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HEADER HYDROLASE 28-SEP-18 6MLY
TITLE BIFUNCTIONAL GH43-CE BACTEROIDES EGGERTHII, BACEGG_01304
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL GH43-CE PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.2.1.37;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES EGGERTHII;
SOURCE 3 ORGANISM_TAXID: 28111;
SOURCE 4 GENE: XYNB_2, NCTC11155_00458;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GLYCOSIDE HYDROLASE, GH43, CARBOHYDRATE ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.M.KOROPATKIN,G.V.PEREIRA,I.CANN
REVDAT 1 02-OCT-19 6MLY 0
JRNL AUTH G.V.PEREIRA,C.DALESSANDRO-GABAZZA,J.FARRIS,D.WEFERS,
JRNL AUTH 2 R.MACKIE,N.M.KOROPATKIN,E.C.GABAZZA,I.CANN
JRNL TITL COMPLEX ARABINOXYLAN FERMENTING BACTEROIDETES RELEASE
JRNL TITL 2 DIETARY ANTIOXIDANTS THAT IMPACT HOST IMMUNE FUNCTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0222
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 107971
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5719
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6923
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.3180
REMARK 3 BIN FREE R VALUE SET COUNT : 406
REMARK 3 BIN FREE R VALUE : 0.3620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23692
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 396
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.05000
REMARK 3 B22 (A**2) : -7.08000
REMARK 3 B33 (A**2) : 1.68000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 3.78000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.351
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.370
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 44.282
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.892
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 24349 ; 0.006 ; 0.014
REMARK 3 BOND LENGTHS OTHERS (A): 21577 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 32966 ; 0.960 ; 1.654
REMARK 3 BOND ANGLES OTHERS (DEGREES): 50417 ; 0.714 ; 1.643
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3017 ; 7.630 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1230 ;32.050 ;22.634
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3896 ;15.835 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 120 ;18.217 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3064 ; 0.044 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 27499 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 4865 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 45926 ; 2.298 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 303 ;73.485 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 45418 ;23.149 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 27 A 788
REMARK 3 ORIGIN FOR THE GROUP (A): -36.3059 21.8862 40.9369
REMARK 3 T TENSOR
REMARK 3 T11: 0.8513 T22: 1.0939
REMARK 3 T33: 0.0452 T12: -0.2969
REMARK 3 T13: -0.1465 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 1.0978 L22: 0.3168
REMARK 3 L33: 1.3733 L12: 0.4697
REMARK 3 L13: 1.1901 L23: 0.6034
REMARK 3 S TENSOR
REMARK 3 S11: 0.1713 S12: 0.0435 S13: -0.0165
REMARK 3 S21: 0.2258 S22: -0.1571 S23: 0.0080
REMARK 3 S31: 0.3448 S32: -0.1600 S33: -0.0141
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 25 B 788
REMARK 3 ORIGIN FOR THE GROUP (A): -19.8728 -22.6804 45.2291
REMARK 3 T TENSOR
REMARK 3 T11: 0.4371 T22: 0.5119
REMARK 3 T33: 0.0725 T12: -0.0022
REMARK 3 T13: -0.1008 T23: 0.0372
REMARK 3 L TENSOR
REMARK 3 L11: 0.6746 L22: 0.2749
REMARK 3 L33: 1.4432 L12: 0.0788
REMARK 3 L13: 0.9361 L23: 0.0760
REMARK 3 S TENSOR
REMARK 3 S11: -0.0010 S12: 0.1455 S13: 0.0105
REMARK 3 S21: 0.0303 S22: 0.0278 S23: 0.0741
REMARK 3 S31: -0.0723 S32: 0.0188 S33: -0.0268
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 23 C 788
REMARK 3 ORIGIN FOR THE GROUP (A): 24.7989 44.6941 45.5872
REMARK 3 T TENSOR
REMARK 3 T11: 0.5809 T22: 0.5836
REMARK 3 T33: 0.1235 T12: 0.0165
REMARK 3 T13: -0.1389 T23: -0.0256
REMARK 3 L TENSOR
REMARK 3 L11: 0.4654 L22: 0.2130
REMARK 3 L33: 1.9016 L12: 0.2490
REMARK 3 L13: -0.8538 L23: -0.5821
REMARK 3 S TENSOR
REMARK 3 S11: 0.0306 S12: 0.1182 S13: 0.0197
REMARK 3 S21: 0.0729 S22: 0.0411 S23: -0.0294
REMARK 3 S31: -0.0977 S32: 0.0021 S33: -0.0716
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 25 D 788
REMARK 3 ORIGIN FOR THE GROUP (A): 41.5370 -1.1876 48.4750
REMARK 3 T TENSOR
REMARK 3 T11: 0.4995 T22: 0.5746
REMARK 3 T33: 0.0988 T12: 0.0101
REMARK 3 T13: -0.1249 T23: -0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 0.9372 L22: 0.1997
REMARK 3 L33: 2.1052 L12: 0.3596
REMARK 3 L13: -1.2695 L23: -0.6344
REMARK 3 S TENSOR
REMARK 3 S11: -0.0526 S12: 0.1641 S13: 0.0296
REMARK 3 S21: 0.0724 S22: 0.0301 S23: -0.0302
REMARK 3 S31: -0.0661 S32: -0.0579 S33: 0.0225
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 6MLY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1000237193.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-APR-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : C(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300-HS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 113694
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.16100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 1.10500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: MRBUMP
REMARK 200 STARTING MODEL: 3ZXL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMSO4, 0.1M MES PH 6.5, 30% PEG
REMARK 280 5K; STREAK SEEDING TO PRODUCE LARGER CRYSTALS, MICROBATCH,
REMARK 280 TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 127.36700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.65500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 127.36700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 46.65500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 7
REMARK 465 SER A 8
REMARK 465 HIS A 9
REMARK 465 MET A 10
REMARK 465 ALA A 11
REMARK 465 SER A 12
REMARK 465 MET A 13
REMARK 465 THR A 14
REMARK 465 GLY A 15
REMARK 465 GLY A 16
REMARK 465 GLN A 17
REMARK 465 GLN A 18
REMARK 465 MET A 19
REMARK 465 GLY A 20
REMARK 465 ARG A 21
REMARK 465 GLY A 22
REMARK 465 SER A 23
REMARK 465 GLN A 24
REMARK 465 LYS A 25
REMARK 465 PRO A 26
REMARK 465 ASN A 166
REMARK 465 GLY A 167
REMARK 465 LYS A 168
REMARK 465 PRO A 183
REMARK 465 GLY A 184
REMARK 465 THR A 185
REMARK 465 GLU A 186
REMARK 465 ARG A 187
REMARK 465 VAL A 188
REMARK 465 LEU A 189
REMARK 465 ILE A 190
REMARK 465 GLU A 191
REMARK 465 ASN A 192
REMARK 465 ALA A 193
REMARK 465 SER A 194
REMARK 465 ALA A 195
REMARK 465 PRO A 196
REMARK 465 ALA A 197
REMARK 465 GLY A 198
REMARK 465 ASP A 199
REMARK 465 ASN A 200
REMARK 465 ILE A 201
REMARK 465 MET A 202
REMARK 465 LEU A 203
REMARK 465 GLY A 204
REMARK 465 ALA A 205
REMARK 465 GLU A 206
REMARK 465 ILE A 222
REMARK 465 THR A 223
REMARK 465 TRP A 224
REMARK 465 PRO A 225
REMARK 465 ARG A 226
REMARK 465 GLY A 227
REMARK 465 GLY A 228
REMARK 465 VAL A 229
REMARK 465 ARG A 230
REMARK 465 THR A 241
REMARK 465 GLY A 242
REMARK 465 PRO A 243
REMARK 465 TYR A 244
REMARK 465 GLU A 245
REMARK 465 LYS A 291
REMARK 465 ASP A 292
REMARK 465 GLY A 293
REMARK 465 GLY A 298
REMARK 465 VAL A 299
REMARK 465 ASN A 300
REMARK 465 GLY A 301
REMARK 465 ARG A 302
