HEADER HYDROLASE 30-JUN-09 3I3E
TITLE E. COLI (LACZ) BETA-GALACTOSIDASE (M542A)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-GALACTOSIDASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RESIDUES 10-1024;
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;
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: LMG104;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBAD/HIS/LACZ
KEYWDS BETA-GALACTOSIDASE, TIM BARREL (ALPHA/BETA BARREL), JELLY-ROLL
KEYWDS 2 BARREL, IMMUNOGLOBULIN BETA SUPERSANDWHICH, GLYCOSIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.L.DUGDALE,D.DYMIANIW,B.MINHAS,R.E.HUBER
REVDAT 4 06-SEP-23 3I3E 1 REMARK
REVDAT 3 13-OCT-21 3I3E 1 REMARK SEQADV LINK
REVDAT 2 10-AUG-11 3I3E 1 JRNL VERSN
REVDAT 1 12-MAY-10 3I3E 0
JRNL AUTH M.L.DUGDALE,D.L.DYMIANIW,B.K.MINHAS,I.D'ANGELO,R.E.HUBER
JRNL TITL ROLE OF MET-542 AS A GUIDE FOR THE CONFORMATIONAL CHANGES OF
JRNL TITL 2 PHE-601 THAT OCCUR DURING THE REACTION OF
JRNL TITL 3 β-GALACTOSIDASE (ESCHERICHIA COLI).
JRNL REF BIOCHEM.CELL BIOL. V. 88 861 2010
JRNL REFN ISSN 0829-8211
JRNL PMID 20921997
JRNL DOI 10.1139/O10-009
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 17.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 293081
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : 1.5
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.400
REMARK 3 FREE R VALUE TEST SET COUNT : 4227
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.20
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 35762
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE : 0.2780
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 544
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 32479
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 563
REMARK 3 SOLVENT ATOMS : 3611
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.23000
REMARK 3 B22 (A**2) : 2.26000
REMARK 3 B33 (A**2) : -0.03000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.18
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 64.78
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3I3E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1000053913.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-OCT-07
REMARK 200 TEMPERATURE (KELVIN) : NULL
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) : 1.11587
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 : 293082
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 17.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.960
REMARK 200 R MERGE (I) : 0.10900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1DP0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, NACL, MGCL2, DTT, BIS-TRIS,
REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 288K
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 74.85050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 100.35450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 84.20850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 100.35450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 74.85050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 84.20850
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 138180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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 LYS B 1023
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 -80.56 -83.47
REMARK 500 ASN A 110 65.25 -157.76
REMARK 500 ASP A 164 97.72 78.94
REMARK 500 ASP A 199 38.69 -98.08
REMARK 500 ASP A 224 152.79 178.12
REMARK 500 ARG A 352 76.73 -104.82
REMARK 500 GLU A 461 69.14 33.06
REMARK 500 ALA A 491 -3.24 64.94
REMARK 500 PRO A 511 50.67 -69.28
REMARK 500 ALA A 514 -46.95 68.33
REMARK 500 ALA A 541 46.87 -90.66
REMARK 500 GLN A 573 55.61 -93.34
REMARK 500 ARG A 599 -118.88 25.79
REMARK 500 ASN A 604 44.65 -148.79
REMARK 500 ASN A 649 53.09 -150.06
REMARK 500 GLU A 689 -76.23 -78.92
REMARK 500 SER A 690 174.32 -59.11
REMARK 500 LEU A 722 -147.88 -98.74
REMARK 500 ARG A 800 75.46 -101.38
REMARK 500 CYS A 825 104.01 -160.63
REMARK 500 ASP A 916 -176.74 -172.22
REMARK 500 PRO A 928 53.73 -69.65
REMARK 500 ASP A 954 87.18 -151.94
REMARK 500 ALA B 34 -11.14 -142.08
REMARK 500 ASN B 102 -81.82 -85.46
REMARK 500 ASP B 164 101.39 79.14
REMARK 500 ASP B 199 33.64 -97.12
REMARK 500 ARG B 352 76.59 -102.77
REMARK 500 GLU B 461 66.68 32.74
REMARK 500 ALA B 491 -5.36 67.36
REMARK 500 PRO B 511 58.90 -69.92
REMARK 500 ALA B 514 -44.83 69.08
REMARK 500 ALA B 541 47.11 -94.85
REMARK 500 GLN B 573 50.12 -93.48
REMARK 500 ARG B 599 -123.78 29.34
REMARK 500 ASN B 604 38.93 -149.14
REMARK 500 ARG B 611 9.27 80.18
REMARK 500 ASN B 649 49.42 -152.44
REMARK 500 GLN B 675 -0.62 75.40
REMARK 500 GLU B 689 -71.91 -86.50
REMARK 500 LEU B 722 -140.63 -105.82
REMARK 500 ARG B 909 67.22 -150.62
REMARK 500 ASP B 916 -174.59 -176.19
REMARK 500 ASP B 954 89.85 -151.74
REMARK 500 ALA C 34 -13.40 -142.44
REMARK 500 ASN C 102 -81.89 -84.79
REMARK 500 ASN C 110 59.52 -152.04
REMARK 500 ASP C 164 99.70 73.97
REMARK 500 ASP C 199 35.45 -96.62
REMARK 500 MET C 205 -169.09 -122.47
REMARK 500
REMARK 500 THIS ENTRY HAS 91 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 A3002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 15 O
REMARK 620 2 ASN A 18 O 106.7
REMARK 620 3 VAL A 21 O 108.7 82.7
REMARK 620 4 GLN A 163 OE1 97.7 155.5 91.0
REMARK 620 5 ASP A 193 OD2 92.8 84.1 157.3 93.5
REMARK 620 6 ASP A 193 OD1 138.6 80.5 112.6 80.1 46.7
REMARK 620 N 1 2 3 4 5
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 GLU A 416 OE2
REMARK 620 2 HIS A 418 ND1 97.9
REMARK 620 3 GLU A 461 OE1 85.0 84.4
REMARK 620 4 HOH A4014 O 76.7 170.1 86.9
REMARK 620 5 HOH A4078 O 170.6 91.2 93.3 94.0
REMARK 620 6 HOH A4156 O 83.5 96.6 168.5 91.0 98.2
REMARK 620 N 1 2 3 4 5
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 PHE A 556 O
REMARK 620 2 TYR A 559 O 90.5
REMARK 620 3 LEU A 562 O 93.3 89.3
REMARK 620 4 HOH A4410 O 84.0 83.6 172.3
REMARK 620 5 HOH A4652 O 115.1 153.9 94.4 93.2
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 601 O
REMARK 620 2 ASN A 604 OD1 83.4
REMARK 620 3 HOH A4170 O 167.3 106.2
REMARK 620 4 HOH A4278 O 86.9 98.9 99.5
REMARK 620 5 HOH A7338 O 78.1 86.0 94.0 163.6
REMARK 620 6 HOH A7434 O 81.2 162.2 87.9 89.2 82.1
REMARK 620 N 1 2 3 4 5
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 SER A 647 O
REMARK 620 2 GLU A 650 O 110.1
REMARK 620 3 LEU A 670 O 77.7 96.7
REMARK 620 4 HOH A6122 O 83.6 166.2 84.2
REMARK 620 5 DMS A8425 O 102.4 91.2 171.5 87.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A3003 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 718 OE1
REMARK 620 2 HOH A4268 O 96.2
REMARK 620 3 HOH A4384 O 89.2 91.8
REMARK 620 4 HOH A4450 O 80.6 175.4 91.6
REMARK 620 5 HOH A4649 O 172.2 89.7 95.7 93.1
REMARK 620 6 HOH A4721 O 57.6 102.3 144.8 73.2 116.2
REMARK 620 N 1 2 3 4 5
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 PRO A 932 O
REMARK 620 2 LEU A 967 O 80.4
REMARK 620 3 THR A 970 O 117.8 77.8
REMARK 620 4 HOH A4207 O 60.1 77.4 155.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A3005 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A7322 O
REMARK 620 2 HOH A7323 O 94.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A3009 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A4674 O
