ALA HIS ALA MET GLY ASN SER LEU
SEQRES 43 D 1023 GLY GLY PHE ALA LYS TYR TRP GLN ALA PHE ARG GLN TYR
SEQRES 44 D 1023 PRO ARG LEU GLN GLY GLY PHE VAL TRP ASP TRP VAL ASP
SEQRES 45 D 1023 GLN SER LEU ILE LYS TYR ASP GLU ASN GLY ASN PRO TRP
SEQRES 46 D 1023 SER ALA TYR GLY GLY ASP PHE GLY ASP THR PRO ASN ASP
SEQRES 47 D 1023 ARG GLN PHE CYS MET ASN GLY LEU VAL PHE ALA ASP ARG
SEQRES 48 D 1023 THR PRO HIS PRO ALA LEU THR GLU ALA LYS HIS GLN GLN
SEQRES 49 D 1023 GLN PHE PHE GLN PHE ARG LEU SER GLY GLN THR ILE GLU
SEQRES 50 D 1023 VAL THR SER GLU TYR LEU PHE ARG HIS SER ASP ASN GLU
SEQRES 51 D 1023 LEU LEU HIS TRP MET VAL ALA LEU ASP GLY LYS PRO LEU
SEQRES 52 D 1023 ALA SER GLY GLU VAL PRO LEU ASP VAL ALA PRO GLN GLY
SEQRES 53 D 1023 LYS GLN LEU ILE GLU LEU PRO GLU LEU PRO GLN PRO GLU
SEQRES 54 D 1023 SER ALA GLY GLN LEU TRP LEU THR VAL ARG VAL VAL GLN
SEQRES 55 D 1023 PRO ASN ALA THR ALA TRP SER GLU ALA GLY HIS ILE SER
SEQRES 56 D 1023 ALA TRP GLN GLN TRP ARG LEU ALA GLU ASN LEU SER VAL
SEQRES 57 D 1023 THR LEU PRO ALA ALA SER HIS ALA ILE PRO HIS LEU THR
SEQRES 58 D 1023 THR SER GLU MET ASP PHE CYS ILE GLU LEU GLY ASN LYS
SEQRES 59 D 1023 ARG TRP GLN PHE ASN ARG GLN SER GLY PHE LEU SER GLN
SEQRES 60 D 1023 MET TRP ILE GLY ASP LYS LYS GLN LEU LEU THR PRO LEU
SEQRES 61 D 1023 ARG ASP GLN PHE THR ARG ALA PRO LEU ASP ASN ASP ILE
SEQRES 62 D 1023 GLY VAL SER GLU ALA THR ARG ILE ASP PRO ASN ALA TRP
SEQRES 63 D 1023 VAL GLU ARG TRP LYS ALA ALA GLY HIS TYR GLN ALA GLU
SEQRES 64 D 1023 ALA ALA LEU LEU GLN CYS THR ALA ASP THR LEU ALA ASP
SEQRES 65 D 1023 ALA VAL LEU ILE THR THR ALA HIS ALA TRP GLN HIS GLN
SEQRES 66 D 1023 GLY LYS THR LEU PHE ILE SER ARG LYS THR TYR ARG ILE
SEQRES 67 D 1023 ASP GLY SER GLY GLN MET ALA ILE THR VAL ASP VAL GLU
SEQRES 68 D 1023 VAL ALA SER ASP THR PRO HIS PRO ALA ARG ILE GLY LEU
SEQRES 69 D 1023 ASN CYS GLN LEU ALA GLN VAL ALA GLU ARG VAL ASN TRP
SEQRES 70 D 1023 LEU GLY LEU GLY PRO GLN GLU ASN TYR PRO ASP ARG LEU
SEQRES 71 D 1023 THR ALA ALA CYS PHE ASP ARG TRP ASP LEU PRO LEU SER
SEQRES 72 D 1023 ASP MET TYR THR PRO TYR VAL PHE PRO SER GLU ASN GLY
SEQRES 73 D 1023 LEU ARG CYS GLY THR ARG GLU LEU ASN TYR GLY PRO HIS
SEQRES 74 D 1023 GLN TRP ARG GLY ASP PHE GLN PHE ASN ILE SER ARG TYR
SEQRES 75 D 1023 SER GLN GLN GLN LEU MET GLU THR SER HIS ARG HIS LEU
SEQRES 76 D 1023 LEU HIS ALA GLU GLU GLY THR TRP LEU ASN ILE ASP GLY
SEQRES 77 D 1023 PHE HIS MET GLY ILE GLY GLY ASP ASP SER TRP SER PRO
SEQRES 78 D 1023 SER VAL SER ALA GLU PHE GLN LEU SER ALA GLY ARG TYR
SEQRES 79 D 1023 HIS TYR GLN LEU VAL TRP CYS GLN LYS
HET MG A3001 1
HET MG A3002 1
HET NA A3101 1
HET NA A3102 1
HET NA A3103 1
HET NA A3104 1
HET BTB A6001 14
HET DMS A7001 4
HET DMS A7002 4
HET DMS A7003 4
HET DMS A7004 4
HET DMS A7005 4
HET DMS A7006 4
HET DMS A7007 4
HET DMS A7008 4
HET DMS A7009 4
HET DMS A7010 4
HET DMS A7011 4
HET DMS A7012 4
HET DMS A7013 4
HET DMS A7014 4
HET DMS A7015 4
HET DMS A7016 4
HET DMS A7017 4
HET DMS A7018 4
HET DMS A7019 4
HET DMS A7020 4
HET DMS A7021 4
HET DMS A7022 4
HET DMS A7023 4
HET DMS A7024 4
HET DMS A7025 4
HET DMS A7026 4
HET DMS A7027 4
HET DMS A7028 4
HET DMS A7029 4
HET DMS A7030 4
HET DMS A7031 4
HET DMS A7032 4
HET MG B3001 1
HET MG B3002 1
HET NA B3101 1
HET NA B3102 1
HET NA B3103 1
HET NA B3104 1
HET BTB B6001 14
HET DMS B7001 4
HET DMS B7002 4
HET DMS B7003 4
HET DMS B7004 4
HET DMS B7005 4
HET DMS B7006 4
HET DMS B7007 4
HET DMS B7008 4
HET DMS B7009 4
HET DMS B7010 4
HET DMS B7011 4
HET DMS B7012 4
HET DMS B7013 4
HET DMS B7014 4
HET DMS B7015 4
HET DMS B7016 4
HET DMS B7017 4
HET DMS B7018 4
HET DMS B7019 4
HET DMS B7020 4
HET DMS B7021 4
HET DMS B7022 4
HET DMS B7023 4
HET DMS B7024 4
HET DMS B7025 4
HET DMS B7026 4
HET DMS B7027 4
HET DMS B7028 4
HET DMS B7029 4
HET DMS B7030 4
HET DMS B7031 4
HET DMS B7032 4
HET DMS B7033 4
HET DMS C7034 4
HET MG C3001 1
HET MG C3002 1
HET NA C3101 1
HET NA C3102 1
HET NA C3103 1
HET NA C3104 1
HET BTB C6001 14
HET DMS C7001 4
HET DMS C7002 4
HET DMS C7003 4
HET DMS C7004 4
HET DMS C7005 4
HET DMS C7006 4
HET DMS C7007 4
HET DMS C7008 4
HET DMS C7009 4
HET DMS C7010 4
HET DMS C7011 4
HET DMS C7012 4
HET DMS C7013 4
HET DMS C7014 4
HET DMS C7015 4
HET DMS C7016 4
HET DMS C7017 4
HET DMS C7018 4
HET DMS C7019 4
HET DMS C7020 4
HET DMS C7021 4
HET DMS C7022 4
HET DMS C7023 4
HET DMS C7024 4
HET DMS C7025 4
HET DMS C7026 4
HET DMS C7027 4
HET DMS C7028 4
HET DMS C7029 4
HET DMS C7030 4
HET DMS C7031 4
HET MG D3001 1
HET MG D3002 1
HET NA D3101 1
HET NA D3102 1
HET NA D3103 1
HET NA D3104 1
HET BTB D6001 14
HET DMS D7001 4
HET DMS D7002 4
HET DMS D7003 4
HET DMS D7004 4
HET DMS D7005 4
HET DMS D7006 4
HET DMS D7007 4
HET DMS D7009 4
HET DMS D7010 4
HET DMS D7011 4
HET DMS D7012 4