REMARK 465 ALA A 303
REMARK 465 PRO A 304
REMARK 465 ALA A 305
REMARK 465 LYS A 306
REMARK 465 THR A 419
REMARK 465 ASP A 420
REMARK 465 GLY A 421
REMARK 465 LYS A 422
REMARK 465 VAL A 777
REMARK 465 THR A 778
REMARK 465 ILE A 797
REMARK 465 TYR A 798
REMARK 465 ARG A 799
REMARK 465 ASP A 800
REMARK 465 LEU A 801
REMARK 465 ASN A 802
REMARK 465 ARG A 803
REMARK 465 ILE A 804
REMARK 465 ARG A 805
REMARK 465 PRO A 806
REMARK 465 ILE A 807
REMARK 465 LYS A 808
REMARK 465 CYS A 809
REMARK 465 ASP A 810
REMARK 465 ASP A 811
REMARK 465 ILE A 812
REMARK 465 LYS A 813
REMARK 465 GLY B 7
REMARK 465 SER B 8
REMARK 465 HIS B 9
REMARK 465 MET B 10
REMARK 465 ALA B 11
REMARK 465 SER B 12
REMARK 465 MET B 13
REMARK 465 THR B 14
REMARK 465 GLY B 15
REMARK 465 GLY B 16
REMARK 465 GLN B 17
REMARK 465 GLN B 18
REMARK 465 MET B 19
REMARK 465 GLY B 20
REMARK 465 ARG B 21
REMARK 465 GLY B 22
REMARK 465 SER B 23
REMARK 465 GLN B 24
REMARK 465 ILE B 797
REMARK 465 TYR B 798
REMARK 465 ARG B 799
REMARK 465 ASP B 800
REMARK 465 LEU B 801
REMARK 465 ASN B 802
REMARK 465 ARG B 803
REMARK 465 ILE B 804
REMARK 465 ARG B 805
REMARK 465 PRO B 806
REMARK 465 ILE B 807
REMARK 465 LYS B 808
REMARK 465 CYS B 809
REMARK 465 ASP B 810
REMARK 465 ASP B 811
REMARK 465 ILE B 812
REMARK 465 LYS B 813
REMARK 465 GLY C 7
REMARK 465 SER C 8
REMARK 465 HIS C 9
REMARK 465 MET C 10
REMARK 465 ALA C 11
REMARK 465 SER C 12
REMARK 465 MET C 13
REMARK 465 THR C 14
REMARK 465 GLY C 15
REMARK 465 GLY C 16
REMARK 465 GLN C 17
REMARK 465 GLN C 18
REMARK 465 MET C 19
REMARK 465 GLY C 20
REMARK 465 ARG C 21
REMARK 465 GLY C 22
REMARK 465 ILE C 797
REMARK 465 TYR C 798
REMARK 465 ARG C 799
REMARK 465 ASP C 800
REMARK 465 LEU C 801
REMARK 465 ASN C 802
REMARK 465 ARG C 803
REMARK 465 ILE C 804
REMARK 465 ARG C 805
REMARK 465 PRO C 806
REMARK 465 ILE C 807
REMARK 465 LYS C 808
REMARK 465 CYS C 809
REMARK 465 ASP C 810
REMARK 465 ASP C 811
REMARK 465 ILE C 812
REMARK 465 LYS C 813
REMARK 465 GLY D 7
REMARK 465 SER D 8
REMARK 465 HIS D 9
REMARK 465 MET D 10
REMARK 465 ALA D 11
REMARK 465 SER D 12
REMARK 465 MET D 13
REMARK 465 THR D 14
REMARK 465 GLY D 15
REMARK 465 GLY D 16
REMARK 465 GLN D 17
REMARK 465 GLN D 18
REMARK 465 MET D 19
REMARK 465 GLY D 20
REMARK 465 ARG D 21
REMARK 465 GLY D 22
REMARK 465 SER D 23
REMARK 465 GLN D 24
REMARK 465 ILE D 797
REMARK 465 TYR D 798
REMARK 465 ARG D 799
REMARK 465 ASP D 800
REMARK 465 LEU D 801
REMARK 465 ASN D 802
REMARK 465 ARG D 803
REMARK 465 ILE D 804
REMARK 465 ARG D 805
REMARK 465 PRO D 806
REMARK 465 ILE D 807
REMARK 465 LYS D 808
REMARK 465 CYS D 809
REMARK 465 ASP D 810
REMARK 465 ASP D 811
REMARK 465 ILE D 812
REMARK 465 LYS D 813
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 139 CG CD CE NZ
REMARK 470 LYS A 175 CG CD CE NZ
REMARK 470 LYS A 182 CG CD CE NZ
REMARK 470 LYS A 239 CG CD CE NZ
REMARK 470 GLU A 308 CG CD OE1 OE2
REMARK 470 ASP A 311 CG OD1 OD2
REMARK 470 ASN A 473 CG OD1 ND2
REMARK 470 MET A 487 CG SD CE
REMARK 470 LYS A 519 CG CD CE NZ
REMARK 470 LYS A 534 CG CD CE NZ
REMARK 470 MET A 547 CG SD CE
REMARK 470 ASP A 548 CG OD1 OD2
REMARK 470 GLU A 549 CG CD OE1 OE2
REMARK 470 LYS A 578 CG CD CE NZ
REMARK 470 GLN A 773 CG CD OE1 NE2
REMARK 470 LYS B 25 CG CD CE NZ
REMARK 470 LYS C 534 CG CD CE NZ
REMARK 470 ASP C 546 CG OD1 OD2
REMARK 470 ASP C 548 CG OD1 OD2
REMARK 470 LYS C 650 CG CD CE NZ
REMARK 470 LYS D 25 CG CD CE NZ
REMARK 470 ASP D 532 CG OD1 OD2
REMARK 470 ASP D 713 CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS A 182 C LYS A 182 O 0.417
REMARK 500 ILE A 240 C ILE A 240 O 0.300
REMARK 500 TRP A 290 C TRP A 290 O 0.178
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 107 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 107 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 MET A 55 -106.76 53.65
REMARK 500 VAL A 61 77.41 47.49
REMARK 500 VAL A 70 -54.40 -121.85
REMARK 500 ASP A 80 -61.69 -94.10
REMARK 500 THR A 96 36.46 -145.82
REMARK 500 ARG A 99 -121.38 -99.34
REMARK 500 TRP A 102 -158.55 -102.69
REMARK 500 PRO A 145 -162.94 -78.19
REMARK 500 GLN A 251 73.52 -155.31
REMARK 500 GLN A 257 123.97 76.52
REMARK 500 CYS A 276 37.16 -97.82
REMARK 500 PRO A 310 167.36 -48.28
REMARK 500 PRO A 335 150.11 -41.29
REMARK 500 HIS A 342 -175.47 62.86
REMARK 500 GLU A 398 109.91 -50.39
REMARK 500 GLN A 408 -147.79 -153.57
REMARK 500 VAL A 438 -60.87 -93.21
REMARK 500 ASN A 499 103.98 -177.30
REMARK 500 SER A 561 -2.76 -145.20
REMARK 500 ASN A 567 20.90 -152.83
REMARK 500 PRO A 601 36.65 -96.87
REMARK 500 THR A 625 30.74 -92.90
REMARK 500 SER A 634 -122.63 51.87
REMARK 500 ASN A 647 109.89 -42.65
REMARK 500 ILE A 685 -60.45 -134.30
REMARK 500 ASN A 694 -64.27 -136.41
REMARK 500 ASN A 747 -58.87 -15.66
REMARK 500 GLN A 773 144.13 78.83
REMARK 500 MET B 55 -122.48 55.43
REMARK 500 VAL B 61 74.90 58.71
REMARK 500 LEU B 69 -6.60 82.34
REMARK 500 ASN B 84 72.55 -100.35
REMARK 500 ARG B 99 -117.45 -125.70
REMARK 500 TRP B 102 -157.60 -105.13
REMARK 500 ALA B 205 116.09 -38.04
REMARK 500 GLN B 257 113.72 82.13
REMARK 500 LYS B 291 -72.02 -112.34
REMARK 500 PRO B 335 153.31 -42.92
REMARK 500 HIS B 342 -173.93 62.40
REMARK 500 THR B 367 -51.71 -127.35
REMARK 500 GLN B 408 -159.85 -161.76
REMARK 500 ASP B 420 -96.60 49.70
REMARK 500 LYS B 440 132.93 -170.05
REMARK 500 ASN B 499 100.23 -177.06
REMARK 500 LYS B 503 -34.44 -146.32
REMARK 500 ASP B 518 32.68 -98.88
REMARK 500 ASP B 532 74.47 -100.86
REMARK 500 SER B 561 15.81 -149.55
REMARK 500 TRP B 563 13.01 59.30
REMARK 500 ASN B 567 45.69 -161.24
REMARK 500
REMARK 500 THIS ENTRY HAS 127 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN B 166 GLY B 167 -41.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG B 494 0.11 SIDE CHAIN
REMARK 500 ARG C 236 0.10 SIDE CHAIN
REMARK 500 ARG C 762 0.08 SIDE CHAIN
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 NA A 904 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 645 O
REMARK 620 2 TYR A 726 O 72.1
REMARK 620 3 ASP A 728 OD1 148.2 110.7
REMARK 620 4 ASP A 731 OD1 92.5 110.5 56.2
REMARK 620 5 ASP A 731 OD2 72.8 65.5 79.7 45.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 903 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 645 O
REMARK 620 2 TYR B 726 O 73.5
REMARK 620 3 ASP B 728 OD1 122.1 92.8
REMARK 620 4 ASP B 731 OD1 75.3 106.5 54.9
REMARK 620 5 ASP B 731 OD2 57.9 65.4 65.2 41.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 904 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 645 O
REMARK 620 2 TYR C 726 O 84.2
REMARK 620 3 ASP C 728 OD1 136.6 97.6
REMARK 620 4 ASP C 731 OD1 77.3 116.5 63.1
REMARK 620 5 ASP C 731 OD2 72.9 71.6 66.9 45.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 906 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 645 O
REMARK 620 2 TYR D 726 O 74.1
REMARK 620 3 ASP D 728 OD1 133.9 91.1
REMARK 620 4 ASP D 731 OD1 80.4 100.0 59.1
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 ACT A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT C 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 906
DBREF1 6MLY A 24 797 UNP A0A380YKU1_9BACE
DBREF2 6MLY A A0A380YKU1 24 797
DBREF1 6MLY B 24 797 UNP A0A380YKU1_9BACE
DBREF2 6MLY B A0A380YKU1 24 797
DBREF1 6MLY C 24 797 UNP A0A380YKU1_9BACE