REMARK 620 2 HOH A5173 O 82.5
REMARK 620 3 HOH A5175 O 72.0 76.8
REMARK 620 4 HOH A7017 O 99.4 172.8 110.3
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 ASP B 15 O
REMARK 620 2 ASN B 18 O 102.3
REMARK 620 3 VAL B 21 O 103.5 80.1
REMARK 620 4 GLN B 163 OE1 101.6 155.9 92.0
REMARK 620 5 ASP B 193 OD2 93.2 88.8 161.6 92.3
REMARK 620 6 ASP B 193 OD1 141.8 82.6 114.6 80.2 48.7
REMARK 620 N 1 2 3 4 5
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 GLU B 416 OE2
REMARK 620 2 HIS B 418 ND1 104.9
REMARK 620 3 GLU B 461 OE1 88.5 87.9
REMARK 620 4 HOH B4014 O 75.0 175.0 87.1
REMARK 620 5 HOH B4078 O 163.0 92.2 92.2 88.0
REMARK 620 6 HOH B4156 O 86.4 96.5 174.0 88.5 91.7
REMARK 620 N 1 2 3 4 5
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 PHE B 556 O
REMARK 620 2 TYR B 559 O 90.9
REMARK 620 3 LEU B 562 O 91.7 91.1
REMARK 620 4 HOH B4410 O 79.9 82.3 169.1
REMARK 620 5 HOH B4652 O 109.7 157.9 96.2 93.2
REMARK 620 N 1 2 3 4
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 601 O
REMARK 620 2 ASN B 604 OD1 79.1
REMARK 620 3 HOH B4170 O 174.6 105.9
REMARK 620 4 HOH B4278 O 87.9 95.0 89.3
REMARK 620 5 HOH B7211 O 88.3 88.8 94.1 174.0
REMARK 620 6 HOH B7216 O 86.3 165.1 88.9 86.9 88.3
REMARK 620 N 1 2 3 4 5
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 SER B 647 O
REMARK 620 2 GLU B 650 O 115.3
REMARK 620 3 LEU B 670 O 69.2 80.9
REMARK 620 4 HOH B7217 O 126.9 69.4 59.1
REMARK 620 5 DMS B8425 O 139.4 85.1 151.3 92.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B3003 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 718 OE1
REMARK 620 2 HOH B4268 O 84.3
REMARK 620 3 HOH B4384 O 87.5 90.3
REMARK 620 4 HOH B4450 O 67.5 151.7 90.8
REMARK 620 5 HOH B4649 O 161.4 105.7 107.7 100.9
REMARK 620 6 HOH B4721 O 70.5 85.7 157.9 82.7 94.3
REMARK 620 N 1 2 3 4 5
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 PRO B 932 O
REMARK 620 2 LEU B 967 O 81.4
REMARK 620 3 THR B 970 O 123.8 86.7
REMARK 620 4 HOH B4207 O 56.9 75.4 161.9
REMARK 620 5 HOH B4558 O 109.7 106.2 126.3 58.4
REMARK 620 N 1 2 3 4
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 ASP C 15 O
REMARK 620 2 ASN C 18 O 104.7
REMARK 620 3 VAL C 21 O 107.7 86.0
REMARK 620 4 GLN C 163 OE1 98.6 154.8 95.9
REMARK 620 5 ASP C 193 OD2 91.4 85.5 160.6 84.6
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 GLU C 416 OE2
REMARK 620 2 HIS C 418 ND1 106.0
REMARK 620 3 GLU C 461 OE1 102.8 86.2
REMARK 620 4 HOH C4014 O 77.9 175.4 90.4
REMARK 620 5 HOH C4078 O 161.5 88.3 89.6 88.6
REMARK 620 6 HOH C4156 O 79.1 93.5 178.2 89.8 88.5
REMARK 620 N 1 2 3 4 5
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 PHE C 556 O
REMARK 620 2 TYR C 559 O 91.3
REMARK 620 3 LEU C 562 O 89.1 89.0
REMARK 620 4 HOH C4410 O 84.4 88.2 172.9
REMARK 620 5 HOH C4652 O 114.7 153.0 98.2 87.2
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 601 O
REMARK 620 2 ASN C 604 OD1 74.7
REMARK 620 3 HOH C4170 O 174.8 108.1
REMARK 620 4 HOH C4278 O 89.9 100.8 93.8
REMARK 620 5 HOH C7262 O 79.3 83.2 96.6 167.1
REMARK 620 6 HOH C7268 O 82.7 155.1 93.6 89.4 82.4
REMARK 620 N 1 2 3 4 5
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 SER C 647 O
REMARK 620 2 GLU C 650 O 114.0
REMARK 620 3 LEU C 670 O 73.7 87.2
REMARK 620 4 HOH C5010 O 73.8 157.6 74.7
REMARK 620 5 DMS C8425 O 118.2 84.3 167.4 111.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C3003 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN C 718 OE1
REMARK 620 2 HOH C4268 O 95.7
REMARK 620 3 HOH C4384 O 95.4 91.2
REMARK 620 4 HOH C4450 O 77.7 172.6 86.1
REMARK 620 5 HOH C4649 O 161.7 98.2 96.1 88.9
REMARK 620 6 HOH C4721 O 73.5 97.0 166.7 84.5 93.1
REMARK 620 N 1 2 3 4 5
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 PRO C 932 O
REMARK 620 2 LEU C 967 O 77.4
REMARK 620 3 THR C 970 O 108.8 79.0
REMARK 620 4 HOH C4207 O 56.7 79.5 156.5
REMARK 620 5 HOH C4763 O 155.7 125.9 73.5 127.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C3006 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C6089 O
REMARK 620 2 HOH C6218 O 85.8
REMARK 620 3 HOH C7207 O 104.6 166.2
REMARK 620 4 HOH C7267 O 172.4 86.7 82.7
REMARK 620 N 1 2 3
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 ASP D 15 O
REMARK 620 2 ASN D 18 O 101.7
REMARK 620 3 VAL D 21 O 106.0 81.5
REMARK 620 4 GLN D 163 OE1 98.5 159.6 96.1
REMARK 620 5 ASP D 193 OD2 94.0 82.5 156.4 92.9
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 GLU D 416 OE2
REMARK 620 2 HIS D 418 ND1 102.5
REMARK 620 3 GLU D 461 OE1 98.4 81.7
REMARK 620 4 HOH D4014 O 74.0 172.5 92.2
REMARK 620 5 HOH D4078 O 164.4 92.8 86.7 91.2
REMARK 620 6 HOH D4156 O 77.3 93.1 172.4 92.6 99.1
REMARK 620 N 1 2 3 4 5
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 PHE D 556 O
REMARK 620 2 TYR D 559 O 92.5
REMARK 620 3 PRO D 560 O 162.2 70.0
REMARK 620 4 LEU D 562 O 89.7 90.4 87.1
REMARK 620 5 HOH D4410 O 82.7 87.4 99.4 172.0
REMARK 620 6 HOH D4652 O 112.8 154.6 84.8 91.0 94.3
REMARK 620 N 1 2 3 4 5
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 601 O
REMARK 620 2 ASN D 604 OD1 80.1
REMARK 620 3 HOH D4278 O 87.9 95.7
REMARK 620 4 HOH D7319 O 174.9 102.9 95.8
REMARK 620 5 HOH D7341 O 77.9 85.7 165.3 98.1
REMARK 620 6 HOH D7378 O 83.3 162.9 87.9 93.4 86.7
REMARK 620 N 1 2 3 4 5
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 113.4
REMARK 620 3 LEU D 670 O 69.1 84.5
REMARK 620 4 DMS D8425 O 117.4 101.8 167.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D3003 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN D 718 OE1
REMARK 620 2 HOH D4268 O 88.1
REMARK 620 3 HOH D4384 O 82.1 89.1
REMARK 620 4 HOH D4450 O 66.3 154.3 85.9
REMARK 620 5 HOH D4649 O 161.1 110.7 99.1 94.9
REMARK 620 6 HOH D4721 O 72.3 94.1 154.1 80.1 103.7
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 PRO D 932 O
REMARK 620 2 LEU D 967 O 73.8
REMARK 620 3 THR D 970 O 106.5 71.7
REMARK 620 4 HOH D4558 O 105.5 102.5 144.1
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 MG A 3003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3009
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 3101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 3102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 3103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 3104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8406
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8407
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8408
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8410
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8411
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8412
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8413
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8414
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8419
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8420
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8421
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8425
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8427
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8502
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8503
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8504