HET DMS D7013 4
HET DMS D7014 4
HET DMS D7015 4
HET DMS D7016 4
HET DMS D7017 4
HET DMS D7018 4
HET DMS D7019 4
HET DMS D7020 4
HET DMS D7021 4
HET DMS D7022 4
HET DMS D7023 4
HET DMS D7024 4
HET DMS D7025 4
HET DMS D7026 4
HET DMS D7027 4
HET DMS D7028 4
HET DMS D7029 4
HETNAM MG MAGNESIUM ION
HETNAM NA SODIUM ION
HETNAM BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-
HETNAM 2 BTB PROPANE-1,3-DIOL
HETNAM DMS DIMETHYL SULFOXIDE
HETSYN BTB BIS-TRIS BUFFER
FORMUL 5 MG 8(MG 2+)
FORMUL 7 NA 16(NA 1+)
FORMUL 11 BTB 4(C8 H19 N O5)
FORMUL 12 DMS 125(C2 H6 O S)
FORMUL 58 HOH *3832(H2 O)
HELIX 1 1 ARG A 14 ASN A 18 5 5
HELIX 2 2 ASN A 38 ASP A 45 1 8
HELIX 3 3 ALA A 65 VAL A 69 5 5
HELIX 4 4 PRO A 70 GLU A 75 5 6
HELIX 5 5 ASN A 89 GLY A 94 5 6
HELIX 6 6 GLU A 131 GLU A 136 1 6
HELIX 7 7 SER A 192 GLU A 198 5 7
HELIX 8 8 ASP A 368 ASN A 382 1 15
HELIX 9 9 HIS A 395 GLY A 406 1 12
HELIX 10 10 ASP A 429 ARG A 431 5 3
HELIX 11 11 TRP A 432 ARG A 448 1 17
HELIX 12 12 GLY A 465 ASP A 479 1 15
HELIX 13 13 SER A 519 SER A 525 1 7
HELIX 14 14 GLY A 548 TYR A 559 1 12
HELIX 15 15 PRO A 615 GLN A 624 1 10
HELIX 16 16 LEU A 789 GLY A 794 1 6
HELIX 17 17 ALA A 805 ALA A 813 1 9
HELIX 18 18 SER A 923 TYR A 926 5 4
HELIX 19 19 SER A 963 THR A 970 1 8
HELIX 20 20 HIS A 972 LEU A 976 5 5
HELIX 21 21 SER A 1004 GLN A 1008 5 5
HELIX 22 22 ARG B 14 ASN B 18 5 5
HELIX 23 23 ASN B 38 ASP B 45 1 8
HELIX 24 24 ALA B 65 VAL B 69 5 5
HELIX 25 25 PRO B 70 GLU B 75 5 6
HELIX 26 26 ASP B 130 GLU B 136 1 7
HELIX 27 27 SER B 192 GLU B 198 5 7
HELIX 28 28 ASP B 368 ASN B 382 1 15
HELIX 29 29 HIS B 395 GLY B 406 1 12
HELIX 30 30 ASP B 429 ARG B 431 5 3
HELIX 31 31 TRP B 432 ARG B 448 1 17
HELIX 32 32 GLY B 465 ASP B 479 1 15
HELIX 33 33 SER B 519 SER B 525 1 7
HELIX 34 34 GLY B 548 TYR B 559 1 12
HELIX 35 35 PRO B 615 GLN B 624 1 10
HELIX 36 36 LEU B 789 GLY B 794 1 6
HELIX 37 37 ALA B 805 ALA B 813 1 9
HELIX 38 38 SER B 923 TYR B 926 5 4
HELIX 39 39 SER B 963 THR B 970 1 8
HELIX 40 40 HIS B 972 LEU B 976 5 5
HELIX 41 41 SER B 1004 GLN B 1008 5 5
HELIX 42 42 ARG C 14 ASN C 18 5 5
HELIX 43 43 ASN C 38 THR C 44 1 7
HELIX 44 44 ALA C 65 VAL C 69 5 5
HELIX 45 45 PRO C 70 GLU C 75 5 6
HELIX 46 46 ASN C 89 GLY C 94 5 6
HELIX 47 47 ASP C 130 GLU C 136 1 7
HELIX 48 48 SER C 192 GLU C 198 5 7
HELIX 49 49 ASP C 368 ASN C 382 1 15
HELIX 50 50 HIS C 395 GLY C 406 1 12
HELIX 51 51 ASP C 429 ARG C 431 5 3
HELIX 52 52 TRP C 432 ARG C 448 1 17
HELIX 53 53 GLY C 465 ASP C 479 1 15
HELIX 54 54 SER C 519 SER C 525 1 7
HELIX 55 55 GLY C 548 TYR C 559 1 12
HELIX 56 56 ASP C 598 MET C 603 5 6
HELIX 57 57 PRO C 615 GLN C 624 1 10
HELIX 58 58 LEU C 789 GLY C 794 1 6
HELIX 59 59 ALA C 805 GLY C 814 1 10
HELIX 60 60 SER C 923 TYR C 926 5 4
HELIX 61 61 SER C 963 THR C 970 1 8
HELIX 62 62 HIS C 972 LEU C 976 5 5
HELIX 63 63 SER C 1004 GLN C 1008 5 5
HELIX 64 64 ARG D 14 ASN D 18 5 5
HELIX 65 65 ASN D 38 ASP D 45 1 8
HELIX 66 66 ALA D 65 VAL D 69 5 5
HELIX 67 67 PRO D 70 GLU D 75 5 6
HELIX 68 68 ASN D 89 GLY D 94 5 6
HELIX 69 69 ASP D 130 GLN D 135 5 6
HELIX 70 70 SER D 192 GLU D 198 5 7
HELIX 71 71 ASP D 368 ASN D 382 1 15
HELIX 72 72 HIS D 395 GLY D 406 1 12
HELIX 73 73 ASP D 429 ARG D 431 5 3
HELIX 74 74 TRP D 432 ARG D 448 1 17
HELIX 75 75 GLY D 465 ASP D 479 1 15
HELIX 76 76 SER D 519 SER D 525 1 7
HELIX 77 77 GLY D 548 TYR D 559 1 12
HELIX 78 78 PRO D 615 GLN D 624 1 10
HELIX 79 79 LEU D 789 GLY D 794 1 6
HELIX 80 80 ALA D 805 GLY D 814 1 10
HELIX 81 81 SER D 923 TYR D 926 5 4
HELIX 82 82 SER D 963 THR D 970 1 8
HELIX 83 83 HIS D 972 LEU D 976 5 5
HELIX 84 84 SER D 1004 GLN D 1008 5 5
SHEET 1 A 7 GLN A 23 LEU A 24 0
SHEET 2 A 7 ARG A 157 GLN A 163 -1 O TYR A 161 N LEU A 24
SHEET 3 A 7 ALA A 149 CYS A 154 -1 N LEU A 152 O VAL A 159
SHEET 4 A 7 GLY A 180 LEU A 189 -1 O ALA A 185 N TRP A 153
SHEET 5 A 7 THR A 120 VAL A 129 -1 N TYR A 123 O VAL A 186
SHEET 6 A 7 GLY A 56 PHE A 63 -1 N PHE A 63 O THR A 120
SHEET 7 A 7 ASP A 82 VAL A 86 -1 O VAL A 84 N TRP A 58
SHEET 1 B 4 LEU A 51 SER A 53 0
SHEET 2 B 4 VAL A 212 LYS A 217 -1 O LEU A 214 N ARG A 52
SHEET 3 B 4 GLN A 138 PHE A 143 -1 N GLN A 138 O LYS A 217
SHEET 4 B 4 SER A 169 ASP A 172 -1 O SER A 169 N PHE A 143
SHEET 1 C 2 ILE A 99 TYR A 100 0
SHEET 2 C 2 TRP A 203 ARG A 204 -1 O ARG A 204 N ILE A 99
SHEET 1 D 2 VAL A 146 ASN A 147 0
SHEET 2 D 2 GLY A 207 ILE A 208 -1 O GLY A 207 N ASN A 147
SHEET 1 E 3 GLN A 221 PHE A 231 0
SHEET 2 E 3 ARG A 237 CYS A 247 -1 O GLN A 245 N ASP A 224
SHEET 3 E 3 ARG A 288 GLU A 296 -1 O VAL A 289 N VAL A 244
SHEET 1 F 4 THR A 265 PRO A 273 0
SHEET 2 F 4 LEU A 254 GLN A 262 -1 N LEU A 260 O ALA A 268
SHEET 3 F 4 TYR A 309 THR A 317 -1 O GLU A 314 N THR A 257
SHEET 4 F 4 LEU A 322 VAL A 330 -1 O GLU A 326 N VAL A 313