DBREF2 6MLY C A0A380YKU1 24 797
DBREF1 6MLY D 24 797 UNP A0A380YKU1_9BACE
DBREF2 6MLY D A0A380YKU1 24 797
SEQADV 6MLY GLY A 7 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY SER A 8 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY HIS A 9 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY MET A 10 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ALA A 11 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY SER A 12 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY MET A 13 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY THR A 14 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLY A 15 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLY A 16 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLN A 17 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLN A 18 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY MET A 19 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLY A 20 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ARG A 21 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLY A 22 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY SER A 23 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY TYR A 798 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ARG A 799 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ASP A 800 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY LEU A 801 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ASN A 802 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ARG A 803 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ILE A 804 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ARG A 805 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY PRO A 806 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ILE A 807 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY LYS A 808 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY CYS A 809 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ASP A 810 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ASP A 811 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ILE A 812 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY LYS A 813 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLY B 7 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY SER B 8 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY HIS B 9 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY MET B 10 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ALA B 11 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY SER B 12 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY MET B 13 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY THR B 14 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLY B 15 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLY B 16 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLN B 17 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLN B 18 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY MET B 19 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLY B 20 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ARG B 21 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLY B 22 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY SER B 23 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY TYR B 798 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ARG B 799 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ASP B 800 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY LEU B 801 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ASN B 802 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ARG B 803 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ILE B 804 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ARG B 805 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY PRO B 806 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ILE B 807 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY LYS B 808 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY CYS B 809 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ASP B 810 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ASP B 811 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ILE B 812 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY LYS B 813 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLY C 7 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY SER C 8 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY HIS C 9 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY MET C 10 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ALA C 11 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY SER C 12 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY MET C 13 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY THR C 14 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLY C 15 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLY C 16 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLN C 17 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLN C 18 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY MET C 19 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLY C 20 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ARG C 21 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLY C 22 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY SER C 23 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY TYR C 798 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ARG C 799 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ASP C 800 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY LEU C 801 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ASN C 802 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ARG C 803 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ILE C 804 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ARG C 805 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY PRO C 806 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ILE C 807 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY LYS C 808 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY CYS C 809 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ASP C 810 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ASP C 811 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ILE C 812 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY LYS C 813 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLY D 7 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY SER D 8 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY HIS D 9 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY MET D 10 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ALA D 11 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY SER D 12 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY MET D 13 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY THR D 14 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLY D 15 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLY D 16 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLN D 17 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLN D 18 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY MET D 19 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLY D 20 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ARG