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8602
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8603
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8604
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8605
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8608
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8609
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8610
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 8612
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3005
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 3003
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 3101
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 3102
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 3103
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 3104
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8401
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8402
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8403
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8404
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8405
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8406
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8407
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8408
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8409
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8410
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8411
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8412
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8413
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8414
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8415
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8416
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8417
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8421
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8423
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8425
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8427
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8502
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8504
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8508
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8601
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8602
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8603
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8604
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8605
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8606
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8607
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8608
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8609
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 8610
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8420
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 3003
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 3006
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 3101
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 3102
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 3103
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 3104
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8401
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8402
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8403
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8404
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8405
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8407
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8408
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8409
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8410
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8411
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8412
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8413
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8414
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8415
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8416
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8417
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8419
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 1024
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8421
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8423
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8425
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8427
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8501
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8503
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8504
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8601
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8602
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8603
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8604
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8605
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8606
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS C 8607
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 3003
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 3101
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 3102
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 3103
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 3104
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8401
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8402
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8403
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8404
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8405
REMARK 800
REMARK 800 SITE_IDENTIFIER: OC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8406
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8407
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8408
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8409
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8410
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8411
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8412
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8413
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8414
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8415
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8416
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8419
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8421
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8423
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8425
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8427
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8501
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8503
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8508
REMARK 800
REMARK 800 SITE_IDENTIFIER: RC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8701
REMARK 800
REMARK 800 SITE_IDENTIFIER: RC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8703
REMARK 800
REMARK 800 SITE_IDENTIFIER: RC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8705
REMARK 800
REMARK 800 SITE_IDENTIFIER: RC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8706