SHEET 1 G 3 VAL A 335 GLU A 338 0
SHEET 2 G 3 LEU A 341 LEU A 344 -1 O LEU A 343 N ARG A 336
SHEET 3 G 3 LYS A 347 PRO A 348 -1 O LYS A 347 N LEU A 344
SHEET 1 H 7 VAL A 484 GLN A 485 0
SHEET 2 H 7 VAL A 453 SER A 457 1 N TRP A 456 O GLN A 485
SHEET 3 H 7 TYR A 408 GLU A 412 1 N ASP A 411 O SER A 457
SHEET 4 H 7 ALA A 386 ARG A 388 1 N VAL A 387 O TYR A 408
SHEET 5 H 7 ILE A 351 ASN A 355 1 N VAL A 354 O ARG A 388
SHEET 6 H 7 LEU A 562 VAL A 567 1 O VAL A 567 N ASN A 355
SHEET 7 H 7 LEU A 533 TYR A 538 1 N LEU A 533 O GLN A 563
SHEET 1 I 2 LEU A 575 TYR A 578 0
SHEET 2 I 2 PRO A 584 ALA A 587 -1 O ALA A 587 N LEU A 575
SHEET 1 J 3 PHE A 627 SER A 632 0
SHEET 2 J 3 THR A 635 SER A 640 -1 O GLU A 637 N ARG A 630
SHEET 3 J 3 LYS A 677 GLU A 681 -1 O ILE A 680 N ILE A 636
SHEET 1 K 4 LYS A 661 PRO A 669 0
SHEET 2 K 4 LEU A 651 LEU A 658 -1 N VAL A 656 O ALA A 664
SHEET 3 K 4 GLY A 692 GLN A 702 -1 O VAL A 701 N LEU A 651
SHEET 4 K 4 HIS A 713 ASN A 725 -1 O LEU A 722 N LEU A 694
SHEET 1 L 5 HIS A 739 THR A 742 0
SHEET 2 L 5 ASP A 746 LEU A 751 -1 O CYS A 748 N THR A 741
SHEET 3 L 5 LYS A 754 ASN A 759 -1 O PHE A 758 N PHE A 747
SHEET 4 L 5 LEU A 765 ILE A 770 -1 O TRP A 769 N ARG A 755
SHEET 5 L 5 LYS A 773 LYS A 774 -1 O LYS A 773 N ILE A 770
SHEET 1 M 9 LEU A 776 GLN A 783 0
SHEET 2 M 9 ARG A 881 LEU A 888 -1 O GLN A 887 N LEU A 777
SHEET 3 M 9 THR A 982 HIS A 990 -1 O ILE A 986 N LEU A 884
SHEET 4 M 9 HIS A 949 SER A 960 -1 N GLN A 956 O ASP A 987
SHEET 5 M 9 ARG A1013 GLN A1022 -1 O VAL A1019 N ARG A 952
SHEET 6 M 9 MET A 864 VAL A 872 -1 N ILE A 866 O LEU A1018
SHEET 7 M 9 LYS A 847 ASP A 859 -1 N ARG A 853 O ASP A 869
SHEET 8 M 9 ALA A 833 HIS A 844 -1 N TRP A 842 O LEU A 849
SHEET 9 M 9 GLU A 819 THR A 829 -1 N LEU A 823 O ALA A 839
SHEET 1 N 7 LEU A 776 GLN A 783 0
SHEET 2 N 7 ARG A 881 LEU A 888 -1 O GLN A 887 N LEU A 777
SHEET 3 N 7 THR A 982 HIS A 990 -1 O ILE A 986 N LEU A 884
SHEET 4 N 7 HIS A 949 SER A 960 -1 N GLN A 956 O ASP A 987
SHEET 5 N 7 ARG A 938 TYR A 946 -1 N LEU A 944 O TRP A 951
SHEET 6 N 7 ARG A 894 GLY A 901 -1 N ASN A 896 O ASN A 945
SHEET 7 N 7 CYS A 914 PRO A 921 -1 O LEU A 920 N VAL A 895
SHEET 1 O 7 GLN B 23 LEU B 24 0
SHEET 2 O 7 ARG B 157 GLN B 163 -1 O TYR B 161 N LEU B 24
SHEET 3 O 7 ALA B 149 CYS B 154 -1 N LEU B 152 O VAL B 159
SHEET 4 O 7 GLY B 180 LEU B 189 -1 O LEU B 189 N ALA B 149
SHEET 5 O 7 THR B 120 VAL B 129 -1 N TYR B 123 O VAL B 186
SHEET 6 O 7 GLY B 56 PHE B 63 -1 N PHE B 63 O THR B 120
SHEET 7 O 7 ASP B 82 VAL B 86 -1 O VAL B 84 N TRP B 58
SHEET 1 P 4 LEU B 51 SER B 53 0
SHEET 2 P 4 VAL B 212 LYS B 217 -1 O LEU B 214 N ARG B 52
SHEET 3 P 4 GLN B 138 PHE B 143 -1 N GLN B 138 O LYS B 217
SHEET 4 P 4 SER B 169 ASP B 172 -1 O SER B 169 N PHE B 143
SHEET 1 Q 2 ILE B 99 TYR B 100 0
SHEET 2 Q 2 TRP B 203 ARG B 204 -1 O ARG B 204 N ILE B 99
SHEET 1 R 2 VAL B 146 ASN B 147 0
SHEET 2 R 2 GLY B 207 ILE B 208 -1 O GLY B 207 N ASN B 147
SHEET 1 S 3 GLN B 221 PHE B 231 0
SHEET 2 S 3 ARG B 237 CYS B 247 -1 O GLN B 245 N ASP B 224
SHEET 3 S 3 ARG B 288 GLU B 296 -1 O VAL B 289 N VAL B 244
SHEET 1 T 4 THR B 265 ALA B 272 0
SHEET 2 T 4 LEU B 254 GLN B 262 -1 N GLN B 262 O THR B 265
SHEET 3 T 4 TYR B 309 THR B 317 -1 O GLU B 314 N THR B 257
SHEET 4 T 4 LEU B 322 VAL B 330 -1 O ILE B 323 N LEU B 315
SHEET 1 U 2 ILE B 278 ASP B 280 0
SHEET 2 U 2 GLY B 283 GLY B 284 -1 O GLY B 283 N ILE B 279
SHEET 1 V 3 VAL B 335 GLU B 338 0
SHEET 2 V 3 LEU B 341 LEU B 344 -1 O LEU B 343 N ARG B 336
SHEET 3 V 3 LYS B 347 PRO B 348 -1 O LYS B 347 N LEU B 344
SHEET 1 W 7 VAL B 484 GLN B 485 0
SHEET 2 W 7 VAL B 453 SER B 457 1 N TRP B 456 O GLN B 485
SHEET 3 W 7 TYR B 408 GLU B 412 1 N ASP B 411 O SER B 457
SHEET 4 W 7 ALA B 386 ARG B 388 1 N VAL B 387 O TYR B 408
SHEET 5 W 7 ILE B 351 ASN B 355 1 N VAL B 354 O ARG B 388
SHEET 6 W 7 LEU B 562 VAL B 567 1 O GLN B 563 N ILE B 351
SHEET 7 W 7 LEU B 533 TYR B 538 1 N LEU B 535 O PHE B 566
SHEET 1 X 2 LEU B 575 TYR B 578 0
SHEET 2 X 2 PRO B 584 ALA B 587 -1 O ALA B 587 N LEU B 575
SHEET 1 Y 3 PHE B 627 SER B 632 0
SHEET 2 Y 3 THR B 635 SER B 640 -1 O THR B 639 N GLN B 628
SHEET 3 Y 3 LYS B 677 GLU B 681 -1 O ILE B 680 N ILE B 636
SHEET 1 Z 4 LYS B 661 PRO B 669 0
SHEET 2 Z 4 LEU B 651 LEU B 658 -1 N LEU B 652 O VAL B 668
SHEET 3 Z 4 GLY B 692 GLN B 702 -1 O VAL B 701 N LEU B 651
SHEET 4 Z 4 HIS B 713 ASN B 725 -1 O LEU B 722 N LEU B 694
SHEET 1 AA 5 HIS B 739 THR B 742 0
SHEET 2 AA 5 ASP B 746 LEU B 751 -1 O CYS B 748 N THR B 741
SHEET 3 AA 5 LYS B 754 ASN B 759 -1 O PHE B 758 N PHE B 747
SHEET 4 AA 5 LEU B 765 ILE B 770 -1 O GLN B 767 N GLN B 757
SHEET 5 AA 5 LYS B 773 LYS B 774 -1 O LYS B 773 N ILE B 770
SHEET 1 AB 9 LEU B 776 GLN B 783 0