D 21 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY GLY D 22 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY SER D 23 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY TYR D 798 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ARG D 799 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ASP D 800 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY LEU D 801 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ASN D 802 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ARG D 803 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ILE D 804 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ARG D 805 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY PRO D 806 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ILE D 807 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY LYS D 808 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY CYS D 809 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ASP D 810 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ASP D 811 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY ILE D 812 UNP A0A380YKU EXPRESSION TAG
SEQADV 6MLY LYS D 813 UNP A0A380YKU EXPRESSION TAG
SEQRES 1 A 807 GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET
SEQRES 2 A 807 GLY ARG GLY SER GLN LYS PRO ALA THR ASN PRO VAL ILE
SEQRES 3 A 807 TYR ALA ASP ALA PRO ASP MET SER MET LEU ARG VAL GLY
SEQRES 4 A 807 ASP THR TYR TYR MET SER SER THR THR MET HIS MET SER
SEQRES 5 A 807 PRO GLY VAL PRO ILE MET LYS SER ASN ASP LEU VAL ASN
SEQRES 6 A 807 TRP LYS LEU VAL ASN TYR ALA TYR ASP THR LEU ALA ASN
SEQRES 7 A 807 ILE PRO THR MET ASN LEU ASP ASP GLY LYS ASN THR TYR
SEQRES 8 A 807 GLY ARG GLY SER TRP ALA SER CYS LEU ARG TYR HIS GLU
SEQRES 9 A 807 GLY VAL TYR TYR LEU SER THR PHE ALA GLN THR THR GLY
SEQRES 10 A 807 LYS THR TYR PHE TYR THR THR LYS ASN LEU GLU LYS GLY
SEQRES 11 A 807 PRO TRP LYS CYS THR GLU PHE SER PRO ALA TYR HIS ASP
SEQRES 12 A 807 HIS SER PHE PHE PHE ASP GLU ASP GLY HIS ILE TYR MET
SEQRES 13 A 807 ILE TYR GLY ASN GLY LYS LEU PHE LEU ALA GLU LEU LYS
SEQRES 14 A 807 PRO ASP LEU SER GLY VAL LYS PRO GLY THR GLU ARG VAL
SEQRES 15 A 807 LEU ILE GLU ASN ALA SER ALA PRO ALA GLY ASP ASN ILE
SEQRES 16 A 807 MET LEU GLY ALA GLU GLY SER GLN LEU PHE LYS VAL ASN
SEQRES 17 A 807 GLY LYS TYR TYR LEU PHE ASN ILE THR TRP PRO ARG GLY
SEQRES 18 A 807 GLY VAL ARG THR VAL ILE VAL HIS ARG ALA ASP LYS ILE
SEQRES 19 A 807 THR GLY PRO TYR GLU GLY ARG VAL VAL PHE GLN ASP ARG
SEQRES 20 A 807 GLY ILE ALA GLN GLY GLY LEU VAL ASP THR PRO ASP GLY
SEQRES 21 A 807 ARG TRP PHE ALA TYR LEU PHE GLU ASP CYS GLY ALA VAL
SEQRES 22 A 807 GLY ARG ILE PRO TYR LEU VAL PRO VAL GLU TRP LYS ASP
SEQRES 23 A 807 GLY TRP PRO VAL LEU GLY VAL ASN GLY ARG ALA PRO ALA
SEQRES 24 A 807 LYS LEU GLU LEU PRO ASP SER ARG GLY LEU ILE PRO GLY
SEQRES 25 A 807 ILE VAL ALA SER ASP ASP PHE ASN ARG LYS LYS GLY GLU
SEQRES 26 A 807 ARG ALA LEU PRO LEU VAL TRP GLN TRP ASN HIS ASN PRO
SEQRES 27 A 807 ASP ASN ALA LEU TRP SER LEU SER ALA ARG LYS GLY TYR
SEQRES 28 A 807 LEU ARG LEU THR THR GLY ARG MET GLU THR SER PHE THR
SEQRES 29 A 807 GLN ALA LYS ASN ILE LEU THR GLN ARG THR ILE GLY PRO
SEQRES 30 A 807 VAL CYS THR GLY SER VAL SER MET ASP VAL SER GLY MET
SEQRES 31 A 807 LYS GLU GLY ASP PHE ALA GLY LEU SER LEU PHE GLN ARG
SEQRES 32 A 807 LYS TYR GLY GLN VAL GLY VAL LYS VAL THR ASP GLY LYS
SEQRES 33 A 807 LYS TYR ILE VAL MET VAL ASN GLY GLU ASN GLU THR PRO
SEQRES 34 A 807 ALA GLU VAL GLU LYS VAL PRO LEU ASN GLN GLN VAL VAL
SEQRES 35 A 807 TYR PHE LYS ALA GLU CYS ASP PHE ARG ASN LYS VAL ASP
SEQRES 36 A 807 LYS GLY TYR PHE TYR TYR SER LEU ASP GLY SER ASN TRP
SEQRES 37 A 807 LYS ALA ILE GLY ASN VAL LEU LYS MET GLN TYR THR MET
SEQRES 38 A 807 PRO HIS PHE MET GLY TYR ARG PHE ALA LEU PHE ASN TYR
SEQRES 39 A 807 ALA THR LYS GLU VAL GLY GLY TYR ALA ASP PHE ASP TYR
SEQRES 40 A 807 PHE LYS ILE GLU ASP LYS ILE SER ASP CYS ARG TRP GLU
SEQRES 41 A 807 ASP ILE CYS TYR ALA ASP ASP LYS LEU GLU GLY HIS LYS
SEQRES 42 A 807 LEU ASP ILE TYR LEU PRO ASP MET ASP GLU PRO SER TYR
SEQRES 43 A 807 LYS VAL VAL VAL LEU ILE TYR GLY SER ALA TRP PHE ALA
SEQRES 44 A 807 ASN ASN MET LYS GLN ALA ALA PHE GLN VAL PHE GLY LYS
SEQRES 45 A 807 SER LEU LEU ASP LYS GLY PHE ALA VAL VAL SER ILE ASN
SEQRES 46 A 807 HIS ARG SER SER GLY ASP ALA LYS PHE PRO ALA GLN ILE
SEQRES 47 A 807 ASN ASP VAL LYS ALA ALA ILE ARG PHE ILE ARG ALA ASN
SEQRES 48 A 807 ALA ALA LYS TYR LYS LEU ASP THR SER PHE ILE GLY ILE
SEQRES 49 A 807 THR GLY PHE SER SER GLY GLY HIS LEU ALA SER LEU ALA
SEQRES 50 A 807 GLY THR THR ASN GLY VAL LYS SER TYR THR ILE GLY ALA
SEQRES 51 A 807 LYS THR VAL ASP LEU GLU GLY ASN VAL GLY LEU TYR PRO
SEQRES 52 A 807 SER PHE SER SER ARG VAL ASP ALA VAL VAL ASN TRP PHE
SEQRES 53 A 807 GLY PRO ILE ASP MET THR ARG MET GLU ASN CYS ASN THR
SEQRES 54 A 807 THR LYS GLY ALA ASN SER PRO GLU ALA ALA LEU ILE GLY
SEQRES 55 A 807 GLY VAL PRO ALA ASP ASN LEU ASP MET LEU ALA LEU LEU
SEQRES 56 A 807 ASN PRO ILE THR TYR ILE ASP LYS ASN ASP PRO LYS PHE
SEQRES 57 A 807 ILE VAL ILE HIS GLY GLU ALA ASP THR VAL VAL PRO ASN
SEQRES 58 A 807 CYS GLN SER ILE PHE PHE SER GLU ALA LEU ARG ALA GLN
SEQRES 59 A 807 GLY ARG LEU GLU GLU PHE ILE SER VAL PRO GLY GLY GLN
SEQRES 60 A 807 HIS GLY PRO VAL THR PHE ASN GLU ASN THR LEU LYS LYS
SEQRES 61 A 807 MET ILE ASP PHE PHE ALA ARG GLU ALA GLY ILE TYR ARG
SEQRES 62 A 807 ASP LEU ASN ARG ILE ARG PRO ILE LYS CYS ASP ASP ILE
SEQRES 63 A 807 LYS
SEQRES 1 B 807 GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET
SEQRES 2 B 807 GLY ARG GLY SER GLN LYS PRO ALA THR ASN PRO VAL ILE
SEQRES 3 B 807 TYR ALA ASP ALA PRO ASP MET SER MET LEU ARG VAL GLY
SEQRES 4 B 807 ASP THR TYR TYR MET SER SER THR THR MET HIS MET SER
SEQRES 5 B 807 PRO GLY VAL PRO ILE MET LYS SER ASN ASP LEU VAL ASN
SEQRES 6 B 807 TRP LYS LEU VAL ASN TYR ALA TYR ASP THR LEU ALA ASN
SEQRES 7 B 807 ILE PRO THR MET ASN LEU ASP ASP GLY LYS ASN THR TYR
SEQRES 8 B 807 GLY ARG GLY SER TRP ALA SER CYS LEU ARG TYR HIS GLU
SEQRES 9 B 807 GLY VAL TYR TYR LEU SER THR PHE ALA GLN THR THR GLY
SEQRES 10 B 807 LYS THR TYR PHE TYR THR THR LYS ASN LEU GLU LYS GLY
SEQRES 11 B 807 PRO TRP LYS CYS THR GLU PHE SER PRO ALA TYR HIS ASP
SEQRES 12 B 807 HIS SER PHE PHE PHE ASP GLU ASP GLY HIS ILE TYR MET
SEQRES 13 B 807 ILE TYR GLY ASN GLY LYS LEU PHE LEU ALA GLU LEU LYS
SEQRES 14 B 807 PRO ASP LEU SER GLY VAL LYS PRO GLY THR GLU ARG VAL
SEQRES 15 B 807 LEU ILE GLU ASN ALA SER ALA PRO ALA GLY ASP ASN ILE
SEQRES 16 B 807 MET LEU GLY ALA GLU GLY SER GLN LEU PHE LYS VAL ASN
SEQRES 17 B 807 GLY LYS TYR TYR LEU PHE ASN ILE THR TRP PRO ARG GLY
SEQRES 18 B 807 GLY VAL ARG THR VAL ILE VAL HIS ARG ALA ASP LYS ILE
SEQRES 19 B 807 THR GLY PRO TYR GLU GLY ARG VAL VAL PHE GLN ASP ARG
SEQRES 20 B 807 GLY ILE ALA GLN GLY GLY LEU VAL ASP THR PRO ASP GLY
SEQRES 21 B 807 ARG TRP PHE ALA TYR LEU PHE GLU ASP CYS GLY ALA VAL
SEQRES 22 B 807 GLY ARG ILE PRO TYR LEU VAL PRO VAL GLU TRP LYS ASP
SEQRES 23 B 807 GLY TRP PRO VAL LEU GLY VAL ASN GLY ARG ALA PRO ALA
SEQRES 24 B 807 LYS LEU GLU LEU PRO ASP SER ARG GLY LEU ILE PRO GLY
SEQRES 25 B 807 ILE VAL ALA SER ASP ASP PHE ASN ARG LYS LYS GLY GLU
SEQRES 26 B 807 ARG ALA LEU PRO LEU VAL TRP GLN TRP ASN HIS ASN PRO
SEQRES 27 B 807 ASP ASN ALA LEU TRP SER LEU SER ALA ARG LYS GLY TYR