REMARK 800
REMARK 800 SITE_IDENTIFIER: RC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8707
REMARK 800
REMARK 800 SITE_IDENTIFIER: RC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8708
REMARK 800
REMARK 800 SITE_IDENTIFIER: RC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8709
REMARK 800
REMARK 800 SITE_IDENTIFIER: RC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8711
REMARK 800
REMARK 800 SITE_IDENTIFIER: RC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS D 8712
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DP0 RELATED DB: PDB
REMARK 900 E. COLI BETA-GALACTOSIDASE AT 1.7 ANGSTROM
REMARK 900 RELATED ID: 1JYX RELATED DB: PDB
REMARK 900 E. COLI (LACZ) BETA-GALACTOSIDASE IN COMPLEX WITH IPTG
REMARK 900 RELATED ID: 1JZ5 RELATED DB: PDB
REMARK 900 E. COLI (LACZ) BETA-GALACTOSIDASE IN COMPLEX WITH D-GALCTOPYRANOSYL-
REMARK 900 1-ON
REMARK 900 RELATED ID: 3I3B RELATED DB: PDB
REMARK 900 E. COLI (LACZ) BETA-GALACTOSIDASE (M542A) IN COMPLEX WITH D-
REMARK 900 GALACTOPYRANOSYL-1-ON
REMARK 900 RELATED ID: 3I3D RELATED DB: PDB
REMARK 900 E. COLI (LACZ) BETA-GALACTOSIDASE (M542A) IN COMPLEX WITH IPTG
DBREF 3I3E A 9 1023 UNP B8LFD6 B8LFD6_ECOLI 10 1024
DBREF 3I3E B 9 1023 UNP B8LFD6 B8LFD6_ECOLI 10 1024
DBREF 3I3E C 9 1023 UNP B8LFD6 B8LFD6_ECOLI 10 1024
DBREF 3I3E D 9 1023 UNP B8LFD6 B8LFD6_ECOLI 10 1024
SEQADV 3I3E GLY A 1 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E SER A 2 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E HIS A 3 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E MET A 4 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E LEU A 5 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E GLU A 6 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E ASP A 7 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E PRO A 8 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E ALA A 542 UNP B8LFD6 MET 543 ENGINEERED MUTATION
SEQADV 3I3E GLY B 1 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E SER B 2 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E HIS B 3 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E MET B 4 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E LEU B 5 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E GLU B 6 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E ASP B 7 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E PRO B 8 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E ALA B 542 UNP B8LFD6 MET 543 ENGINEERED MUTATION
SEQADV 3I3E GLY C 1 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E SER C 2 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E HIS C 3 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E MET C 4 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E LEU C 5 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E GLU C 6 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E ASP C 7 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E PRO C 8 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E ALA C 542 UNP B8LFD6 MET 543 ENGINEERED MUTATION
SEQADV 3I3E GLY D 1 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E SER D 2 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E HIS D 3 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E MET D 4 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E LEU D 5 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E GLU D 6 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E ASP D 7 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E PRO D 8 UNP B8LFD6 EXPRESSION TAG
SEQADV 3I3E ALA D 542 UNP B8LFD6 MET 543 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 GLU
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 ALA 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 GLU
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 ALA 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 GLU
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 ALA 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 GLU
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 ALA 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 MG A3003 1
HET MG A3009 1
HET NA A3101 1
HET NA A3102 1
HET NA A3103 1
HET NA A3104 1
HET DMS A8401 4
HET DMS A8402 4
HET DMS A8403 4
HET DMS A8404 4
HET DMS A8405 4
HET DMS A8406 4
HET DMS A8407 4
HET DMS A8408 4
HET DMS A8409 4
HET DMS A8410 4
HET DMS A8411 4
HET DMS A8412 4
HET DMS A8413 4
HET DMS A8414 4
HET DMS A8419 4
HET DMS A8420 4
HET DMS A8421 4
HET DMS A8425 4
HET DMS A8427 4
HET DMS A8501 4
HET DMS A8502 4
HET DMS A8503 4
HET DMS A8504 4
HET DMS A8602 4
HET DMS A8603 4
HET DMS A8604 4
HET DMS A8605 4
HET DMS A8607 4
HET DMS A8608 4
HET DMS A8609 4
HET DMS A8610 4
HET DMS A8612 4
HET MG A3005 1
HET MG B3001 1
HET MG B3002 1
HET MG B3003 1
HET NA B3101 1
HET NA B3102 1
HET NA B3103 1
HET NA B3104 1
HET DMS B8401 4
HET DMS B8402 4
HET DMS B8403 4
HET DMS B8404 4
HET DMS B8405 4
HET DMS B8406 4
HET DMS B8407 4
HET DMS B8408 4
HET DMS B8409 4
HET DMS B8410 4
HET DMS B8411 4
HET DMS B8412 4
HET DMS B8413 4
HET DMS B8414 4
HET DMS B8415 4
HET DMS B8416 4
HET DMS B8417 4
HET DMS B8421 4
HET DMS B8423 4
HET DMS B8425 4
HET DMS B8427 4
HET DMS B8502 4
HET DMS B8504 4
HET DMS B8508 4
HET DMS B8601 4
HET DMS B8602 4
HET DMS B8603 4
HET DMS B8604 4
HET DMS B8605 4
HET DMS B8606 4
HET DMS B8607 4
HET DMS B8608 4
HET DMS B8609 4
HET DMS B8610 4
HET DMS C8420 4
HET MG C3001 1
HET MG C3002 1
HET MG C3003 1
HET MG C3006 1
HET NA C3101 1
HET NA C3102 1
HET NA C3103 1
HET NA C3104 1
HET DMS C8401 4
HET DMS C8402 4
HET DMS C8403 4
HET DMS C8404 4
HET DMS C8405 4
HET DMS C8407 4
HET DMS C8408 4
HET DMS C8409 4
HET DMS C8410 4
HET DMS C8411 4
HET DMS C8412 4
HET DMS C8413 4
HET DMS C8414 4
HET DMS C8415 4
HET DMS C8416 4
HET DMS C8417 4
HET DMS C8419 4
HET DMS C1024 4
HET DMS C8421 4
HET DMS C8423 4
HET DMS C8425 4
HET DMS C8427 4
HET DMS C8501 4
HET DMS C8503 4
HET DMS C8504 4
HET DMS C8601 4
HET DMS C8602 4
HET DMS C8603 4
HET DMS C8604 4
HET DMS C8605 4
HET DMS C8606 4
HET DMS C8607 4
HET MG D3001 1
HET MG D3002 1
HET MG D3003 1
HET NA D3101 1
HET NA D3102 1
HET NA D3103 1
HET NA D3104 1
HET DMS D8401 4
HET DMS D8402 4
HET DMS D8403 4
HET DMS D8404 4
HET DMS D8405 4
HET DMS D8406 4
HET DMS D8407 4
HET DMS D8408 4
HET DMS D8409 4
HET DMS D8410 4
HET DMS D8411 4
HET DMS D8412 4
HET DMS D8413 4
HET DMS D8414 4
HET DMS D8415 4
HET DMS D8416 4
HET DMS D8419 4
HET DMS D8421 4
HET DMS D8423 4
HET DMS D8425 4
HET DMS D8427 4
HET DMS D8501 4
HET DMS D8503 4
HET DMS D8508 4
HET DMS D8701 4
HET DMS D8703 4
HET DMS D8705 4
HET DMS D8706 4
HET DMS D8707 4
HET DMS D8708 4
HET DMS D8709 4
HET DMS D8710 4
HET DMS D8711 4
HET DMS D8712 4
HETNAM MG MAGNESIUM ION
HETNAM NA SODIUM ION
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 5 MG 15(MG 2+)
FORMUL 9 NA 16(NA 1+)
FORMUL 13 DMS 133(C2 H6 O S)
FORMUL 69 HOH *3611(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 PRO A 70 5 6
HELIX 4 4 GLU A 71 CYS A 76 1 6
HELIX 5 5 ASN A 89 GLY A 94 5 6
HELIX 6 6 ASP A 130 GLU A 136 1 7
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 ASP A 598 MET A 603 5 6
HELIX 16 16 PRO A 615 GLN A 624 1 10