SHEET 2 AB 9 ARG B 881 LEU B 888 -1 O GLN B 887 N LEU B 777
SHEET 3 AB 9 THR B 982 HIS B 990 -1 O THR B 982 N LEU B 888
SHEET 4 AB 9 HIS B 949 SER B 960 -1 N GLN B 956 O ASP B 987
SHEET 5 AB 9 ARG B1013 GLN B1022 -1 O CYS B1021 N GLN B 950
SHEET 6 AB 9 MET B 864 VAL B 872 -1 N ILE B 866 O LEU B1018
SHEET 7 AB 9 LYS B 847 ASP B 859 -1 N ARG B 857 O ALA B 865
SHEET 8 AB 9 ALA B 833 HIS B 844 -1 N TRP B 842 O LEU B 849
SHEET 9 AB 9 GLU B 819 THR B 829 -1 N LEU B 823 O ALA B 839
SHEET 1 AC 7 LEU B 776 GLN B 783 0
SHEET 2 AC 7 ARG B 881 LEU B 888 -1 O GLN B 887 N LEU B 777
SHEET 3 AC 7 THR B 982 HIS B 990 -1 O THR B 982 N LEU B 888
SHEET 4 AC 7 HIS B 949 SER B 960 -1 N GLN B 956 O ASP B 987
SHEET 5 AC 7 ARG B 938 TYR B 946 -1 N LEU B 944 O TRP B 951
SHEET 6 AC 7 ARG B 894 GLY B 901 -1 N ASN B 896 O ASN B 945
SHEET 7 AC 7 CYS B 914 PRO B 921 -1 O TRP B 918 N TRP B 897
SHEET 1 AD 7 GLN C 23 LEU C 24 0
SHEET 2 AD 7 ARG C 157 GLN C 163 -1 O TYR C 161 N LEU C 24
SHEET 3 AD 7 ALA C 149 CYS C 154 -1 N LEU C 152 O VAL C 159
SHEET 4 AD 7 GLY C 180 LEU C 189 -1 O LEU C 189 N ALA C 149
SHEET 5 AD 7 THR C 120 VAL C 129 -1 N TYR C 123 O VAL C 186
SHEET 6 AD 7 GLY C 56 PHE C 63 -1 N PHE C 63 O THR C 120
SHEET 7 AD 7 ASP C 82 VAL C 86 -1 O VAL C 84 N TRP C 58
SHEET 1 AE 4 LEU C 51 SER C 53 0
SHEET 2 AE 4 VAL C 212 LYS C 217 -1 O LEU C 214 N ARG C 52
SHEET 3 AE 4 GLN C 138 PHE C 143 -1 N GLN C 138 O LYS C 217
SHEET 4 AE 4 SER C 169 ASP C 172 -1 O SER C 169 N PHE C 143
SHEET 1 AF 2 ILE C 99 TYR C 100 0
SHEET 2 AF 2 TRP C 203 ARG C 204 -1 O ARG C 204 N ILE C 99
SHEET 1 AG 2 VAL C 146 ASN C 147 0
SHEET 2 AG 2 GLY C 207 ILE C 208 -1 O GLY C 207 N ASN C 147
SHEET 1 AH 3 GLN C 221 PHE C 231 0
SHEET 2 AH 3 ARG C 237 CYS C 247 -1 O GLN C 245 N ASP C 224
SHEET 3 AH 3 ARG C 288 GLU C 296 -1 O VAL C 289 N VAL C 244
SHEET 1 AI 4 THR C 265 ALA C 272 0
SHEET 2 AI 4 LEU C 254 GLN C 262 -1 N GLN C 262 O THR C 265
SHEET 3 AI 4 TYR C 309 THR C 317 -1 O GLU C 314 N THR C 257
SHEET 4 AI 4 LEU C 322 VAL C 330 -1 O GLU C 326 N VAL C 313
SHEET 1 AJ 2 ILE C 278 ASP C 280 0
SHEET 2 AJ 2 GLY C 283 GLY C 284 -1 O GLY C 283 N ILE C 279
SHEET 1 AK 3 VAL C 335 GLU C 338 0
SHEET 2 AK 3 LEU C 341 LEU C 344 -1 O LEU C 343 N ARG C 336
SHEET 3 AK 3 LYS C 347 PRO C 348 -1 O LYS C 347 N LEU C 344
SHEET 1 AL 7 VAL C 484 GLN C 485 0
SHEET 2 AL 7 VAL C 453 SER C 457 1 N TRP C 456 O GLN C 485
SHEET 3 AL 7 TYR C 408 GLU C 412 1 N ASP C 411 O SER C 457
SHEET 4 AL 7 ALA C 386 ARG C 388 1 N VAL C 387 O TYR C 408
SHEET 5 AL 7 ILE C 351 ASN C 355 1 N VAL C 354 O ARG C 388
SHEET 6 AL 7 LEU C 562 VAL C 567 1 O GLN C 563 N ILE C 351
SHEET 7 AL 7 LEU C 533 TYR C 538 1 N LEU C 533 O GLN C 563
SHEET 1 AM 2 LEU C 575 TYR C 578 0
SHEET 2 AM 2 PRO C 584 ALA C 587 -1 O ALA C 587 N LEU C 575
SHEET 1 AN 3 PHE C 627 SER C 632 0
SHEET 2 AN 3 THR C 635 SER C 640 -1 O GLU C 637 N ARG C 630
SHEET 3 AN 3 LYS C 677 GLU C 681 -1 O ILE C 680 N ILE C 636
SHEET 1 AO 4 LYS C 661 PRO C 669 0
SHEET 2 AO 4 LEU C 651 LEU C 658 -1 N VAL C 656 O ALA C 664
SHEET 3 AO 4 GLY C 692 GLN C 702 -1 O VAL C 701 N LEU C 651
SHEET 4 AO 4 HIS C 713 ASN C 725 -1 O LEU C 722 N LEU C 694
SHEET 1 AP 5 HIS C 739 THR C 742 0
SHEET 2 AP 5 ASP C 746 LEU C 751 -1 O CYS C 748 N THR C 741
SHEET 3 AP 5 LYS C 754 ASN C 759 -1 O PHE C 758 N PHE C 747
SHEET 4 AP 5 LEU C 765 ILE C 770 -1 O GLN C 767 N GLN C 757
SHEET 5 AP 5 LYS C 773 LYS C 774 -1 O LYS C 773 N ILE C 770
SHEET 1 AQ 9 LEU C 776 GLN C 783 0
SHEET 2 AQ 9 ARG C 881 LEU C 888 -1 O GLN C 887 N LEU C 777
SHEET 3 AQ 9 THR C 982 HIS C 990 -1 O THR C 982 N LEU C 888
SHEET 4 AQ 9 HIS C 949 SER C 960 -1 N GLN C 956 O ASP C 987
SHEET 5 AQ 9 ARG C1013 GLN C1022 -1 O CYS C1021 N GLN C 950
SHEET 6 AQ 9 MET C 864 VAL C 872 -1 N ILE C 866 O LEU C1018
SHEET 7 AQ 9 LYS C 847 ASP C 859 -1 N ARG C 857 O ALA C 865
SHEET 8 AQ 9 ALA C 833 HIS C 844 -1 N TRP C 842 O LEU C 849
SHEET 9 AQ 9 GLU C 819 THR C 829 -1 N LEU C 823 O ALA C 839
SHEET 1 AR 7 LEU C 776 GLN C 783 0
SHEET 2 AR 7 ARG C 881 LEU C 888 -1 O GLN C 887 N LEU C 777
SHEET 3 AR 7 THR C 982 HIS C 990 -1 O THR C 982 N LEU C 888
SHEET 4 AR 7 HIS C 949 SER C 960 -1 N GLN C 956 O ASP C 987
SHEET 5 AR 7 ARG C 938 TYR C 946 -1 N LEU C 944 O TRP C 951
SHEET 6 AR 7 ARG C 894 GLY C 901 -1 N LEU C 898 O ARG C 942
SHEET 7 AR 7 CYS C 914 PRO C 921 -1 O LEU C 920 N VAL C 895
SHEET 1 AS 7 GLN D 23 LEU D 24 0
SHEET 2 AS 7 ARG D 157 GLN D 163 -1 O TYR D 161 N LEU D 24
SHEET 3 AS 7 ALA D 149 CYS D 154 -1 N LEU D 152 O VAL D 159
SHEET 4 AS 7 GLU D 181 LEU D 189 -1 O LEU D 189 N ALA D 149
SHEET 5 AS 7 THR D 120 ASN D 128 -1 N TYR D 123 O VAL D 186
SHEET 6 AS 7 GLY D 56 PHE D 63 -1 N PHE D 63 O THR D 120
SHEET 7 AS 7 ASP D 82 VAL D 86 -1 O ASP D 82 N PHE D 60
SHEET 1 AT 4 LEU D 51 SER D 53 0