SEQRES 28 B 807 LEU ARG LEU THR THR GLY ARG MET GLU THR SER PHE THR
SEQRES 29 B 807 GLN ALA LYS ASN ILE LEU THR GLN ARG THR ILE GLY PRO
SEQRES 30 B 807 VAL CYS THR GLY SER VAL SER MET ASP VAL SER GLY MET
SEQRES 31 B 807 LYS GLU GLY ASP PHE ALA GLY LEU SER LEU PHE GLN ARG
SEQRES 32 B 807 LYS TYR GLY GLN VAL GLY VAL LYS VAL THR ASP GLY LYS
SEQRES 33 B 807 LYS TYR ILE VAL MET VAL ASN GLY GLU ASN GLU THR PRO
SEQRES 34 B 807 ALA GLU VAL GLU LYS VAL PRO LEU ASN GLN GLN VAL VAL
SEQRES 35 B 807 TYR PHE LYS ALA GLU CYS ASP PHE ARG ASN LYS VAL ASP
SEQRES 36 B 807 LYS GLY TYR PHE TYR TYR SER LEU ASP GLY SER ASN TRP
SEQRES 37 B 807 LYS ALA ILE GLY ASN VAL LEU LYS MET GLN TYR THR MET
SEQRES 38 B 807 PRO HIS PHE MET GLY TYR ARG PHE ALA LEU PHE ASN TYR
SEQRES 39 B 807 ALA THR LYS GLU VAL GLY GLY TYR ALA ASP PHE ASP TYR
SEQRES 40 B 807 PHE LYS ILE GLU ASP LYS ILE SER ASP CYS ARG TRP GLU
SEQRES 41 B 807 ASP ILE CYS TYR ALA ASP ASP LYS LEU GLU GLY HIS LYS
SEQRES 42 B 807 LEU ASP ILE TYR LEU PRO ASP MET ASP GLU PRO SER TYR
SEQRES 43 B 807 LYS VAL VAL VAL LEU ILE TYR GLY SER ALA TRP PHE ALA
SEQRES 44 B 807 ASN ASN MET LYS GLN ALA ALA PHE GLN VAL PHE GLY LYS
SEQRES 45 B 807 SER LEU LEU ASP LYS GLY PHE ALA VAL VAL SER ILE ASN
SEQRES 46 B 807 HIS ARG SER SER GLY ASP ALA LYS PHE PRO ALA GLN ILE
SEQRES 47 B 807 ASN ASP VAL LYS ALA ALA ILE ARG PHE ILE ARG ALA ASN
SEQRES 48 B 807 ALA ALA LYS TYR LYS LEU ASP THR SER PHE ILE GLY ILE
SEQRES 49 B 807 THR GLY PHE SER SER GLY GLY HIS LEU ALA SER LEU ALA
SEQRES 50 B 807 GLY THR THR ASN GLY VAL LYS SER TYR THR ILE GLY ALA
SEQRES 51 B 807 LYS THR VAL ASP LEU GLU GLY ASN VAL GLY LEU TYR PRO
SEQRES 52 B 807 SER PHE SER SER ARG VAL ASP ALA VAL VAL ASN TRP PHE
SEQRES 53 B 807 GLY PRO ILE ASP MET THR ARG MET GLU ASN CYS ASN THR
SEQRES 54 B 807 THR LYS GLY ALA ASN SER PRO GLU ALA ALA LEU ILE GLY
SEQRES 55 B 807 GLY VAL PRO ALA ASP ASN LEU ASP MET LEU ALA LEU LEU
SEQRES 56 B 807 ASN PRO ILE THR TYR ILE ASP LYS ASN ASP PRO LYS PHE
SEQRES 57 B 807 ILE VAL ILE HIS GLY GLU ALA ASP THR VAL VAL PRO ASN
SEQRES 58 B 807 CYS GLN SER ILE PHE PHE SER GLU ALA LEU ARG ALA GLN
SEQRES 59 B 807 GLY ARG LEU GLU GLU PHE ILE SER VAL PRO GLY GLY GLN
SEQRES 60 B 807 HIS GLY PRO VAL THR PHE ASN GLU ASN THR LEU LYS LYS
SEQRES 61 B 807 MET ILE ASP PHE PHE ALA ARG GLU ALA GLY ILE TYR ARG
SEQRES 62 B 807 ASP LEU ASN ARG ILE ARG PRO ILE LYS CYS ASP ASP ILE
SEQRES 63 B 807 LYS
SEQRES 1 C 807 GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET
SEQRES 2 C 807 GLY ARG GLY SER GLN LYS PRO ALA THR ASN PRO VAL ILE
SEQRES 3 C 807 TYR ALA ASP ALA PRO ASP MET SER MET LEU ARG VAL GLY
SEQRES 4 C 807 ASP THR TYR TYR MET SER SER THR THR MET HIS MET SER
SEQRES 5 C 807 PRO GLY VAL PRO ILE MET LYS SER ASN ASP LEU VAL ASN
SEQRES 6 C 807 TRP LYS LEU VAL ASN TYR ALA TYR ASP THR LEU ALA ASN
SEQRES 7 C 807 ILE PRO THR MET ASN LEU ASP ASP GLY LYS ASN THR TYR
SEQRES 8 C 807 GLY ARG GLY SER TRP ALA SER CYS LEU ARG TYR HIS GLU
SEQRES 9 C 807 GLY VAL TYR TYR LEU SER THR PHE ALA GLN THR THR GLY
SEQRES 10 C 807 LYS THR TYR PHE TYR THR THR LYS ASN LEU GLU LYS GLY
SEQRES 11 C 807 PRO TRP LYS CYS THR GLU PHE SER PRO ALA TYR HIS ASP
SEQRES 12 C 807 HIS SER PHE PHE PHE ASP GLU ASP GLY HIS ILE TYR MET
SEQRES 13 C 807 ILE TYR GLY ASN GLY LYS LEU PHE LEU ALA GLU LEU LYS
SEQRES 14 C 807 PRO ASP LEU SER GLY VAL LYS PRO GLY THR GLU ARG VAL
SEQRES 15 C 807 LEU ILE GLU ASN ALA SER ALA PRO ALA GLY ASP ASN ILE
SEQRES 16 C 807 MET LEU GLY ALA GLU GLY SER GLN LEU PHE LYS VAL ASN
SEQRES 17 C 807 GLY LYS TYR TYR LEU PHE ASN ILE THR TRP PRO ARG GLY
SEQRES 18 C 807 GLY VAL ARG THR VAL ILE VAL HIS ARG ALA ASP LYS ILE
SEQRES 19 C 807 THR GLY PRO TYR GLU GLY ARG VAL VAL PHE GLN ASP ARG
SEQRES 20 C 807 GLY ILE ALA GLN GLY GLY LEU VAL ASP THR PRO ASP GLY
SEQRES 21 C 807 ARG TRP PHE ALA TYR LEU PHE GLU ASP CYS GLY ALA VAL
SEQRES 22 C 807 GLY ARG ILE PRO TYR LEU VAL PRO VAL GLU TRP LYS ASP
SEQRES 23 C 807 GLY TRP PRO VAL LEU GLY VAL ASN GLY ARG ALA PRO ALA
SEQRES 24 C 807 LYS LEU GLU LEU PRO ASP SER ARG GLY LEU ILE PRO GLY
SEQRES 25 C 807 ILE VAL ALA SER ASP ASP PHE ASN ARG LYS LYS GLY GLU
SEQRES 26 C 807 ARG ALA LEU PRO LEU VAL TRP GLN TRP ASN HIS ASN PRO
SEQRES 27 C 807 ASP ASN ALA LEU TRP SER LEU SER ALA ARG LYS GLY TYR
SEQRES 28 C 807 LEU ARG LEU THR THR GLY ARG MET GLU THR SER PHE THR
SEQRES 29 C 807 GLN ALA LYS ASN ILE LEU THR GLN ARG THR ILE GLY PRO
SEQRES 30 C 807 VAL CYS THR GLY SER VAL SER MET ASP VAL SER GLY MET
SEQRES 31 C 807 LYS GLU GLY ASP PHE ALA GLY LEU SER LEU PHE GLN ARG
SEQRES 32 C 807 LYS TYR GLY GLN VAL GLY VAL LYS VAL THR ASP GLY LYS
SEQRES 33 C 807 LYS TYR ILE VAL MET VAL ASN GLY GLU ASN GLU THR PRO
SEQRES 34 C 807 ALA GLU VAL GLU LYS VAL PRO LEU ASN GLN GLN VAL VAL
SEQRES 35 C 807 TYR PHE LYS ALA GLU CYS ASP PHE ARG ASN LYS VAL ASP
SEQRES 36 C 807 LYS GLY TYR PHE TYR TYR SER LEU ASP GLY SER ASN TRP
SEQRES 37 C 807 LYS ALA ILE GLY ASN VAL LEU LYS MET GLN TYR THR MET
SEQRES 38 C 807 PRO HIS PHE MET GLY TYR ARG PHE ALA LEU PHE ASN TYR
SEQRES 39 C 807 ALA THR LYS GLU VAL GLY GLY TYR ALA ASP PHE ASP TYR
SEQRES 40 C 807 PHE LYS ILE GLU ASP LYS ILE SER ASP CYS ARG TRP GLU
SEQRES 41 C 807 ASP ILE CYS TYR ALA ASP ASP LYS LEU GLU GLY HIS LYS
SEQRES 42 C 807 LEU ASP ILE TYR LEU PRO ASP MET ASP GLU PRO SER TYR
SEQRES 43 C 807 LYS VAL VAL VAL LEU ILE TYR GLY SER ALA TRP PHE ALA
SEQRES 44 C 807 ASN ASN MET LYS GLN ALA ALA PHE GLN VAL PHE GLY LYS
SEQRES 45 C 807 SER LEU LEU ASP LYS GLY PHE ALA VAL VAL SER ILE ASN
SEQRES 46 C 807 HIS ARG SER SER GLY ASP ALA LYS PHE PRO ALA GLN ILE
SEQRES 47 C 807 ASN ASP VAL LYS ALA ALA ILE ARG PHE ILE ARG ALA ASN
SEQRES 48 C 807 ALA ALA LYS TYR LYS LEU ASP THR SER PHE ILE GLY ILE
SEQRES 49 C 807 THR GLY PHE SER SER GLY GLY HIS LEU ALA SER LEU ALA
SEQRES 50 C 807 GLY THR THR ASN GLY VAL LYS SER TYR THR ILE GLY ALA
SEQRES 51 C 807 LYS THR VAL ASP LEU GLU GLY ASN VAL GLY LEU TYR PRO
SEQRES 52 C 807 SER PHE SER SER ARG VAL ASP ALA VAL VAL ASN TRP PHE
SEQRES 53 C 807 GLY PRO ILE ASP MET THR ARG MET GLU ASN CYS ASN THR
SEQRES 54 C 807 THR LYS GLY ALA ASN SER PRO GLU ALA ALA LEU ILE GLY
SEQRES 55 C 807 GLY VAL PRO ALA ASP ASN LEU ASP MET LEU ALA LEU LEU
SEQRES 56 C 807 ASN PRO ILE THR TYR ILE ASP LYS ASN ASP PRO LYS PHE
SEQRES 57 C 807 ILE VAL ILE HIS GLY GLU ALA ASP THR VAL VAL PRO ASN
SEQRES 58 C 807 CYS GLN SER ILE PHE PHE SER GLU ALA LEU ARG ALA GLN
SEQRES 59 C 807 GLY ARG LEU GLU GLU PHE ILE SER VAL PRO GLY GLY GLN
SEQRES 60 C 807 HIS GLY PRO VAL THR PHE ASN GLU ASN THR LEU LYS LYS
SEQRES 61 C 807 MET ILE ASP PHE PHE ALA ARG GLU ALA GLY ILE TYR ARG
SEQRES 62 C 807 ASP LEU ASN ARG ILE ARG PRO ILE LYS CYS ASP ASP ILE
SEQRES 63 C 807 LYS
SEQRES 1 D 807 GLY SER HIS MET ALA SER MET THR GLY GLY GLN GLN MET
SEQRES 2 D 807 GLY ARG GLY SER GLN LYS PRO ALA THR ASN PRO VAL ILE
SEQRES 3 D 807 TYR ALA ASP ALA PRO ASP MET SER MET LEU ARG VAL GLY
SEQRES 4 D 807 ASP THR TYR TYR MET SER SER THR THR MET HIS MET SER
SEQRES 5 D 807 PRO GLY VAL PRO ILE MET LYS SER ASN ASP LEU VAL ASN
SEQRES 6 D 807 TRP LYS LEU VAL ASN TYR ALA TYR ASP THR LEU ALA ASN
SEQRES 7 D 807 ILE PRO THR MET ASN LEU ASP ASP GLY LYS ASN THR TYR
SEQRES 8 D 807 GLY ARG GLY SER TRP ALA SER CYS LEU ARG TYR HIS GLU