HELIX 17 17 LEU A 789 GLY A 794 1 6
HELIX 18 18 ALA A 805 GLY A 814 1 10
HELIX 19 19 SER A 923 TYR A 926 5 4
HELIX 20 20 SER A 963 THR A 970 1 8
HELIX 21 21 HIS A 972 LEU A 976 5 5
HELIX 22 22 SER A 1004 GLN A 1008 5 5
HELIX 23 23 ARG B 14 ASN B 18 5 5
HELIX 24 24 ASN B 38 THR B 44 1 7
HELIX 25 25 ALA B 65 VAL B 69 5 5
HELIX 26 26 PRO B 70 GLU B 75 5 6
HELIX 27 27 ASN B 89 GLY B 94 5 6
HELIX 28 28 ASP B 130 GLU B 136 1 7
HELIX 29 29 SER B 192 GLU B 198 5 7
HELIX 30 30 ASP B 368 ASN B 382 1 15
HELIX 31 31 HIS B 395 GLY B 406 1 12
HELIX 32 32 ASP B 429 ARG B 431 5 3
HELIX 33 33 TRP B 432 ARG B 448 1 17
HELIX 34 34 GLY B 465 ASP B 479 1 15
HELIX 35 35 SER B 519 SER B 525 1 7
HELIX 36 36 GLY B 548 TYR B 559 1 12
HELIX 37 37 ASP B 598 MET B 603 5 6
HELIX 38 38 PRO B 615 GLN B 624 1 10
HELIX 39 39 LEU B 789 GLY B 794 1 6
HELIX 40 40 ALA B 805 GLY B 814 1 10
HELIX 41 41 SER B 923 TYR B 926 5 4
HELIX 42 42 SER B 963 THR B 970 1 8
HELIX 43 43 HIS B 972 LEU B 976 5 5
HELIX 44 44 SER B 1004 GLN B 1008 5 5
HELIX 45 45 ARG C 14 ASN C 18 5 5
HELIX 46 46 ASN C 38 THR C 44 1 7
HELIX 47 47 ALA C 65 PRO C 70 5 6
HELIX 48 48 GLU C 71 CYS C 76 1 6
HELIX 49 49 ASN C 89 GLY C 94 5 6
HELIX 50 50 ASP C 130 GLN C 135 1 6
HELIX 51 51 SER C 192 GLU C 198 5 7
HELIX 52 52 ASP C 368 ASN C 382 1 15
HELIX 53 53 HIS C 395 GLY C 406 1 12
HELIX 54 54 ASP C 429 ARG C 431 5 3
HELIX 55 55 TRP C 432 ARG C 448 1 17
HELIX 56 56 GLY C 465 ASP C 479 1 15
HELIX 57 57 SER C 519 SER C 525 1 7
HELIX 58 58 GLY C 548 TYR C 559 1 12
HELIX 59 59 ASP C 598 MET C 603 5 6
HELIX 60 60 PRO C 615 GLN C 624 1 10
HELIX 61 61 LEU C 789 GLY C 794 1 6
HELIX 62 62 ALA C 805 GLY C 814 1 10
HELIX 63 63 SER C 923 TYR C 926 5 4
HELIX 64 64 SER C 963 THR C 970 1 8
HELIX 65 65 HIS C 972 LEU C 976 5 5
HELIX 66 66 SER C 1004 GLN C 1008 5 5
HELIX 67 67 ARG D 14 ASN D 18 5 5
HELIX 68 68 ASN D 38 THR D 44 1 7
HELIX 69 69 ALA D 65 VAL D 69 5 5
HELIX 70 70 PRO D 70 GLU D 75 5 6
HELIX 71 71 ASN D 89 GLY D 94 5 6
HELIX 72 72 ASP D 130 GLU D 136 1 7
HELIX 73 73 SER D 192 GLU D 198 5 7
HELIX 74 74 ASP D 368 ASN D 382 1 15
HELIX 75 75 HIS D 395 GLY D 406 1 12
HELIX 76 76 ASP D 429 ARG D 431 5 3
HELIX 77 77 TRP D 432 ARG D 448 1 17
HELIX 78 78 GLY D 465 ASP D 479 1 15
HELIX 79 79 SER D 519 SER D 525 1 7
HELIX 80 80 GLY D 548 TYR D 559 1 12
HELIX 81 81 ASP D 598 MET D 603 5 6
HELIX 82 82 PRO D 615 GLN D 624 1 10
HELIX 83 83 LEU D 789 GLY D 794 1 6
HELIX 84 84 ALA D 805 GLY D 814 1 10
HELIX 85 85 SER D 923 TYR D 926 5 4
HELIX 86 86 SER D 963 THR D 970 1 8
HELIX 87 87 HIS D 972 LEU D 976 5 5
HELIX 88 88 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 THR A 101 0
SHEET 2 C 2 MET A 202 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 VAL A 267
SHEET 3 F 4 TYR A 309 THR A 317 -1 O ARG A 310 N TRP A 261
SHEET 4 F 4 LEU A 322 VAL A 330 -1 O VAL A 330 N TYR A 309
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 GLN A 563 N ILE A 351
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 THR A 639 N GLN A 628
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 LEU A 652 O VAL A 668
SHEET 3 K 4 GLY A 692 GLN A 702 -1 O THR A 697 N MET A 655
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 SER A 960 O TRP A 983
SHEET 5 M 9 ARG A1013 GLN A1022 -1 O CYS A1021 N GLN A 950
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 PHE A 850
SHEET 9 M 9 GLU A 819 THR A 829 -1 N ASP A 828 O LEU A 835
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 SER A 960 O TRP A 983
SHEET 5 N 7 ARG A 938 TYR A 946 -1 N THR A 941 O PHE A 955
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 TRP A 918 N TRP A 897
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 THR B 101 0
SHEET 2 Q 2 MET B 202 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 LEU B 260 O ALA B 268
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 VAL B 330 N TYR B 309
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 GLU B 637 N ARG B 630
SHEET 3 Y 3 LYS B 677 GLU B 681 -1 O GLN B 678 N VAL B 638
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 ARG B 699 N HIS B 653
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 LYS B 754 N LEU B 751
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 SER B 960 O TRP B 983
SHEET 5 AB 9 ARG B1013 CYS B1021 -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 LEU B 830 -1 N LEU B 830 O ALA B 833
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 SER B 960 O TRP B 983
SHEET 5 AC 7 ARG B 938 TYR B 946 -1 N THR B 941 O PHE B 955
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 PHE C 171 N ILE C 141
SHEET 1 AF 2 ILE C 99 THR C 101 0
SHEET 2 AF 2 MET C 202 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 LEU C 260 O ALA C 268
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 VAL C 330 N TYR C 309
SHEET 1 AJ 3 VAL C 335 GLU C 338 0
SHEET 2 AJ 3 LEU C 341 LEU C 344 -1 O LEU C 343 N ARG C 336
SHEET 3 AJ 3 LYS C 347 PRO C 348 -1 O LYS C 347 N LEU C 344
SHEET 1 AK 7 VAL C 484 GLN C 485 0
SHEET 2 AK 7 VAL C 453 SER C 457 1 N TRP C 456 O GLN C 485
SHEET 3 AK 7 TYR C 408 GLU C 412 1 N ASP C 411 O SER C 457
SHEET 4 AK 7 ALA C 386 ARG C 388 1 N VAL C 387 O TYR C 408
SHEET 5 AK 7 ILE C 351 ASN C 355 1 N VAL C 354 O ARG C 388
SHEET 6 AK 7 LEU C 562 VAL C 567 1 O VAL C 567 N ASN C 355
SHEET 7 AK 7 LEU C 533 TYR C 538 1 N LEU C 533 O GLN C 563
SHEET 1 AL 2 LEU C 575 TYR C 578 0
SHEET 2 AL 2 PRO C 584 ALA C 587 -1 O ALA C 587 N LEU C 575
SHEET 1 AM 3 PHE C 627 SER C 632 0
SHEET 2 AM 3 THR C 635 SER C 640 -1 O GLU C 637 N ARG C 630
SHEET 3 AM 3 LYS C 677 GLU C 681 -1 O ILE C 680 N ILE C 636
SHEET 1 AN 4 LYS C 661 PRO C 669 0
SHEET 2 AN 4 LEU C 651 LEU C 658 -1 N LEU C 652 O VAL C 668
SHEET 3 AN 4 GLY C 692 GLN C 702 -1 O TRP C 695 N ALA C 657
SHEET 4 AN 4 HIS C 713 ASN C 725 -1 O ASN C 725 N GLY C 692
SHEET 1 AO 5 HIS C 739 THR C 742 0
SHEET 2 AO 5 ASP C 746 LEU C 751 -1 O GLU C 750 N HIS C 739
SHEET 3 AO 5 LYS C 754 ASN C 759 -1 O PHE C 758 N PHE C 747
SHEET 4 AO 5 LEU C 765 ILE C 770 -1 O GLN C 767 N GLN C 757
SHEET 5 AO 5 LYS C 773 LYS C 774 -1 O LYS C 773 N ILE C 770
SHEET 1 AP 9 LEU C 776 GLN C 783 0
SHEET 2 AP 9 ARG C 881 LEU C 888 -1 O GLN C 887 N LEU C 777
SHEET 3 AP 9 THR C 982 HIS C 990 -1 O THR C 982 N LEU C 888
SHEET 4 AP 9 HIS C 949 SER C 960 -1 N GLN C 956 O ASP C 987
SHEET 5 AP 9 ARG C1013 GLN C1022 -1 O CYS C1021 N GLN C 950
SHEET 6 AP 9 MET C 864 VAL C 872 -1 N ILE C 866 O LEU C1018
SHEET 7 AP 9 LYS C 847 ASP C 859 -1 N ARG C 853 O ASP C 869
SHEET 8 AP 9 ALA C 833 HIS C 844 -1 N TRP C 842 O PHE C 850
SHEET 9 AP 9 GLU C 819 LEU C 830 -1 N LEU C 830 O ALA C 833
SHEET 1 AQ 7 LEU C 776 GLN C 783 0
SHEET 2 AQ 7 ARG C 881 LEU C 888 -1 O GLN C 887 N LEU C 777
SHEET 3 AQ 7 THR C 982 HIS C 990 -1 O THR C 982 N LEU C 888
SHEET 4 AQ 7 HIS C 949 SER C 960 -1 N GLN C 956 O ASP C 987
SHEET 5 AQ 7 ARG C 938 TYR C 946 -1 N THR C 941 O PHE C 955
SHEET 6 AQ 7 ARG C 894 GLY C 901 -1 N ASN C 896 O ASN C 945
SHEET 7 AQ 7 CYS C 914 PRO C 921 -1 O TRP C 918 N TRP C 897
SHEET 1 AR 7 GLN D 23 LEU D 24 0
SHEET 2 AR 7 ARG D 157 GLN D 163 -1 O TYR D 161 N LEU D 24
SHEET 3 AR 7 ALA D 149 CYS D 154 -1 N LEU D 152 O VAL D 159
SHEET 4 AR 7 ASN D 182 LEU D 189 -1 O LEU D 189 N ALA D 149
SHEET 5 AR 7 THR D 120 PHE D 127 -1 N TYR D 123 O VAL D 186