SHEET 2 AT 4 VAL D 212 LYS D 217 -1 O LEU D 214 N ARG D 52
SHEET 3 AT 4 GLN D 138 PHE D 143 -1 N GLN D 138 O LYS D 217
SHEET 4 AT 4 SER D 169 ASP D 172 -1 O PHE D 171 N ILE D 141
SHEET 1 AU 2 ILE D 99 TYR D 100 0
SHEET 2 AU 2 TRP D 203 ARG D 204 -1 O ARG D 204 N ILE D 99
SHEET 1 AV 2 VAL D 146 ASN D 147 0
SHEET 2 AV 2 GLY D 207 ILE D 208 -1 O GLY D 207 N ASN D 147
SHEET 1 AW 3 GLN D 221 PHE D 231 0
SHEET 2 AW 3 ARG D 237 CYS D 247 -1 O GLN D 245 N ASP D 224
SHEET 3 AW 3 ARG D 288 GLU D 296 -1 O LEU D 291 N ALA D 242
SHEET 1 AX 4 THR D 265 PRO D 273 0
SHEET 2 AX 4 LEU D 254 GLN D 262 -1 N GLN D 262 O THR D 265
SHEET 3 AX 4 TYR D 309 THR D 317 -1 O HIS D 316 N ARG D 255
SHEET 4 AX 4 LEU D 322 VAL D 330 -1 O GLU D 326 N VAL D 313
SHEET 1 AY 2 ILE D 278 ASP D 280 0
SHEET 2 AY 2 GLY D 283 GLY D 284 -1 O GLY D 283 N ILE D 279
SHEET 1 AZ 3 VAL D 335 GLU D 338 0
SHEET 2 AZ 3 LEU D 341 LEU D 344 -1 O LEU D 343 N ARG D 336
SHEET 3 AZ 3 LYS D 347 PRO D 348 -1 O LYS D 347 N LEU D 344
SHEET 1 BA 7 VAL D 484 GLN D 485 0
SHEET 2 BA 7 VAL D 453 SER D 457 1 N TRP D 456 O GLN D 485
SHEET 3 BA 7 TYR D 408 GLU D 412 1 N ASP D 411 O SER D 457
SHEET 4 BA 7 ALA D 386 ARG D 388 1 N VAL D 387 O TYR D 408
SHEET 5 BA 7 ILE D 351 ASN D 355 1 N VAL D 354 O ARG D 388
SHEET 6 BA 7 LEU D 562 VAL D 567 1 O VAL D 567 N ASN D 355
SHEET 7 BA 7 LEU D 533 TYR D 538 1 N LEU D 533 O GLN D 563
SHEET 1 BB 2 LEU D 575 TYR D 578 0
SHEET 2 BB 2 PRO D 584 ALA D 587 -1 O ALA D 587 N LEU D 575
SHEET 1 BC 3 PHE D 627 SER D 632 0
SHEET 2 BC 3 THR D 635 SER D 640 -1 O GLU D 637 N ARG D 630
SHEET 3 BC 3 LYS D 677 GLU D 681 -1 O ILE D 680 N ILE D 636
SHEET 1 BD 4 LYS D 661 PRO D 669 0
SHEET 2 BD 4 LEU D 651 LEU D 658 -1 N VAL D 656 O ALA D 664
SHEET 3 BD 4 GLY D 692 GLN D 702 -1 O ARG D 699 N HIS D 653
SHEET 4 BD 4 HIS D 713 ASN D 725 -1 O LEU D 722 N LEU D 694
SHEET 1 BE 5 HIS D 739 THR D 742 0
SHEET 2 BE 5 ASP D 746 LEU D 751 -1 O CYS D 748 N THR D 741
SHEET 3 BE 5 LYS D 754 ASN D 759 -1 O PHE D 758 N PHE D 747
SHEET 4 BE 5 LEU D 765 ILE D 770 -1 O GLN D 767 N GLN D 757
SHEET 5 BE 5 LYS D 773 LYS D 774 -1 O LYS D 773 N ILE D 770
SHEET 1 BF 9 LEU D 776 GLN D 783 0
SHEET 2 BF 9 ARG D 881 LEU D 888 -1 O GLN D 887 N LEU D 777
SHEET 3 BF 9 THR D 982 HIS D 990 -1 O THR D 982 N LEU D 888
SHEET 4 BF 9 HIS D 949 SER D 960 -1 N GLN D 956 O ASP D 987
SHEET 5 BF 9 ARG D1013 GLN D1022 -1 O CYS D1021 N GLN D 950
SHEET 6 BF 9 MET D 864 VAL D 872 -1 N ILE D 866 O LEU D1018
SHEET 7 BF 9 LYS D 847 ASP D 859 -1 N ARG D 853 O ASP D 869
SHEET 8 BF 9 ALA D 833 HIS D 844 -1 N TRP D 842 O LEU D 849
SHEET 9 BF 9 GLU D 819 THR D 829 -1 N LEU D 823 O ALA D 839
SHEET 1 BG 7 LEU D 776 GLN D 783 0
SHEET 2 BG 7 ARG D 881 LEU D 888 -1 O GLN D 887 N LEU D 777
SHEET 3 BG 7 THR D 982 HIS D 990 -1 O THR D 982 N LEU D 888
SHEET 4 BG 7 HIS D 949 SER D 960 -1 N GLN D 956 O ASP D 987
SHEET 5 BG 7 ARG D 938 TYR D 946 -1 N LEU D 944 O TRP D 951
SHEET 6 BG 7 ARG D 894 GLY D 901 -1 N ASN D 896 O ASN D 945
SHEET 7 BG 7 CYS D 914 PRO D 921 -1 O TRP D 918 N TRP D 897
LINK O ASP A 15 MG MG A3001 1555 1555 2.13
LINK O ASN A 18 MG MG A3001 1555 1555 2.32
LINK O VAL A 21 MG MG A3001 1555 1555 2.17
LINK NE2 GLN A 163 MG MG A3001 1555 1555 2.34
LINK OD2 ASP A 193 MG MG A3001 1555 1555 2.38
LINK O PHE A 556 NA NA A3101 1555 1555 2.28
LINK O TYR A 559 NA NA A3101 1555 1555 2.36
LINK O LEU A 562 NA NA A3101 1555 1555 2.22
LINK O PHE A 601 NA NA A3104 1555 1555 2.81
LINK OD1 ASN A 604 NA NA A3104 1555 1555 2.57
LINK O SER A 647 NA NA A3103 1555 1555 2.68
LINK O GLU A 650 NA NA A3103 1555 1555 2.84
LINK O LEU A 670 NA NA A3103 1555 1555 2.65
LINK O PRO A 932 NA NA A3102 1555 1555 2.94
LINK O LEU A 967 NA NA A3102 1555 1555 2.60
LINK O THR A 970 NA NA A3102 1555 1555 2.66
LINK MG MG A3002 O HOH A4192 1555 1555 2.73
LINK MG MG A3002 O HOH A4482 1555 1555 2.98
LINK MG MG A3002 O HOH A4941 1555 1555 2.72
LINK NA NA A3101 O HOH A4227 1555 1555 2.60
LINK NA NA A3101 O HOH A4649 1555 1555 2.34
LINK NA NA A3102 O HOH A4213 1555 1555 2.63
LINK NA NA A3102 O HOH A4610 1555 1555 2.56
LINK NA NA A3103 O HOH A4686 1555 1555 2.99
LINK NA NA A3104 O HOH A4947 1555 1555 2.40
LINK NA NA A3104 O3 BTB A6001 1555 1555 2.75
LINK O ASP B 15 MG MG B3001 1555 1555 2.23
LINK O ASN B 18 MG MG B3001 1555 1555 2.22
LINK O VAL B 21 MG MG B3001 1555 1555 2.18
LINK NE2 GLN B 163 MG MG B3001 1555 1555 2.39
LINK OD2 ASP B 193 MG MG B3001 1555 1555 2.25
LINK OD2 ASP B 201 NA NA B3104 1555 1555 2.89
LINK O PHE B 556 NA NA B3101 1555 1555 2.21
LINK O TYR B 559 NA NA B3101 1555 1555 2.37
LINK O LEU B 562 NA NA B3101 1555 1555 2.36
LINK O PHE B 601 NA NA B3104 1555 1555 2.08
LINK ND2 ASN B 604 NA NA B3104 1555 1555 2.64
LINK O SER B 647 NA NA B3103 1555 1555 2.64