SEQRES 9 D 807 GLY VAL TYR TYR LEU SER THR PHE ALA GLN THR THR GLY
SEQRES 10 D 807 LYS THR TYR PHE TYR THR THR LYS ASN LEU GLU LYS GLY
SEQRES 11 D 807 PRO TRP LYS CYS THR GLU PHE SER PRO ALA TYR HIS ASP
SEQRES 12 D 807 HIS SER PHE PHE PHE ASP GLU ASP GLY HIS ILE TYR MET
SEQRES 13 D 807 ILE TYR GLY ASN GLY LYS LEU PHE LEU ALA GLU LEU LYS
SEQRES 14 D 807 PRO ASP LEU SER GLY VAL LYS PRO GLY THR GLU ARG VAL
SEQRES 15 D 807 LEU ILE GLU ASN ALA SER ALA PRO ALA GLY ASP ASN ILE
SEQRES 16 D 807 MET LEU GLY ALA GLU GLY SER GLN LEU PHE LYS VAL ASN
SEQRES 17 D 807 GLY LYS TYR TYR LEU PHE ASN ILE THR TRP PRO ARG GLY
SEQRES 18 D 807 GLY VAL ARG THR VAL ILE VAL HIS ARG ALA ASP LYS ILE
SEQRES 19 D 807 THR GLY PRO TYR GLU GLY ARG VAL VAL PHE GLN ASP ARG
SEQRES 20 D 807 GLY ILE ALA GLN GLY GLY LEU VAL ASP THR PRO ASP GLY
SEQRES 21 D 807 ARG TRP PHE ALA TYR LEU PHE GLU ASP CYS GLY ALA VAL
SEQRES 22 D 807 GLY ARG ILE PRO TYR LEU VAL PRO VAL GLU TRP LYS ASP
SEQRES 23 D 807 GLY TRP PRO VAL LEU GLY VAL ASN GLY ARG ALA PRO ALA
SEQRES 24 D 807 LYS LEU GLU LEU PRO ASP SER ARG GLY LEU ILE PRO GLY
SEQRES 25 D 807 ILE VAL ALA SER ASP ASP PHE ASN ARG LYS LYS GLY GLU
SEQRES 26 D 807 ARG ALA LEU PRO LEU VAL TRP GLN TRP ASN HIS ASN PRO
SEQRES 27 D 807 ASP ASN ALA LEU TRP SER LEU SER ALA ARG LYS GLY TYR
SEQRES 28 D 807 LEU ARG LEU THR THR GLY ARG MET GLU THR SER PHE THR
SEQRES 29 D 807 GLN ALA LYS ASN ILE LEU THR GLN ARG THR ILE GLY PRO
SEQRES 30 D 807 VAL CYS THR GLY SER VAL SER MET ASP VAL SER GLY MET
SEQRES 31 D 807 LYS GLU GLY ASP PHE ALA GLY LEU SER LEU PHE GLN ARG
SEQRES 32 D 807 LYS TYR GLY GLN VAL GLY VAL LYS VAL THR ASP GLY LYS
SEQRES 33 D 807 LYS TYR ILE VAL MET VAL ASN GLY GLU ASN GLU THR PRO
SEQRES 34 D 807 ALA GLU VAL GLU LYS VAL PRO LEU ASN GLN GLN VAL VAL
SEQRES 35 D 807 TYR PHE LYS ALA GLU CYS ASP PHE ARG ASN LYS VAL ASP
SEQRES 36 D 807 LYS GLY TYR PHE TYR TYR SER LEU ASP GLY SER ASN TRP
SEQRES 37 D 807 LYS ALA ILE GLY ASN VAL LEU LYS MET GLN TYR THR MET
SEQRES 38 D 807 PRO HIS PHE MET GLY TYR ARG PHE ALA LEU PHE ASN TYR
SEQRES 39 D 807 ALA THR LYS GLU VAL GLY GLY TYR ALA ASP PHE ASP TYR
SEQRES 40 D 807 PHE LYS ILE GLU ASP LYS ILE SER ASP CYS ARG TRP GLU
SEQRES 41 D 807 ASP ILE CYS TYR ALA ASP ASP LYS LEU GLU GLY HIS LYS
SEQRES 42 D 807 LEU ASP ILE TYR LEU PRO ASP MET ASP GLU PRO SER TYR
SEQRES 43 D 807 LYS VAL VAL VAL LEU ILE TYR GLY SER ALA TRP PHE ALA
SEQRES 44 D 807 ASN ASN MET LYS GLN ALA ALA PHE GLN VAL PHE GLY LYS
SEQRES 45 D 807 SER LEU LEU ASP LYS GLY PHE ALA VAL VAL SER ILE ASN
SEQRES 46 D 807 HIS ARG SER SER GLY ASP ALA LYS PHE PRO ALA GLN ILE
SEQRES 47 D 807 ASN ASP VAL LYS ALA ALA ILE ARG PHE ILE ARG ALA ASN
SEQRES 48 D 807 ALA ALA LYS TYR LYS LEU ASP THR SER PHE ILE GLY ILE
SEQRES 49 D 807 THR GLY PHE SER SER GLY GLY HIS LEU ALA SER LEU ALA
SEQRES 50 D 807 GLY THR THR ASN GLY VAL LYS SER TYR THR ILE GLY ALA
SEQRES 51 D 807 LYS THR VAL ASP LEU GLU GLY ASN VAL GLY LEU TYR PRO
SEQRES 52 D 807 SER PHE SER SER ARG VAL ASP ALA VAL VAL ASN TRP PHE
SEQRES 53 D 807 GLY PRO ILE ASP MET THR ARG MET GLU ASN CYS ASN THR
SEQRES 54 D 807 THR LYS GLY ALA ASN SER PRO GLU ALA ALA LEU ILE GLY
SEQRES 55 D 807 GLY VAL PRO ALA ASP ASN LEU ASP MET LEU ALA LEU LEU
SEQRES 56 D 807 ASN PRO ILE THR TYR ILE ASP LYS ASN ASP PRO LYS PHE
SEQRES 57 D 807 ILE VAL ILE HIS GLY GLU ALA ASP THR VAL VAL PRO ASN
SEQRES 58 D 807 CYS GLN SER ILE PHE PHE SER GLU ALA LEU ARG ALA GLN
SEQRES 59 D 807 GLY ARG LEU GLU GLU PHE ILE SER VAL PRO GLY GLY GLN
SEQRES 60 D 807 HIS GLY PRO VAL THR PHE ASN GLU ASN THR LEU LYS LYS
SEQRES 61 D 807 MET ILE ASP PHE PHE ALA ARG GLU ALA GLY ILE TYR ARG
SEQRES 62 D 807 ASP LEU ASN ARG ILE ARG PRO ILE LYS CYS ASP ASP ILE
SEQRES 63 D 807 LYS
HET ACT A 901 4
HET EDO A 902 4
HET EDO A 903 4
HET NA A 904 1
HET ACT B 901 4
HET EDO B 902 4
HET NA B 903 1
HET ACT C 901 4
HET EDO C 902 4
HET EDO C 903 4
HET NA C 904 1
HET ACT D 901 4
HET EDO D 902 4
HET EDO D 903 4
HET EDO D 904 4
HET EDO D 905 4
HET NA D 906 1
HETNAM ACT ACETATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NA SODIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 ACT 4(C2 H3 O2 1-)
FORMUL 6 EDO 9(C2 H6 O2)
FORMUL 8 NA 4(NA 1+)
FORMUL 22 HOH *396(H2 O)
HELIX 1 AA1 ILE A 85 LEU A 90 1 6
HELIX 2 AA2 ARG A 457 VAL A 460 5 4
HELIX 3 AA3 LEU A 535 GLY A 537 5 3
HELIX 4 AA4 MET A 568 PHE A 576 1 9
HELIX 5 AA5 PHE A 576 GLY A 584 1 9
HELIX 6 AA6 PRO A 601 ASN A 617 1 17
HELIX 7 AA7 SER A 634 THR A 646 1 13
HELIX 8 AA8 ASP A 686 MET A 690 5 5
HELIX 9 AA9 SER A 701 GLY A 708 1 8
HELIX 10 AB1 VAL A 710 ASP A 713 5 4
HELIX 11 AB2 ASN A 714 LEU A 721 1 8
HELIX 12 AB3 ASN A 722 ILE A 727 5 6
HELIX 13 AB4 PRO A 746 ALA A 759 1 14
HELIX 14 AB5 ASN A 780 GLY A 796 1 17
HELIX 15 AB6 ILE B 85 LEU B 90 1 6
HELIX 16 AB7 SER B 194 GLY B 198 5 5
HELIX 17 AB8 GLY B 277 VAL B 279 5 3
HELIX 18 AB9 VAL B 299 ARG B 302 5 4
HELIX 19 AC1 SER B 368 ALA B 372 5 5
HELIX 20 AC2 ARG B 457 VAL B 460 5 4
HELIX 21 AC3 LEU B 535 GLY B 537 5 3
HELIX 22 AC4 MET B 568 GLY B 584 1 17
HELIX 23 AC5 PRO B 601 ASN B 617 1 17
HELIX 24 AC6 ALA B 618 TYR B 621 5 4
HELIX 25 AC7 SER B 634 THR B 646 1 13
HELIX 26 AC8 ASP B 686 MET B 690 5 5
HELIX 27 AC9 SER B 701 GLY B 708 1 8
HELIX 28 AD1 VAL B 710 ASP B 713 5 4
HELIX 29 AD2 ASN B 714 LEU B 721 1 8
HELIX 30 AD3 ASN B 722 ILE B 727 5 6
HELIX 31 AD4 ASN B 747 ALA B 759 1 13
HELIX 32 AD5 ASN B 780 GLY B 796 1 17
HELIX 33 AD6 SER C 194 GLY C 198 5 5
HELIX 34 AD7 GLY C 277 VAL C 279 5 3
HELIX 35 AD8 VAL C 299 ARG C 302 5 4
HELIX 36 AD9 ASP C 345 ALA C 347 5 3
HELIX 37 AE1 ARG C 457 VAL C 460 5 4
HELIX 38 AE2 LEU C 535 GLY C 537 5 3
HELIX 39 AE3 MET C 568 LYS C 583 1 16
HELIX 40 AE4 PRO C 601 ASN C 617 1 17
HELIX 41 AE5 SER C 634 THR C 646 1 13
HELIX 42 AE6 ASP C 686 MET C 690 5 5
HELIX 43 AE7 SER C 701 GLY C 708 1 8
HELIX 44 AE8 ASN C 714 LEU C 721 1 8
HELIX 45 AE9 ASN C 722 ILE C 727 5 6
HELIX 46 AF1 ASN C 747 ALA C 759 1 13
HELIX 47 AF2 ASN C 780 ALA C 795 1 16
HELIX 48 AF3 ILE D 85 LEU D 90 1 6
HELIX 49 AF4 SER D 194 GLY D 198 5 5
HELIX 50 AF5 GLY D 277 VAL D 279 5 3
HELIX 51 AF6 VAL D 299 ARG D 302 5 4
HELIX 52 AF7 ASP D 345 ALA D 347 5 3
HELIX 53 AF8 SER D 368 ALA D 372 5 5
HELIX 54 AF9 ARG D 457 VAL D 460 5 4
HELIX 55 AG1 LEU D 535 GLY D 537 5 3
HELIX 56 AG2 MET D 568 GLY D 584 1 17
HELIX 57 AG3 PRO D 601 ASN D 617 1 17
HELIX 58 AG4 SER D 634 THR D 646 1 13
HELIX 59 AG5 ASP D 686 MET D 690 5 5
HELIX 60 AG6 SER D 701 ILE D 707 1 7
HELIX 61 AG7 ASN D 714 LEU D 721 1 8
HELIX 62 AG8 ASN D 722 ILE D 727 5 6
HELIX 63 AG9 ASN D 747 GLN D 760 1 14
HELIX 64 AH1 ASN D 780 GLY D 796 1 17
SHEET 1 AA1 4 SER A 40 VAL A 44 0
SHEET 2 AA1 4 THR A 47 SER A 51 -1 O TYR A 49 N LEU A 42
SHEET 3 AA1 4 GLY A 60 SER A 66 -1 O MET A 64 N MET A 50
SHEET 4 AA1 4 TRP A 72 TYR A 79 -1 O ASN A 76 N ILE A 63
SHEET 1 AA2 8 MET A 57 SER A 58 0
SHEET 2 AA2 8 GLN A 339 ASN A 341 -1 O TRP A 340 N SER A 58
SHEET 3 AA2 8 LEU A 376 ARG A 379 -1 O THR A 377 N GLN A 339
SHEET 4 AA2 8 ARG A 494 LEU A 497 -1 O LEU A 497 N LEU A 376
SHEET 5 AA2 8 PHE A 401 PHE A 407 -1 N PHE A 407 O ARG A 494
SHEET 6 AA2 8 GLY A 412 LYS A 417 -1 O VAL A 414 N LEU A 404
SHEET 7 AA2 8 TYR A 424 ASN A 429 -1 O VAL A 426 N GLY A 415
SHEET 8 AA2 8 ALA A 436 PRO A 442 -1 O VAL A 441 N ILE A 425