SHEET 6 AR 7 GLY D 56 PHE D 63 -1 N PHE D 63 O THR D 120
SHEET 7 AR 7 ASP D 82 VAL D 86 -1 O ASP D 82 N PHE D 60
SHEET 1 AS 4 LEU D 51 SER D 53 0
SHEET 2 AS 4 VAL D 212 LYS D 217 -1 O LEU D 214 N ARG D 52
SHEET 3 AS 4 GLN D 138 PHE D 143 -1 N ILE D 142 O SER D 213
SHEET 4 AS 4 SER D 169 ASP D 172 -1 O PHE D 171 N ILE D 141
SHEET 1 AT 2 ILE D 99 THR D 101 0
SHEET 2 AT 2 MET D 202 ARG D 204 -1 O ARG D 204 N ILE D 99
SHEET 1 AU 2 VAL D 146 ASN D 147 0
SHEET 2 AU 2 GLY D 207 ILE D 208 -1 O GLY D 207 N ASN D 147
SHEET 1 AV 3 GLN D 221 PHE D 231 0
SHEET 2 AV 3 ARG D 237 CYS D 247 -1 O GLN D 245 N ASP D 224
SHEET 3 AV 3 ARG D 288 GLU D 296 -1 O VAL D 289 N VAL D 244
SHEET 1 AW 4 THR D 265 PRO D 273 0
SHEET 2 AW 4 LEU D 254 GLN D 262 -1 N GLN D 262 O THR D 265
SHEET 3 AW 4 TYR D 309 THR D 317 -1 O HIS D 316 N ARG D 255
SHEET 4 AW 4 LEU D 322 VAL D 330 -1 O VAL D 330 N TYR D 309
SHEET 1 AX 3 VAL D 335 GLU D 338 0
SHEET 2 AX 3 LEU D 341 LEU D 344 -1 O LEU D 343 N ARG D 336
SHEET 3 AX 3 LYS D 347 PRO D 348 -1 O LYS D 347 N LEU D 344
SHEET 1 AY 7 VAL D 484 GLN D 485 0
SHEET 2 AY 7 VAL D 453 SER D 457 1 N TRP D 456 O GLN D 485
SHEET 3 AY 7 TYR D 408 GLU D 412 1 N ASP D 411 O SER D 457
SHEET 4 AY 7 ALA D 386 ARG D 388 1 N VAL D 387 O TYR D 408
SHEET 5 AY 7 ILE D 351 ASN D 355 1 N VAL D 354 O ARG D 388
SHEET 6 AY 7 LEU D 562 VAL D 567 1 O GLN D 563 N ILE D 351
SHEET 7 AY 7 LEU D 533 TYR D 538 1 N LEU D 535 O PHE D 566
SHEET 1 AZ 2 LEU D 575 TYR D 578 0
SHEET 2 AZ 2 PRO D 584 ALA D 587 -1 O ALA D 587 N LEU D 575
SHEET 1 BA 3 PHE D 627 SER D 632 0
SHEET 2 BA 3 THR D 635 SER D 640 -1 O GLU D 637 N ARG D 630
SHEET 3 BA 3 LYS D 677 GLU D 681 -1 O GLN D 678 N VAL D 638
SHEET 1 BB 4 LYS D 661 PRO D 669 0
SHEET 2 BB 4 LEU D 651 LEU D 658 -1 N LEU D 652 O VAL D 668
SHEET 3 BB 4 GLY D 692 GLN D 702 -1 O ARG D 699 N HIS D 653
SHEET 4 BB 4 HIS D 713 ASN D 725 -1 O LEU D 722 N LEU D 694
SHEET 1 BC 5 HIS D 739 THR D 742 0
SHEET 2 BC 5 ASP D 746 LEU D 751 -1 O CYS D 748 N THR D 741
SHEET 3 BC 5 LYS D 754 ASN D 759 -1 O PHE D 758 N PHE D 747
SHEET 4 BC 5 LEU D 765 ILE D 770 -1 O GLN D 767 N GLN D 757
SHEET 5 BC 5 LYS D 773 LYS D 774 -1 O LYS D 773 N ILE D 770
SHEET 1 BD 9 LEU D 776 GLN D 783 0
SHEET 2 BD 9 ARG D 881 LEU D 888 -1 O GLN D 887 N LEU D 777
SHEET 3 BD 9 THR D 982 HIS D 990 -1 O ILE D 986 N LEU D 884
SHEET 4 BD 9 HIS D 949 SER D 960 -1 N GLN D 956 O ASP D 987
SHEET 5 BD 9 ARG D1013 GLN D1022 -1 O CYS D1021 N GLN D 950
SHEET 6 BD 9 MET D 864 VAL D 872 -1 N ILE D 866 O LEU D1018
SHEET 7 BD 9 LYS D 847 ASP D 859 -1 N ARG D 853 O ASP D 869
SHEET 8 BD 9 ALA D 833 HIS D 844 -1 N TRP D 842 O PHE D 850
SHEET 9 BD 9 GLU D 819 THR D 829 -1 N ASP D 828 O LEU D 835
SHEET 1 BE 7 LEU D 776 GLN D 783 0
SHEET 2 BE 7 ARG D 881 LEU D 888 -1 O GLN D 887 N LEU D 777
SHEET 3 BE 7 THR D 982 HIS D 990 -1 O ILE D 986 N LEU D 884
SHEET 4 BE 7 HIS D 949 SER D 960 -1 N GLN D 956 O ASP D 987
SHEET 5 BE 7 ARG D 938 TYR D 946 -1 N LEU D 944 O TRP D 951
SHEET 6 BE 7 ARG D 894 GLY D 901 -1 N ASN D 896 O ASN D 945
SHEET 7 BE 7 CYS D 914 PRO D 921 -1 O TRP D 918 N TRP D 897
LINK O ASP A 15 MG MG A3002 1555 1555 2.21
LINK O ASN A 18 MG MG A3002 1555 1555 2.30
LINK O VAL A 21 MG MG A3002 1555 1555 2.28
LINK OE1 GLN A 163 MG MG A3002 1555 1555 2.24
LINK OD2 ASP A 193 MG MG A3002 1555 1555 2.30
LINK OD1 ASP A 193 MG MG A3002 1555 1555 3.00
LINK OE2 GLU A 416 MG MG A3001 1555 1555 2.14
LINK ND1 HIS A 418 MG MG A3001 1555 1555 2.25
LINK OE1 GLU A 461 MG MG A3001 1555 1555 2.19
LINK O PHE A 556 NA NA A3102 1555 1555 2.21
LINK O TYR A 559 NA NA A3102 1555 1555 2.27
LINK O LEU A 562 NA NA A3102 1555 1555 2.27
LINK O PHE A 601 NA NA A3101 1555 1555 2.24
LINK OD1 ASN A 604 NA NA A3101 1555 1555 2.22
LINK O SER A 647 NA NA A3104 1555 1555 2.58
LINK O GLU A 650 NA NA A3104 1555 1555 2.47
LINK O LEU A 670 NA NA A3104 1555 1555 2.38
LINK OE1 GLN A 718 MG MG A3003 1555 1555 2.32
LINK O PRO A 932 NA NA A3103 1555 1555 2.73
LINK O LEU A 967 NA NA A3103 1555 1555 2.88
LINK O THR A 970 NA NA A3103 1555 1555 2.79
LINK MG MG A3001 O HOH A4014 1555 1555 2.28
LINK MG MG A3001 O HOH A4078 1555 1555 2.12
LINK MG MG A3001 O HOH A4156 1555 1555 2.17
LINK MG MG A3003 O HOH A4268 1555 1555 2.33
LINK MG MG A3003 O HOH A4384 1555 1555 2.33
LINK MG MG A3003 O HOH A4450 1555 1555 2.38
LINK MG MG A3003 O HOH A4649 1555 1555 2.24
LINK MG MG A3003 O HOH A4721 1555 1555 2.74
LINK MG MG A3005 O HOH A7322 1555 1555 2.81
LINK MG MG A3005 O HOH A7323 1555 1555 2.16
LINK MG MG A3009 O HOH A4674 1555 1555 2.46
LINK MG MG A3009 O HOH A5173 1555 1555 2.42
LINK MG MG A3009 O HOH A5175 1555 1555 2.73
LINK MG MG A3009 O HOH A7017 1555 1555 2.75
LINK NA NA A3101 O HOH A4170 1555 1555 2.36
LINK NA NA A3101 O HOH A4278 1555 1555 2.38
LINK NA NA A3101 O HOH A7338 1555 1555 2.53
LINK NA NA A3101 O HOH A7434 1555 1555 2.52
LINK NA NA A3102 O HOH A4410 1555 1555 2.61
LINK NA NA A3102 O HOH A4652 1555 1555 2.41
LINK NA NA A3103 O HOH A4207 1555 1555 3.17
LINK NA NA A3104 O HOH A6122 1555 1555 2.87
LINK NA NA A3104 O DMS A8425 1555 1555 2.27
LINK O ASP B 15 MG MG B3002 1555 1555 2.26
LINK O ASN B 18 MG MG B3002 1555 1555 2.37
LINK O VAL B 21 MG MG B3002 1555 1555 2.37
LINK OE1 GLN B 163 MG MG B3002 1555 1555 2.23
LINK OD2 ASP B 193 MG MG B3002 1555 1555 2.23
LINK OD1 ASP B 193 MG MG B3002 1555 1555 2.88
LINK OE2 GLU B 416 MG MG B3001 1555 1555 2.07
LINK ND1 HIS B 418 MG MG B3001 1555 1555 2.27
LINK OE1 GLU B 461 MG MG B3001 1555 1555 1.99
LINK O PHE B 556 NA NA B3102 1555 1555 2.20
LINK O TYR B 559 NA NA B3102 1555 1555 2.22
LINK O LEU B 562 NA NA B3102 1555 1555 2.28
LINK O PHE B 601 NA NA B3101 1555 1555 2.09
LINK OD1 ASN B 604 NA NA B3101 1555 1555 2.28
LINK O SER B 647 NA NA B3104 1555 1555 2.38
LINK O GLU B 650 NA NA B3104 1555 1555 2.77
LINK O LEU B 670 NA NA B3104 1555 1555 2.87
LINK OE1 GLN B 718 MG MG B3003 1555 1555 2.52
LINK O PRO B 932 NA NA B3103 1555 1555 2.71
LINK O LEU B 967 NA NA B3103 1555 1555 2.58
LINK O THR B 970 NA NA B3103 1555 1555 2.50
LINK MG MG B3001 O HOH B4014 1555 1555 2.37
LINK MG MG B3001 O HOH B4078 1555 1555 2.21
LINK MG MG B3001 O HOH B4156 1555 1555 2.18
LINK MG MG B3003 O HOH B4268 1555 1555 2.26
LINK MG MG B3003 O HOH B4384 1555 1555 2.35
LINK MG MG B3003 O HOH B4450 1555 1555 2.26
LINK MG MG B3003 O HOH B4649 1555 1555 2.10
LINK MG MG B3003 O HOH B4721 1555 1555 2.60
LINK NA NA B3101 O HOH B4170 1555 1555 2.30
LINK NA NA B3101 O HOH B4278 1555 1555 2.37
LINK NA NA B3101 O HOH B7211 1555 1555 2.38
LINK NA NA B3101 O HOH B7216 1555 1555 2.40
LINK NA NA B3102 O HOH B4410 1555 1555 2.64
LINK NA NA B3102 O HOH B4652 1555 1555 2.44
LINK NA NA B3103 O HOH B4207 1555 1555 3.20
LINK NA NA B3103 O HOH B4558 1555 1555 3.09
LINK NA NA B3104 O HOH B7217 1555 1555 2.64
LINK NA NA B3104 O DMS B8425 1555 1555 2.18
LINK O ASP C 15 MG MG C3002 1555 1555 2.29
LINK O ASN C 18 MG MG C3002 1555 1555 2.30
LINK O VAL C 21 MG MG C3002 1555 1555 2.18
LINK OE1 GLN C 163 MG MG C3002 1555 1555 2.41
LINK OD2 ASP C 193 MG MG C3002 1555 1555 2.45
LINK OE2 GLU C 416 MG MG C3001 1555 1555 2.02
LINK ND1 HIS C 418 MG MG C3001 1555 1555 2.35
LINK OE1 GLU C 461 MG MG C3001 1555 1555 2.01
LINK O PHE C 556 NA NA C3102 1555 1555 2.28