LINK O GLU B 650 NA NA B3103 1555 1555 2.80
LINK O LEU B 670 NA NA B3103 1555 1555 2.71
LINK OE1 GLN B 718 MG MG B3002 1555 1555 2.77
LINK O PRO B 932 NA NA B3102 1555 1555 2.95
LINK O LEU B 967 NA NA B3102 1555 1555 2.77
LINK O THR B 970 NA NA B3102 1555 1555 2.76
LINK MG MG B3002 O HOH B4236 1555 1555 2.25
LINK MG MG B3002 O HOH B4466 1555 1555 2.41
LINK MG MG B3002 O HOH B4574 1555 1555 2.60
LINK MG MG B3002 O HOH B4594 1555 1555 2.57
LINK NA NA B3101 O HOH B4437 1555 1555 2.56
LINK NA NA B3101 O HOH B4468 1555 1555 2.47
LINK NA NA B3102 O HOH B4415 1555 1555 2.66
LINK NA NA B3102 O HOH B4518 1555 1555 2.48
LINK NA NA B3103 O DMS B7016 1555 1555 2.34
LINK NA NA B3104 O HOH B4695 1555 1555 2.74
LINK O ASP C 15 MG MG C3001 1555 1555 2.27
LINK O ASN C 18 MG MG C3001 1555 1555 2.22
LINK O VAL C 21 MG MG C3001 1555 1555 2.14
LINK NE2 GLN C 163 MG MG C3001 1555 1555 2.35
LINK OD2 ASP C 193 MG MG C3001 1555 1555 2.44
LINK O PHE C 556 NA NA C3101 1555 1555 2.29
LINK O TYR C 559 NA NA C3101 1555 1555 2.52
LINK O LEU C 562 NA NA C3101 1555 1555 2.33
LINK O PHE C 601 NA NA C3104 1555 1555 2.85
LINK OD1 ASN C 604 NA NA C3104 1555 1555 2.61
LINK O SER C 647 NA NA C3103 1555 1555 2.69
LINK O GLU C 650 NA NA C3103 1555 1555 2.90
LINK O LEU C 670 NA NA C3103 1555 1555 2.64
LINK OE1 GLN C 718 MG MG C3002 1555 1555 2.91
LINK O PRO C 932 NA NA C3102 1555 1555 2.88
LINK O LEU C 967 NA NA C3102 1555 1555 2.73
LINK O THR C 970 NA NA C3102 1555 1555 2.72
LINK MG MG C3002 O HOH C4235 1555 1555 2.25
LINK MG MG C3002 O HOH C4324 1555 1555 2.05
LINK MG MG C3002 O HOH C4519 1555 1555 2.67
LINK MG MG C3002 O HOH C4636 1555 1555 2.36
LINK NA NA C3101 O HOH C4337 1555 1555 2.53
LINK NA NA C3101 O HOH C4485 1555 1555 2.37
LINK NA NA C3102 O HOH C4434 1555 1555 2.93
LINK NA NA C3102 O HOH C4538 1555 1555 2.50
LINK NA NA C3103 O DMS C7017 1555 1555 2.75
LINK O ASP D 15 MG MG D3001 1555 1555 2.28
LINK O ASN D 18 MG MG D3001 1555 1555 2.20
LINK O VAL D 21 MG MG D3001 1555 1555 2.21
LINK NE2 GLN D 163 MG MG D3001 1555 1555 2.40
LINK OD2 ASP D 193 MG MG D3001 1555 1555 2.33
LINK OD1 ASP D 193 MG MG D3001 1555 1555 2.94
LINK OD2 ASP D 201 NA NA D3103 1555 1555 2.93
LINK O PHE D 556 NA NA D3101 1555 1555 2.30
LINK O TYR D 559 NA NA D3101 1555 1555 2.43
LINK O LEU D 562 NA NA D3101 1555 1555 2.25
LINK O PHE D 601 NA NA D3103 1555 1555 2.05
LINK ND2 ASN D 604 NA NA D3103 1555 1555 2.21
LINK O SER D 647 NA NA D3104 1555 1555 2.72
LINK O GLU D 650 NA NA D3104 1555 1555 2.80
LINK O LEU D 670 NA NA D3104 1555 1555 2.74
LINK OE1 GLN D 718 MG MG D3002 1555 1555 2.79
LINK O PRO D 932 NA NA D3102 1555 1555 2.92
LINK O LEU D 967 NA NA D3102 1555 1555 2.64
LINK O THR D 970 NA NA D3102 1555 1555 2.65
LINK MG MG D3002 O HOH D4247 1555 1555 2.06
LINK MG MG D3002 O HOH D4520 1555 1555 2.59
LINK MG MG D3002 O HOH D4894 1555 1555 2.57
LINK NA NA D3101 O HOH D4357 1555 1555 2.80
LINK NA NA D3101 O HOH D4494 1555 1555 2.54
LINK NA NA D3102 O HOH D4440 1555 1555 2.47
LINK NA NA D3103 O1 BTB D6001 1555 1555 2.13
CISPEP 1 VAL A 86 PRO A 87 0 1.83
CISPEP 2 PRO A 111 PRO A 112 0 -0.13
CISPEP 3 ASN A 147 SER A 148 0 3.73
CISPEP 4 SER A 390 HIS A 391 0 -6.03
CISPEP 5 VAL A 421 PRO A 422 0 -5.54
CISPEP 6 TRP A 568 ASP A 569 0 -8.70
CISPEP 7 THR A 595 PRO A 596 0 0.07
CISPEP 8 GLY A 901 PRO A 902 0 3.45
CISPEP 9 VAL B 86 PRO B 87 0 4.41
CISPEP 10 PRO B 111 PRO B 112 0 -0.54
CISPEP 11 ASN B 147 SER B 148 0 2.20
CISPEP 12 SER B 390 HIS B 391 0 -8.68
CISPEP 13 VAL B 421 PRO B 422 0 -6.74
CISPEP 14 TRP B 568 ASP B 569 0 -7.38
CISPEP 15 THR B 595 PRO B 596 0 0.15
CISPEP 16 GLY B 901 PRO B 902 0 3.44
CISPEP 17 VAL C 86 PRO C 87 0 5.33
CISPEP 18 PRO C 111 PRO C 112 0 0.00
CISPEP 19 ASN C 147 SER C 148 0 2.51
CISPEP 20 SER C 390 HIS C 391 0 -7.36
CISPEP 21 VAL C 421 PRO C 422 0 -6.98
CISPEP 22 TRP C 568 ASP C 569 0 -5.52
CISPEP 23 THR C 595 PRO C 596 0 1.77
CISPEP 24 GLY C 901 PRO C 902 0 2.65
CISPEP 25 VAL D 86 PRO D 87 0 5.95
CISPEP 26 PRO D 111 PRO D 112 0 0.17
CISPEP 27 ASN D 147 SER D 148 0 3.33
CISPEP 28 SER D 390 HIS D 391 0 -6.70
CISPEP 29 VAL D 421 PRO D 422 0 -5.17
CISPEP 30 TRP D 568 ASP D 569 0 -8.08
CISPEP 31 THR D 595 PRO D 596 0 -0.22
CISPEP 32 GLY D 901 PRO D 902 0 4.66
SITE 1 AC1 5 ASP A 15 ASN A 18 VAL A 21 GLN A 163
SITE 2 AC1 5 ASP A 193
SITE 1 AC2 5 THR A 911 HOH A4192 HOH A4482 HOH A4941
SITE 2 AC2 5 DMS A7006
SITE 1 AC3 6 PHE A 556 TYR A 559 PRO A 560 LEU A 562
SITE 2 AC3 6 HOH A4227 HOH A4649
SITE 1 AC4 7 PHE A 931 PRO A 932 LEU A 967 MET A 968
SITE 2 AC4 7 THR A 970 HOH A4213 HOH A4610
SITE 1 AC5 4 SER A 647 GLU A 650 LEU A 670 HOH A4686
SITE 1 AC6 6 ASP A 201 TRP A 568 PHE A 601 ASN A 604
SITE 2 AC6 6 HOH A4947 BTB A6001
SITE 1 AC7 13 ASN A 102 ASP A 201 HIS A 391 GLN A 416