SHEET 1 AA3 4 CYS A 105 HIS A 109 0
SHEET 2 AA3 4 VAL A 112 ALA A 119 -1 O TYR A 114 N ARG A 107
SHEET 3 AA3 4 LYS A 124 THR A 130 -1 O TYR A 126 N THR A 117
SHEET 4 AA3 4 LYS A 139 PHE A 143 -1 O PHE A 143 N THR A 125
SHEET 1 AA4 3 SER A 151 PHE A 154 0
SHEET 2 AA4 3 ILE A 160 TYR A 164 -1 O ILE A 163 N SER A 151
SHEET 3 AA4 3 PHE A 170 GLU A 173 -1 O PHE A 170 N TYR A 164
SHEET 1 AA5 3 GLN A 209 VAL A 213 0
SHEET 2 AA5 3 LYS A 216 PHE A 220 -1 O TYR A 218 N PHE A 211
SHEET 3 AA5 3 HIS A 235 ALA A 237 -1 O ALA A 237 N TYR A 217
SHEET 1 AA6 3 ALA A 256 ASP A 262 0
SHEET 2 AA6 3 TRP A 268 ASP A 275 -1 O PHE A 269 N VAL A 261
SHEET 3 AA6 3 ARG A 281 VAL A 288 -1 O TYR A 284 N LEU A 272
SHEET 1 AA7 7 TRP A 349 SER A 350 0
SHEET 2 AA7 7 LEU A 358 THR A 361 -1 O ARG A 359 N SER A 350
SHEET 3 AA7 7 TYR A 508 GLU A 517 -1 O PHE A 511 N LEU A 358
SHEET 4 AA7 7 VAL A 384 ASP A 392 -1 N SER A 390 O ASP A 512
SHEET 5 AA7 7 VAL A 447 ASP A 455 -1 O VAL A 448 N MET A 391
SHEET 6 AA7 7 LYS A 462 SER A 468 -1 O SER A 468 N TYR A 449
SHEET 7 AA7 7 LYS A 475 ALA A 476 -1 O LYS A 475 N TYR A 467
SHEET 1 AA8 7 TRP A 349 SER A 350 0
SHEET 2 AA8 7 LEU A 358 THR A 361 -1 O ARG A 359 N SER A 350
SHEET 3 AA8 7 TYR A 508 GLU A 517 -1 O PHE A 511 N LEU A 358
SHEET 4 AA8 7 VAL A 384 ASP A 392 -1 N SER A 390 O ASP A 512
SHEET 5 AA8 7 VAL A 447 ASP A 455 -1 O VAL A 448 N MET A 391
SHEET 6 AA8 7 LYS A 462 SER A 468 -1 O SER A 468 N TYR A 449
SHEET 7 AA8 7 LEU A 481 LYS A 482 -1 O LEU A 481 N GLY A 463
SHEET 1 AA9 8 ARG A 524 CYS A 529 0
SHEET 2 AA9 8 LYS A 539 TYR A 543 -1 O ILE A 542 N TRP A 525
SHEET 3 AA9 8 PHE A 585 ILE A 590 -1 O VAL A 587 N TYR A 543
SHEET 4 AA9 8 TYR A 552 ILE A 558 1 N LYS A 553 O ALA A 586
SHEET 5 AA9 8 LEU A 623 PHE A 633 1 O ASP A 624 N TYR A 552
SHEET 6 AA9 8 ALA A 677 TRP A 681 1 O TRP A 681 N GLY A 632
SHEET 7 AA9 8 LYS A 733 GLY A 739 1 O ILE A 737 N ASN A 680
SHEET 8 AA9 8 LEU A 763 VAL A 769 1 O GLU A 764 N PHE A 734
SHEET 1 AB1 2 SER A 651 ILE A 654 0
SHEET 2 AB1 2 LYS A 657 ASP A 660 -1 O VAL A 659 N TYR A 652
SHEET 1 AB2 4 SER B 40 VAL B 44 0
SHEET 2 AB2 4 THR B 47 SER B 51 -1 O TYR B 49 N LEU B 42
SHEET 3 AB2 4 GLY B 60 SER B 66 -1 O MET B 64 N MET B 50
SHEET 4 AB2 4 TRP B 72 TYR B 79 -1 O ASN B 76 N ILE B 63
SHEET 1 AB3 8 MET B 57 SER B 58 0
SHEET 2 AB3 8 GLN B 339 ASN B 341 -1 O TRP B 340 N SER B 58
SHEET 3 AB3 8 LEU B 376 ARG B 379 -1 O THR B 377 N GLN B 339
SHEET 4 AB3 8 ARG B 494 ALA B 501 -1 O LEU B 497 N LEU B 376
SHEET 5 AB3 8 ASP B 400 PHE B 407 -1 N PHE B 407 O ARG B 494
SHEET 6 AB3 8 GLY B 412 VAL B 418 -1 O VAL B 416 N ALA B 402
SHEET 7 AB3 8 LYS B 423 ASN B 429 -1 O VAL B 426 N GLY B 415
SHEET 8 AB3 8 ALA B 436 LEU B 443 -1 O LEU B 443 N LYS B 423
SHEET 1 AB4 4 CYS B 105 HIS B 109 0
SHEET 2 AB4 4 VAL B 112 ALA B 119 -1 O TYR B 114 N ARG B 107
SHEET 3 AB4 4 LYS B 124 THR B 130 -1 O TYR B 128 N LEU B 115
SHEET 4 AB4 4 LYS B 139 PHE B 143 -1 O THR B 141 N PHE B 127
SHEET 1 AB5 4 SER B 151 PHE B 154 0
SHEET 2 AB5 4 ILE B 160 GLY B 165 -1 O ILE B 163 N SER B 151
SHEET 3 AB5 4 LEU B 169 LEU B 174 -1 O PHE B 170 N TYR B 164
SHEET 4 AB5 4 ARG B 187 ILE B 190 -1 O ARG B 187 N LEU B 171
SHEET 1 AB6 4 ILE B 201 VAL B 213 0
SHEET 2 AB6 4 LYS B 216 PRO B 225 -1 O TYR B 218 N PHE B 211
SHEET 3 AB6 4 THR B 231 ALA B 237 -1 O THR B 231 N THR B 223
SHEET 4 AB6 4 GLU B 245 PHE B 250 -1 O PHE B 250 N VAL B 232
SHEET 1 AB7 4 ALA B 256 ASP B 262 0
SHEET 2 AB7 4 TRP B 268 ASP B 275 -1 O TYR B 271 N GLY B 259
SHEET 3 AB7 4 ARG B 281 TRP B 290 -1 O VAL B 286 N ALA B 270
SHEET 4 AB7 4 PRO B 295 LEU B 297 -1 O VAL B 296 N GLU B 289
SHEET 1 AB8 7 TRP B 349 SER B 350 0
SHEET 2 AB8 7 LEU B 358 THR B 361 -1 O ARG B 359 N SER B 350
SHEET 3 AB8 7 TYR B 508 GLU B 517 -1 O PHE B 511 N LEU B 358
SHEET 4 AB8 7 VAL B 384 ASP B 392 -1 N SER B 388 O LYS B 515
SHEET 5 AB8 7 VAL B 447 ASP B 455 -1 O CYS B 454 N CYS B 385
SHEET 6 AB8 7 LYS B 462 SER B 468 -1 O SER B 468 N TYR B 449
SHEET 7 AB8 7 LYS B 475 ALA B 476 -1 O LYS B 475 N TYR B 467
SHEET 1 AB9 7 TRP B 349 SER B 350 0
SHEET 2 AB9 7 LEU B 358 THR B 361 -1 O ARG B 359 N SER B 350
SHEET 3 AB9 7 TYR B 508 GLU B 517 -1 O PHE B 511 N LEU B 358
SHEET 4 AB9 7 VAL B 384 ASP B 392 -1 N SER B 388 O LYS B 515
SHEET 5 AB9 7 VAL B 447 ASP B 455 -1 O CYS B 454 N CYS B 385
SHEET 6 AB9 7 LYS B 462 SER B 468 -1 O SER B 468 N TYR B 449
SHEET 7 AB9 7 LEU B 481 LYS B 482 -1 O LEU B 481 N GLY B 463
SHEET 1 AC1 8 ARG B 524 CYS B 529 0
SHEET 2 AC1 8 LYS B 539 TYR B 543 -1 O ILE B 542 N TRP B 525
SHEET 3 AC1 8 ALA B 586 ILE B 590 -1 O VAL B 587 N TYR B 543
SHEET 4 AC1 8 TYR B 552 ILE B 558 1 N LEU B 557 O ILE B 590
SHEET 5 AC1 8 LEU B 623 PHE B 633 1 O GLY B 629 N VAL B 554
SHEET 6 AC1 8 ALA B 677 TRP B 681 1 O TRP B 681 N GLY B 632
SHEET 7 AC1 8 LYS B 733 GLY B 739 1 O ILE B 737 N ASN B 680
SHEET 8 AC1 8 LEU B 763 VAL B 769 1 O GLU B 764 N PHE B 734
SHEET 1 AC2 2 SER B 651 ILE B 654 0
SHEET 2 AC2 2 LYS B 657 ASP B 660 -1 O LYS B 657 N ILE B 654
SHEET 1 AC3 4 SER C 40 VAL C 44 0
SHEET 2 AC3 4 THR C 47 SER C 51 -1 O TYR C 49 N LEU C 42
SHEET 3 AC3 4 GLY C 60 SER C 66 -1 O SER C 66 N TYR C 48
SHEET 4 AC3 4 TRP C 72 TYR C 79 -1 O LYS C 73 N LYS C 65
SHEET 1 AC4 8 MET C 57 SER C 58 0
SHEET 2 AC4 8 GLN C 339 ASN C 341 -1 O TRP C 340 N SER C 58
SHEET 3 AC4 8 LEU C 376 ARG C 379 -1 O THR C 377 N GLN C 339
SHEET 4 AC4 8 ARG C 494 ALA C 501 -1 O LEU C 497 N LEU C 376
SHEET 5 AC4 8 ASP C 400 PHE C 407 -1 N PHE C 407 O ARG C 494
SHEET 6 AC4 8 GLY C 412 THR C 419 -1 O VAL C 414 N LEU C 404
SHEET 7 AC4 8 LYS C 422 ASN C 429 -1 O VAL C 426 N GLY C 415
SHEET 8 AC4 8 ALA C 436 PRO C 442 -1 O VAL C 441 N ILE C 425
SHEET 1 AC5 4 CYS C 105 HIS C 109 0
SHEET 2 AC5 4 VAL C 112 ALA C 119 -1 O TYR C 114 N ARG C 107
SHEET 3 AC5 4 LYS C 124 THR C 130 -1 O TYR C 128 N LEU C 115
SHEET 4 AC5 4 LYS C 139 PHE C 143 -1 O THR C 141 N PHE C 127
SHEET 1 AC6 4 SER C 151 PHE C 154 0
SHEET 2 AC6 4 ILE C 160 GLY C 165 -1 O TYR C 161 N PHE C 153
SHEET 3 AC6 4 LEU C 169 LEU C 174 -1 O PHE C 170 N TYR C 164
SHEET 4 AC6 4 ARG C 187 ILE C 190 -1 O ARG C 187 N LEU C 171
SHEET 1 AC7 4 ILE C 201 VAL C 213 0
SHEET 2 AC7 4 LYS C 216 PRO C 225 -1 O TYR C 218 N PHE C 211
SHEET 3 AC7 4 THR C 231 ALA C 237 -1 O THR C 231 N THR C 223
SHEET 4 AC7 4 GLU C 245 PHE C 250 -1 O GLU C 245 N ARG C 236
SHEET 1 AC8 4 ALA C 256 ASP C 262 0
SHEET 2 AC8 4 TRP C 268 ASP C 275 -1 O PHE C 269 N VAL C 261
SHEET 3 AC8 4 ARG C 281 TRP C 290 -1 O TYR C 284 N LEU C 272
SHEET 4 AC8 4 PRO C 295 LEU C 297 -1 O VAL C 296 N GLU C 289
SHEET 1 AC9 7 TRP C 349 SER C 350 0
SHEET 2 AC9 7 LEU C 358 THR C 361 -1 O ARG C 359 N SER C 350
SHEET 3 AC9 7 TYR C 508 GLU C 517 -1 O PHE C 511 N LEU C 358
SHEET 4 AC9 7 VAL C 384 ASP C 392 -1 N SER C 390 O ASP C 512
SHEET 5 AC9 7 VAL C 447 ASP C 455 -1 O ALA C 452 N GLY C 387
SHEET 6 AC9 7 LYS C 462 SER C 468 -1 O LYS C 462 N ASP C 455
SHEET 7 AC9 7 LYS C 475 ALA C 476 -1 O LYS C 475 N TYR C 467
SHEET 1 AD1 7 TRP C 349 SER C 350 0
SHEET 2 AD1 7 LEU C 358 THR C 361 -1 O ARG C 359 N SER C 350
SHEET 3 AD1 7 TYR C 508 GLU C 517 -1 O PHE C 511 N LEU C 358
SHEET 4 AD1 7 VAL C 384 ASP C 392 -1 N SER C 390 O ASP C 512
SHEET 5 AD1 7 VAL C 447 ASP C 455 -1 O ALA C 452 N GLY C 387
SHEET 6 AD1 7 LYS C 462 SER C 468 -1 O LYS C 462 N ASP C 455