LINK O TYR C 559 NA NA C3102 1555 1555 2.26
LINK O LEU C 562 NA NA C3102 1555 1555 2.33
LINK O PHE C 601 NA NA C3101 1555 1555 2.19
LINK OD1 ASN C 604 NA NA C3101 1555 1555 2.24
LINK O SER C 647 NA NA C3104 1555 1555 2.39
LINK O GLU C 650 NA NA C3104 1555 1555 2.67
LINK O LEU C 670 NA NA C3104 1555 1555 2.47
LINK OE1 GLN C 718 MG MG C3003 1555 1555 2.24
LINK O PRO C 932 NA NA C3103 1555 1555 2.94
LINK O LEU C 967 NA NA C3103 1555 1555 2.70
LINK O THR C 970 NA NA C3103 1555 1555 2.69
LINK MG MG C3001 O HOH C4014 1555 1555 2.26
LINK MG MG C3001 O HOH C4078 1555 1555 2.39
LINK MG MG C3001 O HOH C4156 1555 1555 2.19
LINK MG MG C3003 O HOH C4268 1555 1555 2.14
LINK MG MG C3003 O HOH C4384 1555 1555 2.46
LINK MG MG C3003 O HOH C4450 1555 1555 2.40
LINK MG MG C3003 O HOH C4649 1555 1555 2.27
LINK MG MG C3003 O HOH C4721 1555 1555 2.35
LINK MG MG C3006 O HOH C6089 1555 1555 2.16
LINK MG MG C3006 O HOH C6218 1555 1555 2.33
LINK MG MG C3006 O HOH C7207 1555 1555 2.59
LINK MG MG C3006 O HOH C7267 1555 1555 2.28
LINK NA NA C3101 O HOH C4170 1555 1555 2.31
LINK NA NA C3101 O HOH C4278 1555 1555 2.28
LINK NA NA C3101 O HOH C7262 1555 1555 2.49
LINK NA NA C3101 O HOH C7268 1555 1555 2.38
LINK NA NA C3102 O HOH C4410 1555 1555 2.55
LINK NA NA C3102 O HOH C4652 1555 1555 2.72
LINK NA NA C3103 O HOH C4207 1555 1555 3.12
LINK NA NA C3103 O HOH C4763 1555 1555 3.13
LINK NA NA C3104 O HOH C5010 1555 1555 2.93
LINK NA NA C3104 O DMS C8425 1555 1555 2.26
LINK O ASP D 15 MG MG D3002 1555 1555 2.26
LINK O ASN D 18 MG MG D3002 1555 1555 2.36
LINK O VAL D 21 MG MG D3002 1555 1555 2.27
LINK OE1 GLN D 163 MG MG D3002 1555 1555 2.33
LINK OD2 ASP D 193 MG MG D3002 1555 1555 2.28
LINK OE2 GLU D 416 MG MG D3001 1555 1555 2.11
LINK ND1 HIS D 418 MG MG D3001 1555 1555 2.29
LINK OE1 GLU D 461 MG MG D3001 1555 1555 2.05
LINK O PHE D 556 NA NA D3102 1555 1555 2.23
LINK O TYR D 559 NA NA D3102 1555 1555 2.20
LINK O PRO D 560 NA NA D3102 1555 1555 3.20
LINK O LEU D 562 NA NA D3102 1555 1555 2.32
LINK O PHE D 601 NA NA D3101 1555 1555 2.18
LINK OD1 ASN D 604 NA NA D3101 1555 1555 2.30
LINK O SER D 647 NA NA D3104 1555 1555 2.46
LINK O GLU D 650 NA NA D3104 1555 1555 2.76
LINK O LEU D 670 NA NA D3104 1555 1555 2.81
LINK OE1 GLN D 718 MG MG D3003 1555 1555 2.61
LINK O PRO D 932 NA NA D3103 1555 1555 3.01
LINK O LEU D 967 NA NA D3103 1555 1555 3.06
LINK O THR D 970 NA NA D3103 1555 1555 2.86
LINK MG MG D3001 O HOH D4014 1555 1555 2.26
LINK MG MG D3001 O HOH D4078 1555 1555 2.18
LINK MG MG D3001 O HOH D4156 1555 1555 2.26
LINK MG MG D3003 O HOH D4268 1555 1555 2.22
LINK MG MG D3003 O HOH D4384 1555 1555 2.43
LINK MG MG D3003 O HOH D4450 1555 1555 2.35
LINK MG MG D3003 O HOH D4649 1555 1555 2.41
LINK MG MG D3003 O HOH D4721 1555 1555 2.48
LINK NA NA D3101 O HOH D4278 1555 1555 2.52
LINK NA NA D3101 O HOH D7319 1555 1555 2.41
LINK NA NA D3101 O HOH D7341 1555 1555 2.44
LINK NA NA D3101 O HOH D7378 1555 1555 2.53
LINK NA NA D3102 O HOH D4410 1555 1555 2.52
LINK NA NA D3102 O HOH D4652 1555 1555 2.49
LINK NA NA D3103 O HOH D4558 1555 1555 3.07
LINK NA NA D3104 O DMS D8425 1555 1555 2.28
CISPEP 1 VAL A 86 PRO A 87 0 0.34
CISPEP 2 PRO A 111 PRO A 112 0 0.09
CISPEP 3 ASN A 147 SER A 148 0 0.22
CISPEP 4 SER A 390 HIS A 391 0 -0.50
CISPEP 5 VAL A 421 PRO A 422 0 -0.51
CISPEP 6 TRP A 568 ASP A 569 0 -0.52
CISPEP 7 THR A 595 PRO A 596 0 -0.12
CISPEP 8 GLY A 901 PRO A 902 0 0.32
CISPEP 9 VAL B 86 PRO B 87 0 0.30
CISPEP 10 PRO B 111 PRO B 112 0 0.24
CISPEP 11 ASN B 147 SER B 148 0 0.29
CISPEP 12 SER B 390 HIS B 391 0 -0.36
CISPEP 13 VAL B 421 PRO B 422 0 -0.31
CISPEP 14 TRP B 568 ASP B 569 0 -0.40
CISPEP 15 THR B 595 PRO B 596 0 -0.10
CISPEP 16 GLY B 901 PRO B 902 0 0.37
CISPEP 17 VAL C 86 PRO C 87 0 0.26
CISPEP 18 PRO C 111 PRO C 112 0 0.14
CISPEP 19 ASN C 147 SER C 148 0 0.12
CISPEP 20 SER C 390 HIS C 391 0 -0.42
CISPEP 21 VAL C 421 PRO C 422 0 -0.51
CISPEP 22 TRP C 568 ASP C 569 0 -0.43
CISPEP 23 THR C 595 PRO C 596 0 -0.03
CISPEP 24 GLY C 901 PRO C 902 0 0.28
CISPEP 25 VAL D 86 PRO D 87 0 0.10
CISPEP 26 PRO D 111 PRO D 112 0 0.13
CISPEP 27 ASN D 147 SER D 148 0 0.22
CISPEP 28 SER D 390 HIS D 391 0 -0.42
CISPEP 29 VAL D 421 PRO D 422 0 -0.53
CISPEP 30 TRP D 568 ASP D 569 0 -0.48
CISPEP 31 THR D 595 PRO D 596 0 -0.09
CISPEP 32 GLY D 901 PRO D 902 0 0.23
SITE 1 AC1 6 GLU A 416 HIS A 418 GLU A 461 HOH A4014
SITE 2 AC1 6 HOH A4078 HOH A4156
SITE 1 AC2 5 ASP A 15 ASN A 18 VAL A 21 GLN A 163
SITE 2 AC2 5 ASP A 193
SITE 1 AC3 6 GLN A 718 HOH A4268 HOH A4384 HOH A4450
SITE 2 AC3 6 HOH A4649 HOH A4721
SITE 1 AC4 4 HOH A4674 HOH A5173 HOH A5175 HOH A7017
SITE 1 AC5 7 ASP A 201 PHE A 601 ASN A 604 HOH A4170
SITE 2 AC5 7 HOH A4278 HOH A7338 HOH A7434
SITE 1 AC6 6 PHE A 556 TYR A 559 PRO A 560 LEU A 562
SITE 2 AC6 6 HOH A4410 HOH A4652
SITE 1 AC7 4 PHE A 931 PRO A 932 LEU A 967 THR A 970
SITE 1 AC8 5 SER A 647 GLU A 650 LEU A 670 HOH A6122
SITE 2 AC8 5 DMS A8425
SITE 1 AC9 7 THR A 229 VAL A 330 GLY A 331 ASN A 449
SITE 2 AC9 7 PRO A 451 ARG A 482 HOH A4011
SITE 1 BC1 4 ARG A 557 HIS A 622 GLN A 628 HOH A4205
SITE 1 BC2 7 LYS A 380 ASN A 383 PHE A 626 TYR A 642
SITE 2 BC2 7 TRP A 708 HOH A4214 HOH A7340
SITE 1 BC3 8 PRO A 32 PHE A 33 ALA A 34 TRP A 36
SITE 2 BC3 8 ALA A 327 HOH A4423 HOH A4663 HOH A7341
SITE 1 BC4 4 THR A 271 LEU A 291 ARG A 292 HOH A7342
SITE 1 BC5 3 HIS A 316 GLY A 320 LEU A 322
SITE 1 BC6 5 ARG A 505 GLU A 508 PRO A1001 VAL A1003
SITE 2 BC6 5 HOH A4037
SITE 1 BC7 3 LEU A 54 ASN A 55 HOH A4764
SITE 1 BC8 4 VAL A 335 PRO A 480 HOH A4212 HOH A7346
SITE 1 BC9 3 PRO A 106 TRP A 191 HOH A4371
SITE 1 CC1 5 PRO A 584 TRP A 585 SER A 586 ARG A 973
SITE 2 CC1 5 HOH A4102
SITE 1 CC2 5 GLU A 277 VAL A 289 THR A 290 ARG A 292
SITE 2 CC2 5 HOH A4615
SITE 1 CC3 3 GLY A 593 THR A 595 HOH A7349
SITE 1 CC4 3 VAL A 84 VAL A 85 HIS A 93
SITE 1 CC5 4 TYR A 105 PRO A 106 THR A 108 HOH A4481
SITE 1 CC6 3 ASP A 428 PRO A 430 ARG D 448
SITE 1 CC7 2 GLY A 94 TYR A 95
SITE 1 CC8 6 ASP A 648 ASN A 649 GLU A 650 ASN A 704
SITE 2 CC8 6 NA A3104 LYS C1023
SITE 1 CC9 4 TRP A 695 GLN A 719 ARG A 721 HOH A4450
SITE 1 DC1 4 TRP A 36 ASP A 45 PRO A 47 HOH A4757
SITE 1 DC2 4 GLU A 57 ARG A 59 LEU A 125 THR A 126
SITE 1 DC3 6 PHE A 629 ARG A 630 GLN A 718 TRP A 720
SITE 2 DC3 6 HOH A4238 HOH A5003
SITE 1 DC4 4 ARG A 37 SER A 132 TRP A 133 HIS A 216
SITE 1 DC5 2 GLN A 266 VAL A 267
SITE 1 DC6 3 ARG A 699 ILE A 714 TRP A 717
SITE 1 DC7 3 GLY A 283 GLY A 284 VAL D 421
SITE 1 DC8 3 ARG A 251 ASP A 252 ARG D 251
SITE 1 DC9 4 TYR A 472 THR A 494 THR A 496 ARG A 531
SITE 1 EC1 4 ARG A 630 SER A 632 THR A 635 GLU A 637
SITE 1 EC2 4 ARG A 230 PHE A 231 ASN A 232 VAL A 239
SITE 1 EC3 3 GLU B 40 TRP B 261 GLU B 264
SITE 1 EC4 5 HOH A7322 HOH A7323 HOH D4674 HOH D5173
SITE 2 EC4 5 HOH D5175
SITE 1 EC5 6 GLU B 416 HIS B 418 GLU B 461 HOH B4014
SITE 2 EC5 6 HOH B4078 HOH B4156
SITE 1 EC6 5 ASP B 15 ASN B 18 VAL B 21 GLN B 163
SITE 2 EC6 5 ASP B 193
SITE 1 EC7 6 GLN B 718 HOH B4268 HOH B4384 HOH B4450
SITE 2 EC7 6 HOH B4649 HOH B4721
SITE 1 EC8 7 ASP B 201 PHE B 601 ASN B 604 HOH B4170
SITE 2 EC8 7 HOH B4278 HOH B7211 HOH B7216
SITE 1 EC9 6 PHE B 556 TYR B 559 PRO B 560 LEU B 562
SITE 2 EC9 6 HOH B4410 HOH B4652