SITE 2 AC7 13 ASN A 460 GLU A 461 TYR A 503 GLU A 537
SITE 3 AC7 13 HIS A 540 TRP A 568 TRP A 999 NA A3104
SITE 4 AC7 13 HOH A4947
SITE 1 AC8 8 THR A 229 VAL A 330 GLY A 331 ARG A 448
SITE 2 AC8 8 ASN A 449 PRO A 451 ARG A 482 HOH A4342
SITE 1 AC9 4 GLU A 508 PRO A1001 VAL A1003 HOH A4360
SITE 1 BC1 4 VAL A 84 VAL A 85 HIS A 93 HOH A4881
SITE 1 BC2 4 ASP A 45 ARG A 46 SER A 48 DMS A7013
SITE 1 BC3 5 SER A 53 LEU A 54 ASN A 55 LEU A 125
SITE 2 BC3 5 HOH A4324
SITE 1 BC4 4 GLN A 719 ARG A 721 MG A3002 HOH A4941
SITE 1 BC5 5 GLU A 57 TRP A 58 ARG A 59 THR A 126
SITE 2 BC5 5 HOH A4999
SITE 1 BC6 5 TYR A 472 THR A 494 THR A 496 ARG A 531
SITE 2 BC6 5 HOH A4276
SITE 1 BC7 4 GLY A 940 GLN A 956 HOH A4224 HOH A4644
SITE 1 BC8 2 THR A 706 SER A 709
SITE 1 BC9 3 ARG A 282 GLY A 284 HOH A4196
SITE 1 CC1 4 ARG A 404 TYR A 405 HOH A5052 ASP C 772
SITE 1 CC2 6 PRO A 32 PHE A 33 TRP A 36 ASP A 45
SITE 2 CC2 6 ALA A 327 DMS A7004
SITE 1 CC3 6 LEU A 250 ARG A 251 ASP A 252 HOH A4657
SITE 2 CC3 6 ARG D 251 TYR D 253
SITE 1 CC4 4 ARG A 37 TRP A 133 GLU A 136 HIS A 216
SITE 1 CC5 2 GLN A 266 VAL A 267
SITE 1 CC6 3 GLY A 275 THR A 290 ARG A 292
SITE 1 CC7 4 GLN A 783 PHE A 784 THR A 785 HIS A 815
SITE 1 CC8 4 PHE A 629 ARG A 630 LEU A 631 TRP A 720
SITE 1 CC9 3 ILE A 714 TRP A 717 CYS A 914
SITE 1 DC1 6 ARG A 557 HIS A 622 GLN A 625 GLN A 628
SITE 2 DC1 6 GLN A 718 HOH A4454
SITE 1 DC2 6 LYS A 380 ASN A 383 PHE A 626 TYR A 642
SITE 2 DC2 6 TRP A 708 HOH A4460
SITE 1 DC3 4 VAL A 335 PRO A 480 HOH A4071 HOH A4458
SITE 1 DC4 5 ILE A 576 PRO A 584 TRP A 585 SER A 586
SITE 2 DC4 5 ARG A 973
SITE 1 DC5 5 ARG A 230 PHE A 231 ASN A 232 ARG A 237
SITE 2 DC5 5 HOH A4331
SITE 1 DC6 4 ARG A 630 SER A 632 THR A 635 GLU A 637
SITE 1 DC7 4 ILE A 737 GLU A 750 LEU A 751 GLY A 752
SITE 1 DC8 3 ASP A 428 TRP D 474 VAL D 478
SITE 1 DC9 4 THR A 271 THR A 290 LEU A 291 ARG A 292
SITE 1 EC1 3 GLU A 314 GLY A 320 HOH A4658
SITE 1 EC2 1 GLU A 264
SITE 1 EC3 3 PRO A 306 ASN A 307 ASP C 772
SITE 1 EC4 5 ASP B 15 ASN B 18 VAL B 21 GLN B 163
SITE 2 EC4 5 ASP B 193
SITE 1 EC5 6 GLN B 718 HOH B4236 HOH B4466 HOH B4574
SITE 2 EC5 6 HOH B4594 DMS B7029
SITE 1 EC6 6 PHE B 556 TYR B 559 PRO B 560 LEU B 562
SITE 2 EC6 6 HOH B4437 HOH B4468
SITE 1 EC7 6 PRO B 932 LEU B 967 MET B 968 THR B 970
SITE 2 EC7 6 HOH B4415 HOH B4518
SITE 1 EC8 4 SER B 647 GLU B 650 LEU B 670 DMS B7016
SITE 1 EC9 6 TYR B 100 ASP B 201 PHE B 601 ASN B 604
SITE 2 EC9 6 HOH B4695 BTB B6001
SITE 1 FC1 12 ASN B 102 ASP B 201 GLN B 416 GLU B 461
SITE 2 FC1 12 MET B 502 TYR B 503 GLU B 537 TRP B 568
SITE 3 FC1 12 TRP B 999 NA B3104 HOH B4024 HOH B4695
SITE 1 FC2 7 THR B 229 VAL B 330 GLY B 331 ASN B 449
SITE 2 FC2 7 PRO B 451 ARG B 482 HOH B4009
SITE 1 FC3 6 ARG B 557 HIS B 622 GLN B 628 GLN B 718
SITE 2 FC3 6 HOH B4080 HOH B4182
SITE 1 FC4 7 LYS B 380 ASN B 383 PHE B 626 TYR B 642
SITE 2 FC4 7 TRP B 708 HOH B4190 HOH B4259
SITE 1 FC5 9 PRO B 32 PHE B 33 TRP B 36 ASP B 45
SITE 2 FC5 9 ALA B 327 HOH B4350 HOH B4473 HOH B4688
SITE 3 FC5 9 DMS B7024
SITE 1 FC6 3 THR B 271 LEU B 291 ARG B 292
SITE 1 FC7 3 GLU B 314 HIS B 316 GLY B 320
SITE 1 FC8 3 PRO B 480 HOH B4185 HOH B4188
SITE 1 FC9 6 ILE B 576 PRO B 584 TRP B 585 SER B 586
SITE 2 FC9 6 ARG B 973 HOH B4093
SITE 1 GC1 6 GLY B 275 GLY B 276 VAL B 289 THR B 290
SITE 2 GC1 6 ARG B 292 HOH B4687
SITE 1 GC2 2 VAL B 85 HIS B 93
SITE 1 GC3 3 ARG B 251 ASP B 252 HOH B4929
SITE 1 GC4 5 PHE B 231 ASN B 232 ASP B 233 GLU B 334
SITE 2 GC4 5 HOH B4870
SITE 1 GC5 5 ASP B 428 PRO B 430 HIS C 226 ARG C 448
SITE 2 GC5 5 VAL C 478
SITE 1 GC6 1 HIS B 93
SITE 1 GC7 4 TYR B 926 TYR B 962 ARG B 973 HOH B4703
SITE 1 GC8 5 ASP B 648 ASN B 649 GLU B 650 ASN B 704
SITE 2 GC8 5 NA B3103
SITE 1 GC9 4 ARG B 37 SER B 132 TRP B 133 HIS B 216
SITE 1 HC1 2 TYR B 926 TYR B 962
SITE 1 HC2 4 GLU B 369 LEU B 401 ARG B 404 DMS B7020
SITE 1 HC3 3 ARG B 404 TYR B 405 DMS B7019
SITE 1 HC4 4 ILE B 305 PRO B 306 ASN B 307 HOH B4891
SITE 1 HC5 4 THR B 706 SER B 709 GLU B 710 HOH B4576
SITE 1 HC6 4 ARG B 630 SER B 632 THR B 635 GLU B 637
SITE 1 HC7 3 ASP B 45 PRO B 47 DMS B7004
SITE 1 HC8 2 ASN B 102 VAL B 103
SITE 1 HC9 5 GLN B 49 SER C 48 GLN C 49 LEU C 51
SITE 2 HC9 5 HOH C4391
SITE 1 IC1 5 ARG B 52 SER B 53 LEU B 54 ASN B 55
SITE 2 IC1 5 LEU B 125
SITE 1 IC2 3 PRO B 662 LEU B 663 SER B 665
SITE 1 IC3 6 TRP B 695 GLN B 719 ARG B 721 MG B3002
SITE 2 IC3 6 HOH B4248 HOH B4411
SITE 1 IC4 4 THR B 618 LYS B 621 ILE B 714 TRP B 717
SITE 1 IC5 3 GLU B 57 LEU B 125 THR B 126
SITE 1 IC6 4 TYR B 472 THR B 494 THR B 496 HOH C4673
SITE 1 IC7 2 ASN B 232 VAL B 239
SITE 1 IC8 4 PRO C 19 ARG C 431 TRP C 432 HOH C4879
SITE 1 IC9 5 ASP C 15 ASN C 18 VAL C 21 GLN C 163
SITE 2 IC9 5 ASP C 193
SITE 1 JC1 6 GLN C 718 HOH C4235 HOH C4324 HOH C4519