SHEET 7 AD1 7 LEU C 481 LYS C 482 -1 O LEU C 481 N GLY C 463
SHEET 1 AD2 8 ARG C 524 CYS C 529 0
SHEET 2 AD2 8 LYS C 539 TYR C 543 -1 O ILE C 542 N TRP C 525
SHEET 3 AD2 8 ALA C 586 ILE C 590 -1 O SER C 589 N ASP C 541
SHEET 4 AD2 8 TYR C 552 ILE C 558 1 N LYS C 553 O ALA C 586
SHEET 5 AD2 8 LEU C 623 PHE C 633 1 O ASP C 624 N TYR C 552
SHEET 6 AD2 8 ALA C 677 TRP C 681 1 O TRP C 681 N GLY C 632
SHEET 7 AD2 8 LYS C 733 GLY C 739 1 O ILE C 735 N ASN C 680
SHEET 8 AD2 8 LEU C 763 VAL C 769 1 O GLU C 764 N PHE C 734
SHEET 1 AD3 2 SER C 651 ILE C 654 0
SHEET 2 AD3 2 LYS C 657 ASP C 660 -1 O VAL C 659 N TYR C 652
SHEET 1 AD4 4 SER D 40 VAL D 44 0
SHEET 2 AD4 4 THR D 47 SER D 51 -1 O THR D 47 N VAL D 44
SHEET 3 AD4 4 GLY D 60 SER D 66 -1 O MET D 64 N MET D 50
SHEET 4 AD4 4 TRP D 72 TYR D 79 -1 O ASN D 76 N ILE D 63
SHEET 1 AD5 8 MET D 57 SER D 58 0
SHEET 2 AD5 8 GLN D 339 ASN D 341 -1 O TRP D 340 N SER D 58
SHEET 3 AD5 8 LEU D 376 ARG D 379 -1 O THR D 377 N GLN D 339
SHEET 4 AD5 8 ARG D 494 ALA D 501 -1 O LEU D 497 N LEU D 376
SHEET 5 AD5 8 ASP D 400 PHE D 407 -1 N SER D 405 O ALA D 496
SHEET 6 AD5 8 GLY D 412 THR D 419 -1 O GLY D 412 N LEU D 406
SHEET 7 AD5 8 LYS D 422 ASN D 429 -1 O VAL D 426 N GLY D 415
SHEET 8 AD5 8 ALA D 436 LEU D 443 -1 O VAL D 441 N ILE D 425
SHEET 1 AD6 4 CYS D 105 HIS D 109 0
SHEET 2 AD6 4 VAL D 112 ALA D 119 -1 O TYR D 114 N ARG D 107
SHEET 3 AD6 4 LYS D 124 THR D 130 -1 O TYR D 126 N THR D 117
SHEET 4 AD6 4 LYS D 139 PHE D 143 -1 O PHE D 143 N THR D 125
SHEET 1 AD7 4 SER D 151 PHE D 154 0
SHEET 2 AD7 4 ILE D 160 GLY D 165 -1 O ILE D 163 N SER D 151
SHEET 3 AD7 4 LEU D 169 LEU D 174 -1 O LEU D 174 N ILE D 160
SHEET 4 AD7 4 ARG D 187 ILE D 190 -1 O ARG D 187 N LEU D 171
SHEET 1 AD8 4 ILE D 201 VAL D 213 0
SHEET 2 AD8 4 LYS D 216 PRO D 225 -1 O TYR D 218 N PHE D 211
SHEET 3 AD8 4 THR D 231 ALA D 237 -1 O THR D 231 N THR D 223
SHEET 4 AD8 4 GLU D 245 PHE D 250 -1 O PHE D 250 N VAL D 232
SHEET 1 AD9 4 ALA D 256 ASP D 262 0
SHEET 2 AD9 4 TRP D 268 CYS D 276 -1 O PHE D 269 N VAL D 261
SHEET 3 AD9 4 GLY D 280 TRP D 290 -1 O TYR D 284 N LEU D 272
SHEET 4 AD9 4 PRO D 295 LEU D 297 -1 O VAL D 296 N GLU D 289
SHEET 1 AE1 7 TRP D 349 SER D 350 0
SHEET 2 AE1 7 LEU D 358 THR D 361 -1 O ARG D 359 N SER D 350
SHEET 3 AE1 7 TYR D 508 GLU D 517 -1 O PHE D 511 N LEU D 358
SHEET 4 AE1 7 VAL D 384 ASP D 392 -1 N SER D 388 O LYS D 515
SHEET 5 AE1 7 VAL D 447 ASP D 455 -1 O ALA D 452 N GLY D 387
SHEET 6 AE1 7 LYS D 462 SER D 468 -1 O LYS D 462 N ASP D 455
SHEET 7 AE1 7 LYS D 475 ALA D 476 -1 O LYS D 475 N TYR D 467
SHEET 1 AE2 7 TRP D 349 SER D 350 0
SHEET 2 AE2 7 LEU D 358 THR D 361 -1 O ARG D 359 N SER D 350
SHEET 3 AE2 7 TYR D 508 GLU D 517 -1 O PHE D 511 N LEU D 358
SHEET 4 AE2 7 VAL D 384 ASP D 392 -1 N SER D 388 O LYS D 515
SHEET 5 AE2 7 VAL D 447 ASP D 455 -1 O ALA D 452 N GLY D 387
SHEET 6 AE2 7 LYS D 462 SER D 468 -1 O LYS D 462 N ASP D 455
SHEET 7 AE2 7 LEU D 481 LYS D 482 -1 O LEU D 481 N GLY D 463
SHEET 1 AE3 8 ARG D 524 CYS D 529 0
SHEET 2 AE3 8 LYS D 539 TYR D 543 -1 O LEU D 540 N ILE D 528
SHEET 3 AE3 8 ALA D 586 ILE D 590 -1 O VAL D 587 N TYR D 543
SHEET 4 AE3 8 TYR D 552 ILE D 558 1 N LYS D 553 O ALA D 586
SHEET 5 AE3 8 LEU D 623 PHE D 633 1 O ASP D 624 N TYR D 552
SHEET 6 AE3 8 ALA D 677 TRP D 681 1 O TRP D 681 N GLY D 632
SHEET 7 AE3 8 LYS D 733 GLY D 739 1 O ILE D 737 N ASN D 680
SHEET 8 AE3 8 LEU D 763 VAL D 769 1 O GLU D 764 N PHE D 734
SHEET 1 AE4 2 SER D 651 ILE D 654 0
SHEET 2 AE4 2 LYS D 657 ASP D 660 -1 O VAL D 659 N TYR D 652
SSBOND 1 CYS A 693 CYS A 748 1555 1555 2.08
SSBOND 2 CYS B 693 CYS B 748 1555 1555 2.07
SSBOND 3 CYS D 693 CYS D 748 1555 1555 2.09
LINK O THR A 645 NA NA A 904 1555 1555 2.42
LINK O TYR A 726 NA NA A 904 1555 1555 2.26
LINK OD1 ASP A 728 NA NA A 904 1555 1555 2.48
LINK OD1 ASP A 731 NA NA A 904 1555 1555 2.76
LINK OD2 ASP A 731 NA NA A 904 1555 1555 2.90
LINK O THR B 645 NA NA B 903 1555 1555 2.49
LINK O TYR B 726 NA NA B 903 1555 1555 2.49
LINK OD1 ASP B 728 NA NA B 903 1555 1555 2.36
LINK OD1 ASP B 731 NA NA B 903 1555 1555 3.09
LINK OD2 ASP B 731 NA NA B 903 1555 1555 3.09
LINK O THR C 645 NA NA C 904 1555 1555 2.31
LINK O TYR C 726 NA NA C 904 1555 1555 2.19
LINK OD1 ASP C 728 NA NA C 904 1555 1555 2.31
LINK OD1 ASP C 731 NA NA C 904 1555 1555 3.02
LINK OD2 ASP C 731 NA NA C 904 1555 1555 2.66
LINK O THR D 645 NA NA D 906 1555 1555 2.28
LINK O TYR D 726 NA NA D 906 1555 1555 2.41
LINK OD1 ASP D 728 NA NA D 906 1555 1555 2.33
LINK OD1 ASP D 731 NA NA D 906 1555 1555 2.90
CISPEP 1 ASN A 29 PRO A 30 0 2.31
CISPEP 2 SER A 58 PRO A 59 0 5.24
CISPEP 3 GLY A 136 PRO A 137 0 4.95
CISPEP 4 SER A 144 PRO A 145 0 -4.49
CISPEP 5 ILE A 316 PRO A 317 0 6.74
CISPEP 6 GLY A 382 PRO A 383 0 3.13
CISPEP 7 MET A 487 PRO A 488 0 3.24
CISPEP 8 PRO A 488 HIS A 489 0 6.88
CISPEP 9 PHE A 600 PRO A 601 0 11.12
CISPEP 10 ASN B 29 PRO B 30 0 3.32
CISPEP 11 SER B 58 PRO B 59 0 11.63
CISPEP 12 GLY B 136 PRO B 137 0 -0.84
CISPEP 13 SER B 144 PRO B 145 0 -10.83
CISPEP 14 ILE B 316 PRO B 317 0 6.60
CISPEP 15 GLY B 382 PRO B 383 0 -2.32
CISPEP 16 MET B 487 PRO B 488 0 0.89
CISPEP 17 PRO B 488 HIS B 489 0 4.99
CISPEP 18 PHE B 600 PRO B 601 0 9.93
CISPEP 19 ASN C 29 PRO C 30 0 -3.48
CISPEP 20 SER C 58 PRO C 59 0 5.68
CISPEP 21 GLY C 136 PRO C 137 0 5.52
CISPEP 22 SER C 144 PRO C 145 0 -4.01
CISPEP 23 ASN C 166 GLY C 167 0 -25.30
CISPEP 24 ILE C 316 PRO C 317 0 6.76
CISPEP 25 GLY C 382 PRO C 383 0 -3.44
CISPEP 26 MET C 487 PRO C 488 0 4.10
CISPEP 27 PRO C 488 HIS C 489 0 7.87
CISPEP 28 PHE C 600 PRO C 601 0 12.35
CISPEP 29 ASN D 29 PRO D 30 0 0.80
CISPEP 30 SER D 58 PRO D 59 0 -0.50
CISPEP 31 GLY D 136 PRO D 137 0 -3.72
CISPEP 32 SER D 144 PRO D 145 0 -7.20
CISPEP 33 ASN D 166 GLY D 167 0 -24.77
CISPEP 34 ILE D 316 PRO D 317 0 7.22
CISPEP 35 GLY D 382 PRO D 383 0 -5.83
CISPEP 36 MET D 487 PRO D 488 0 1.78
CISPEP 37 PRO D 488 HIS D 489 0 14.69
CISPEP 38 PHE D 600 PRO D 601 0 12.38
SITE 1 AC1 6 GLY A 560 SER A 561 ALA A 562 SER A 634
SITE 2 AC1 6 SER A 635 HIS A 774
SITE 1 AC2 3 ASP A 38 TRP A 102 ARG A 281
SITE 1 AC3 4 SER A 672 ARG A 674 HOH A1032 SER C 651
SITE 1 AC4 4 THR A 645 TYR A 726 ASP A 728 ASP A 731
SITE 1 AC5 5 GLY B 560 SER B 561 ALA B 562 SER B 634
SITE 2 AC5 5 HIS B 774
SITE 1 AC6 2 ASP B 38 ARG B 281
SITE 1 AC7 4 THR B 645 TYR B 726 ASP B 728 ASP B 731
SITE 1 AC8 4 SER C 561 ALA C 562 SER C 634 HIS C 774
SITE 1 AC9 4 ASP C 38 MET C 55 TRP C 102 ARG C 281
SITE 1 AD1 4 ARG C 230 PHE C 273 ASP C 275 ARG C 281
SITE 1 AD2 4 THR C 645 TYR C 726 ASP C 728 ASP C 731
SITE 1 AD3 4 SER D 561 ALA D 562 SER D 634 HIS D 774
SITE 1 AD4 4 ASP D 38 MET D 55 GLN D 257 ARG D 281
SITE 1 AD5 5 LEU D 348 THR D 361 LYS D 373 ASN D 374
SITE 2 AD5 5 ASN D 499
SITE 1 AD6 2 LYS D 65 LYS D 73
SITE 1 AD7 4 TYR D 48 ASN D 67 ARG D 267 PRO D 310
SITE 1 AD8 4 THR D 645 TYR D 726 ASP D 728 ASP D 731
CRYST1 254.734 93.310 214.039 90.00 123.38 90.00 C 1 2 1 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 0.003926 0.000000 0.002587 0.00000
SCALE2 0.000000 0.010717 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005595 0.00000
TER 5556 GLY A 796
TER 11603 GLY B 796
TER 17655 GLY C 796
TER 23696 GLY D 796
MASTER 815 0 17 64 205 0 20 624144 4 84 252
END |