SITE 1 FC1 4 PRO B 932 LEU B 967 THR B 970 HOH B4558
SITE 1 FC2 7 SER B 647 ASP B 648 ASN B 649 GLU B 650
SITE 2 FC2 7 LEU B 670 HOH B7217 DMS B8425
SITE 1 FC3 6 THR B 229 GLY B 331 ASN B 449 PRO B 451
SITE 2 FC3 6 ARG B 482 HOH B4011
SITE 1 FC4 5 ARG B 557 HIS B 622 GLN B 625 GLN B 628
SITE 2 FC4 5 HOH B4205
SITE 1 FC5 6 LYS B 380 ASN B 383 PHE B 626 TYR B 642
SITE 2 FC5 6 TRP B 708 HOH B4214
SITE 1 FC6 6 PRO B 32 PHE B 33 ALA B 34 ASP B 45
SITE 2 FC6 6 ALA B 327 HOH B4423
SITE 1 FC7 4 THR B 271 LEU B 291 ARG B 292 HOH B4724
SITE 1 FC8 3 GLU B 314 HIS B 316 GLY B 320
SITE 1 FC9 5 GLU B 508 PRO B1001 VAL B1003 HOH B4037
SITE 2 FC9 5 HOH B7195
SITE 1 GC1 2 LEU B 54 ASN B 55
SITE 1 GC2 5 GLU B 334 PRO B 480 HOH B4209 HOH B4212
SITE 2 GC2 5 HOH B7221
SITE 1 GC3 3 PRO B 106 ILE B 107 THR B 108
SITE 1 GC4 3 SER B 586 ARG B 973 HOH B4102
SITE 1 GC5 5 GLY B 275 GLY B 276 THR B 290 ARG B 292
SITE 2 GC5 5 HOH B6053
SITE 1 GC6 2 PRO B 106 PRO B 115
SITE 1 GC7 3 VAL B 84 VAL B 85 HIS B 93
SITE 1 GC8 2 LYS B 621 HOH B4339
SITE 1 GC9 3 LEU B 250 ARG B 251 ASP B 252
SITE 1 HC1 3 PHE B 231 ASN B 232 GLU B 334
SITE 1 HC2 3 HIS B 93 GLY B 94 TYR B 95
SITE 1 HC3 3 TYR B 926 TYR B 962 ARG B 973
SITE 1 HC4 5 ASP B 648 ASN B 649 GLU B 650 ASN B 704
SITE 2 HC4 5 NA B3104
SITE 1 HC5 4 GLN B 719 ARG B 721 HOH B4284 HOH B4552
SITE 1 HC6 4 GLU B 57 LEU B 125 THR B 126 HOH B4539
SITE 1 HC7 4 ARG B 37 SER B 132 TRP B 133 HIS B 216
SITE 1 HC8 1 TYR B 962
SITE 1 HC9 4 VAL B 267 VAL B 295 GLU B 296 HOH B4586
SITE 1 IC1 3 ASP B 45 ARG B 46 PRO B 47
SITE 1 IC2 6 ARG B 230 PHE B 231 ASN B 232 ARG B 237
SITE 2 IC2 6 ALA B 238 VAL B 239
SITE 1 IC3 6 TYR B 472 THR B 494 THR B 496 ASP B 497
SITE 2 IC3 6 HOH B4681 HOH B7290
SITE 1 IC4 3 SER B 269 ARG B 292 ASN B 294
SITE 1 IC5 2 TYR B 405 HOH B4189
SITE 1 IC6 2 ALA B 707 SER B 709
SITE 1 IC7 1 GLY B 346
SITE 1 IC8 4 PHE B 608 ASP B 610 THR B 612 ARG B 973
SITE 1 IC9 5 ARG B 630 SER B 632 THR B 635 GLU B 637
SITE 2 IC9 5 LEU B 679
SITE 1 JC1 2 ASP B 428 VAL C 478
SITE 1 JC2 6 GLU C 416 HIS C 418 GLU C 461 HOH C4014
SITE 2 JC2 6 HOH C4078 HOH C4156
SITE 1 JC3 5 ASP C 15 ASN C 18 VAL C 21 GLN C 163
SITE 2 JC3 5 ASP C 193
SITE 1 JC4 6 GLN C 718 HOH C4268 HOH C4384 HOH C4450
SITE 2 JC4 6 HOH C4649 HOH C4721
SITE 1 JC5 6 HOH A7052 HOH B7156 HOH C6089 HOH C6218
SITE 2 JC5 6 HOH C7207 HOH C7267
SITE 1 JC6 7 ASP C 201 PHE C 601 ASN C 604 HOH C4170
SITE 2 JC6 7 HOH C4278 HOH C7262 HOH C7268
SITE 1 JC7 6 PHE C 556 TYR C 559 PRO C 560 LEU C 562
SITE 2 JC7 6 HOH C4410 HOH C4652
SITE 1 JC8 5 PHE C 931 PRO C 932 LEU C 967 MET C 968
SITE 2 JC8 5 THR C 970
SITE 1 JC9 5 SER C 647 GLU C 650 LEU C 670 HOH C5010
SITE 2 JC9 5 DMS C8425
SITE 1 KC1 6 THR C 229 GLY C 331 ASN C 449 PRO C 451
SITE 2 KC1 6 ARG C 482 HOH C4011
SITE 1 KC2 4 ARG C 557 HIS C 622 GLN C 628 HOH C4205
SITE 1 KC3 6 LYS C 380 ASN C 383 PHE C 626 TYR C 642
SITE 2 KC3 6 TRP C 708 HOH C4214
SITE 1 KC4 8 PRO C 32 PHE C 33 TRP C 36 ASP C 45
SITE 2 KC4 8 ALA C 327 HOH C4423 HOH C4436 HOH C4663
SITE 1 KC5 3 THR C 271 LEU C 291 ARG C 292
SITE 1 KC6 7 ARG C 505 GLU C 508 PRO C1001 SER C1002
SITE 2 KC6 7 VAL C1003 HOH C4037 HOH C7279
SITE 1 KC7 3 LEU C 54 ASN C 55 HOH C6186
SITE 1 KC8 4 VAL C 335 PRO C 480 HOH C4209 HOH C4212
SITE 1 KC9 4 PRO C 106 PRO C 115 TRP C 191 HOH C4371
SITE 1 LC1 4 PRO C 584 SER C 586 ARG C 973 HOH C4102
SITE 1 LC2 5 GLY C 275 GLU C 277 THR C 290 ARG C 292
SITE 2 LC2 5 HOH C6053
SITE 1 LC3 1 THR C 595
SITE 1 LC4 3 VAL C 84 VAL C 85 HIS C 93
SITE 1 LC5 3 LYS C 621 TRP C 717 HOH C4339
SITE 1 LC6 3 LEU C 250 ARG C 251 ASP C 252
SITE 1 LC7 2 PHE C 231 GLU C 334
SITE 1 LC8 3 TYR C 105 PRO C 106 HOH C4481
SITE 1 LC9 2 ASP C 428 PRO C 430
SITE 1 MC1 3 HIS C 93 TYR C 95 HOH C4650
SITE 1 MC2 3 TYR C 926 TYR C 962 ARG C 973
SITE 1 MC3 5 ASP C 648 ASN C 649 GLU C 650 ASN C 704
SITE 2 MC3 5 NA C3104
SITE 1 MC4 5 GLN C 719 ARG C 721 HOH C4284 HOH C4450
SITE 2 MC4 5 HOH C4552
SITE 1 MC5 2 ASP C 45 PRO C 47
SITE 1 MC6 4 PHE C 629 GLN C 718 TRP C 720 HOH C4238
SITE 1 MC7 4 ARG C 37 SER C 132 TRP C 133 HIS C 216
SITE 1 MC8 4 VAL C 267 VAL C 295 GLU C 296 HOH C4586
SITE 1 MC9 5 GLN C 266 VAL C 267 ALA C 268 LEU D 740
SITE 2 MC9 5 THR D 742
SITE 1 NC1 3 ALA C 707 SER C 709 GLU C 710
SITE 1 NC2 5 ALA C 268 SER C 269 ARG C 292 LEU C 293
SITE 2 NC2 5 ASN C 294
SITE 1 NC3 2 ILE C 305 ASN C 307
SITE 1 NC4 4 TYR C 472 THR C 494 THR C 496 ASP C 497
SITE 1 NC5 6 ARG C 230 PHE C 231 ASN C 232 ARG C 237
SITE 2 NC5 6 ALA C 238 VAL C 239
SITE 1 NC6 6 GLU D 416 HIS D 418 GLU D 461 HOH D4014
SITE 2 NC6 6 HOH D4078 HOH D4156
SITE 1 NC7 5 ASP D 15 ASN D 18 VAL D 21 GLN D 163
SITE 2 NC7 5 ASP D 193
SITE 1 NC8 6 GLN D 718 HOH D4268 HOH D4384 HOH D4450
SITE 2 NC8 6 HOH D4649 HOH D4721
SITE 1 NC9 7 ASP D 201 PHE D 601 ASN D 604 HOH D4278
SITE 2 NC9 7 HOH D7319 HOH D7341 HOH D7378
SITE 1 OC1 6 PHE D 556 TYR D 559 PRO D 560 LEU D 562
SITE 2 OC1 6 HOH D4410 HOH D4652
SITE 1 OC2 5 PHE D 931 PRO D 932 LEU D 967 THR D 970
SITE 2 OC2 5 HOH D4558
SITE 1 OC3 6 SER D 647 ASP D 648 ASN D 649 GLU D 650
SITE 2 OC3 6 LEU D 670 DMS D8425
SITE 1 OC4 6 THR D 229 VAL D 330 GLY D 331 ASN D 449
SITE 2 OC4 6 PRO D 451 HOH D4011
SITE 1 OC5 4 ARG D 557 HIS D 622 GLN D 628 HOH D4205
SITE 1 OC6 7 LYS D 380 ASN D 383 PHE D 626 TYR D 642
SITE 2 OC6 7 TRP D 708 HOH D4214 HOH D4301
SITE 1 OC7 5 PRO D 32 PHE D 33 TRP D 36 ALA D 327
SITE 2 OC7 5 HOH D7372
SITE 1 OC8 3 THR D 271 LEU D 291 ARG D 292
SITE 1 OC9 5 GLU A 136 GLU D 314 HIS D 316 GLY D 320
SITE 2 OC9 5 HOH D7245
SITE 1 PC1 5 ARG D 505 GLU D 508 PRO D1001 VAL D1003
SITE 2 PC1 5 HOH D4387
SITE 1 PC2 4 LEU D 54 ASN D 55 GLU D 57 HOH D4764
SITE 1 PC3 3 VAL D 335 PRO D 480 HOH D4212
SITE 1 PC4 3 PRO D 106 PRO D 115 HOH D4371
SITE 1 PC5 4 PRO D 584 SER D 586 ARG D 973 HOH D4102
SITE 1 PC6 5 GLY D 275 GLY D 276 THR D 290 ARG D 292
SITE 2 PC6 5 HOH D4615
SITE 1 PC7 2 GLY D 593 THR D 595
SITE 1 PC8 4 THR D 83 VAL D 84 VAL D 85 HIS D 93
SITE 1 PC9 3 LYS D 621 TRP D 717 HOH D4339
SITE 1 QC1 3 LEU D 250 ARG D 251 ASP D 252
SITE 1 QC2 4 TYR D 105 PRO D 106 ILE D 107 THR D 108
SITE 1 QC3 1 GLY D 94
SITE 1 QC4 3 TYR D 926 TYR D 962 ARG D 973
SITE 1 QC5 6 GLN B1022 ASP D 648 ASN D 649 GLU D 650
SITE 2 QC5 6 ASN D 704 NA D3104
SITE 1 QC6 3 TRP D 695 GLN D 719 ARG D 721
SITE 1 QC7 4 TRP D 36 ASP D 45 PRO D 47 HOH D4512
SITE 1 QC8 5 PHE D 629 ARG D 630 GLN D 718 TRP D 720
SITE 2 QC8 5 HOH D4238
SITE 1 QC9 5 SER D 923 TYR D 926 ARG D 961 TYR D 962
SITE 2 QC9 5 HOH D4111
SITE 1 RC1 5 PRO A 218 ILE A 323 HOH A5081 HOH A5084
SITE 2 RC1 5 GLY D 320
SITE 1 RC2 2 GLN D 49 ASP D 130
SITE 1 RC3 1 ASP D 428
SITE 1 RC4 4 ARG C 721 LEU C 722 ALA C 723 ASP D 875
SITE 1 RC5 3 THR D 706 SER D 709 GLU D 710
SITE 1 RC6 4 ARG D 630 SER D 632 THR D 635 GLU D 637
SITE 1 RC7 3 ILE D 737 HIS D 739 GLY D 752
SITE 1 RC8 5 TRP D 133 LEU D 134 GLU D 136 GLY D 137
SITE 2 RC8 5 SER D 174
SITE 1 RC9 5 PHE D 231 ASN D 232 ASP D 233 PHE D 235
SITE 2 RC9 5 GLU D 334
CRYST1 149.701 168.417 200.709 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 0.006680 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005938 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004982 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