SITE 2 JC1 6 HOH C4636 DMS C7030
SITE 1 JC2 6 PHE C 556 TYR C 559 PRO C 560 LEU C 562
SITE 2 JC2 6 HOH C4337 HOH C4485
SITE 1 JC3 6 PRO C 932 LEU C 967 MET C 968 THR C 970
SITE 2 JC3 6 HOH C4434 HOH C4538
SITE 1 JC4 4 SER C 647 GLU C 650 LEU C 670 DMS C7017
SITE 1 JC5 5 ASP C 201 TRP C 568 PHE C 601 ASN C 604
SITE 2 JC5 5 HOH C4784
SITE 1 JC6 12 ASN C 102 VAL C 103 ASP C 201 HIS C 391
SITE 2 JC6 12 GLN C 416 HIS C 418 ASN C 460 GLU C 461
SITE 3 JC6 12 MET C 502 TYR C 503 GLU C 537 TRP C 568
SITE 1 JC7 8 THR C 229 VAL C 330 GLY C 331 ARG C 448
SITE 2 JC7 8 ASN C 449 PRO C 451 ARG C 482 HOH C4010
SITE 1 JC8 4 ARG C 557 HIS C 622 GLN C 623 GLN C 628
SITE 1 JC9 7 LYS C 380 ASN C 383 PHE C 626 TYR C 642
SITE 2 JC9 7 TRP C 708 HOH C4189 HOH C4258
SITE 1 KC1 7 PRO C 32 PHE C 33 TRP C 36 ASP C 45
SITE 2 KC1 7 ALA C 327 HOH C4349 HOH C4705
SITE 1 KC2 4 THR C 271 LEU C 291 ARG C 292 HOH C4830
SITE 1 KC3 4 GLU C 508 PRO C1001 VAL C1003 HOH C4034
SITE 1 KC4 4 VAL C 335 PRO C 480 HOH C4187 HOH C4414
SITE 1 KC5 2 PRO C 106 DMS C7020
SITE 1 KC6 3 TRP C 585 SER C 586 ARG C 973
SITE 1 KC7 5 GLY C 275 VAL C 289 THR C 290 ARG C 292
SITE 2 KC7 5 HOH C4590
SITE 1 KC8 4 THR C 83 VAL C 84 VAL C 85 HIS C 93
SITE 1 KC9 4 THR C 618 LYS C 621 HOH C4861 DMS C7026
SITE 1 LC1 3 LEU C 250 ARG C 251 ASP C 252
SITE 1 LC2 1 ASP C 428
SITE 1 LC3 2 GLY C 94 HOH C4639
SITE 1 LC4 2 TYR C 926 ARG C 973
SITE 1 LC5 2 ASN C 704 NA C3103
SITE 1 LC6 4 TRP C 36 ASP C 45 ARG C 46 PRO C 47
SITE 1 LC7 3 GLN C 266 LEU D 740 THR D 742
SITE 1 LC8 2 THR C 108 DMS C7008
SITE 1 LC9 3 ARG C 630 SER C 632 THR C 635
SITE 1 MC1 5 GLN C 381 THR C 706 ALA C 707 TRP C 708
SITE 2 MC1 5 SER C 709
SITE 1 MC2 3 ARG C 404 TYR C 405 HOH C4584
SITE 1 MC3 5 GLU C 314 HIS C 316 GLY C 320 THR C 321
SITE 2 MC3 5 LEU C 322
SITE 1 MC4 6 ARG C 37 GLN C 50 SER C 132 TRP C 133
SITE 2 MC4 6 GLU C 136 HIS C 216
SITE 1 MC5 3 ARG C 699 TRP C 717 DMS C7012
SITE 1 MC6 3 ARG C 230 PHE C 231 ASN C 232
SITE 1 MC7 5 LEU C 54 ASN C 55 LEU C 125 HOH C4699
SITE 2 MC7 5 HOH C4876
SITE 1 MC8 4 PHE C 231 ASN C 232 PHE C 235 GLU C 334
SITE 1 MC9 5 TRP C 695 GLN C 719 ARG C 721 MG C3002
SITE 2 MC9 5 HOH C4247
SITE 1 NC1 1 ASN C 307
SITE 1 NC2 5 ASP D 15 ASN D 18 VAL D 21 GLN D 163
SITE 2 NC2 5 ASP D 193
SITE 1 NC3 6 GLN D 718 THR D 911 HOH D4247 HOH D4520
SITE 2 NC3 6 HOH D4894 DMS D7026
SITE 1 NC4 6 PHE D 556 TYR D 559 PRO D 560 LEU D 562
SITE 2 NC4 6 HOH D4357 HOH D4494
SITE 1 NC5 6 PHE D 931 PRO D 932 LEU D 967 MET D 968
SITE 2 NC5 6 THR D 970 HOH D4440
SITE 1 NC6 4 ASP D 201 PHE D 601 ASN D 604 BTB D6001
SITE 1 NC7 3 SER D 647 GLU D 650 LEU D 670
SITE 1 NC8 13 ASN D 102 ASP D 201 HIS D 391 HIS D 418
SITE 2 NC8 13 ASN D 460 GLU D 461 TYR D 503 GLU D 537
SITE 3 NC8 13 HIS D 540 TRP D 568 ASN D 604 TRP D 999
SITE 4 NC8 13 NA D3103
SITE 1 NC9 7 THR D 229 VAL D 330 GLY D 331 ARG D 448
SITE 2 NC9 7 ASN D 449 ARG D 482 HOH D4014
SITE 1 OC1 7 ARG D 557 HIS D 622 GLN D 623 GLN D 625
SITE 2 OC1 7 GLN D 628 GLN D 718 HOH D4020
SITE 1 OC2 6 LYS D 380 ASN D 383 PHE D 626 TYR D 642
SITE 2 OC2 6 TRP D 708 HOH D4202
SITE 1 OC3 9 PRO D 32 PHE D 33 TRP D 36 ASP D 45
SITE 2 OC3 9 ALA D 327 HOH D4368 HOH D4723 HOH D4785
SITE 3 OC3 9 DMS D7015
SITE 1 OC4 4 THR D 271 LEU D 291 ARG D 292 HOH D4717
SITE 1 OC5 4 GLU A 136 GLU D 314 GLY D 320 LEU D 322
SITE 1 OC6 5 VAL D 335 PRO D 480 HOH D4197 HOH D4200
SITE 2 OC6 5 HOH D4757
SITE 1 OC7 3 SER D 586 ARG D 973 HOH D4102
SITE 1 OC8 6 GLY D 275 GLY D 276 VAL D 289 THR D 290
SITE 2 OC8 6 ARG D 292 HOH D4799
SITE 1 OC9 3 THR D 83 VAL D 85 HIS D 93
SITE 1 PC1 3 LEU D 250 ARG D 251 ASP D 252
SITE 1 PC2 1 GLY D 94
SITE 1 PC3 2 TYR D 926 ARG D 973
SITE 1 PC4 6 TRP D 36 ASP D 45 ARG D 46 PRO D 47
SITE 2 PC4 6 HOH D4420 DMS D7004
SITE 1 PC5 4 PHE D 629 GLN D 718 TRP D 720 HOH D4224
SITE 1 PC6 4 TYR D 926 ARG D 961 TYR D 962 HOH D4111
SITE 1 PC7 6 LEU D 134 GLN D 135 GLU D 136 GLY D 137
SITE 2 PC7 6 SER D 174 HOH D4847
SITE 1 PC8 1 GLY D 752
SITE 1 PC9 4 LYS D 621 TRP D 717 HOH D4304 DMS D7024
SITE 1 QC1 2 ARG D 630 SER D 632
SITE 1 QC2 3 THR D 706 SER D 709 GLU D 710
SITE 1 QC3 5 ARG D 505 GLU D 508 PRO D1001 VAL D1003
SITE 2 QC3 5 HOH D4338
SITE 1 QC4 4 TRP D 717 HOH D4331 HOH D4393 DMS D7020
SITE 1 QC5 3 LEU D 54 ASN D 55 GLU D 57
SITE 1 QC6 3 GLN D 719 ARG D 721 MG D3002
SITE 1 QC7 4 TYR D 472 THR D 494 THR D 496 ARG D 531
SITE 1 QC8 2 LEU D 823 CYS D 825
SITE 1 QC9 4 GLU D 689 LEU D 726 THR D 729 HOH D4548
CRYST1 151.230 162.340 202.060 90.00 90.00 90.00 P 21 21 21 16
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 0.006612 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006160 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004949 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
