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HEADER HYDROLASE 03-SEP-13 4MJ3
TITLE HALOALKANE DEHALOGENASE DMRA FROM MYCOBACTERIUM RHODESIAE JS60
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM RHODESIAE;
SOURCE 3 ORGANISM_TAXID: 931627;
SOURCE 4 STRAIN: JS60;
SOURCE 5 GENE: MYCRHDRAFT_3907;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DEHALOGENASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.FUNG,M.S.GADD,J.M.GUSS,J.M.MATTHEWS
REVDAT 1 25-FEB-15 4MJ3 0
JRNL AUTH H.K.H.FUNG,M.S.GADD,T.A.DRURY,S.CHEUNG,J.M.GUSS,N.V.COLEMAN,
JRNL AUTH 2 J.M.MATTHEWS
JRNL TITL HALOALKANE DEHALOGENASES FROM MYCOBACTERIUM RHODESIAE JS60
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 134419
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6791
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9110
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.61
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE SET COUNT : 508
REMARK 3 BIN FREE R VALUE : 0.2660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9219
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 1051
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.61000
REMARK 3 B22 (A**2) : -0.46000
REMARK 3 B33 (A**2) : -0.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.10000
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.100
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.094
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.580
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9531 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8740 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13035 ; 1.332 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): 20090 ; 1.073 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1215 ; 5.415 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 422 ;31.240 ;23.270
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1256 ;11.386 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 64 ;15.192 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1403 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11005 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2219 ; 0.005 ; 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): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 301 B 1 301 18181 0.060 0.050
REMARK 3 2 A 1 301 C 1 301 18239 0.050 0.050
REMARK 3 3 A 1 301 D 1 301 18294 0.050 0.050
REMARK 3 4 B 1 303 C 1 303 18151 0.070 0.050
REMARK 3 5 B 1 303 D 1 303 18342 0.060 0.050
REMARK 3 6 C 1 303 D 1 303 18255 0.060 0.050
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 1 A 302
REMARK 3 ORIGIN FOR THE GROUP (A): 61.0058 41.8159 -11.5548
REMARK 3 T TENSOR
REMARK 3 T11: 0.0147 T22: 0.0374
REMARK 3 T33: 0.0070 T12: 0.0017
REMARK 3 T13: 0.0074 T23: 0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.4371 L22: 0.6168
REMARK 3 L33: 0.8264 L12: -0.0323
REMARK 3 L13: 0.0619 L23: 0.2051
REMARK 3 S TENSOR
REMARK 3 S11: 0.0025 S12: 0.0326 S13: -0.0054
REMARK 3 S21: -0.0723 S22: 0.0139 S23: -0.0621
REMARK 3 S31: -0.0883 S32: 0.0291 S33: -0.0164
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 1 B 303
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5652 43.4109 13.5115
REMARK 3 T TENSOR
REMARK 3 T11: 0.0052 T22: 0.0265
REMARK 3 T33: 0.0082 T12: 0.0014
REMARK 3 T13: -0.0015 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 1.2663 L22: 0.4154
REMARK 3 L33: 0.7800 L12: 0.0715
REMARK 3 L13: -0.1016 L23: -0.0380
REMARK 3 S TENSOR
REMARK 3 S11: 0.0110 S12: 0.0121 S13: -0.0871
REMARK 3 S21: -0.0123 S22: -0.0182 S23: 0.0214
REMARK 3 S31: 0.0603 S32: 0.0024 S33: 0.0072
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 1 C 303
REMARK 3 ORIGIN FOR THE GROUP (A): 62.3536 8.2084 36.0932
REMARK 3 T TENSOR
REMARK 3 T11: 0.0097 T22: 0.0551
REMARK 3 T33: 0.0171 T12: -0.0109
REMARK 3 T13: -0.0097 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.6339 L22: 0.4803
REMARK 3 L33: 0.6954 L12: -0.0331
REMARK 3 L13: -0.0746 L23: 0.0459
REMARK 3 S TENSOR
REMARK 3 S11: -0.0063 S12: 0.0265 S13: 0.0459
REMARK 3 S21: -0.0155 S22: 0.0122 S23: 0.0145
REMARK 3 S31: 0.0282 S32: -0.0319 S33: -0.0059
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 1 D 303
REMARK 3 ORIGIN FOR THE GROUP (A): 66.4242 45.9715 34.8907
REMARK 3 T TENSOR
REMARK 3 T11: 0.0064 T22: 0.0591
REMARK 3 T33: 0.0136 T12: -0.0135
REMARK 3 T13: -0.0051 T23: 0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.8107 L22: 0.6103
REMARK 3 L33: 0.8095 L12: -0.2299
REMARK 3 L13: 0.1959 L23: -0.0703
REMARK 3 S TENSOR
REMARK 3 S11: 0.0191 S12: -0.0028 S13: -0.0363
REMARK 3 S21: 0.0134 S22: -0.0078 S23: 0.0319
REMARK 3 S31: -0.0339 S32: 0.0134 S33: -0.0113
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 4MJ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-SEP-13.
REMARK 100 THE RCSB ID CODE IS RCSB081973.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-AUG-12
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 : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : SILICON DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 134710
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
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 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHASER (PHENIX AUTOSOL)
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PROPANE, PH 6.5, 0.2 M
REMARK 280 POTASSIUM THIOCYANATE, 16% PEG 3350, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 39.53950
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ARG A 303
REMARK 465 ALA A 304
REMARK 465 GLU A 305
REMARK 465 LEU A 306
REMARK 465 ASN A 307
REMARK 465 SER A 308
REMARK 465 SER A 309
REMARK 465 SER A 310
REMARK 465 VAL A 311
REMARK 465 ASP A 312
REMARK 465 LYS A 313
REMARK 465 LEU A 314
REMARK 465 ALA A 315
REMARK 465 ALA A 316
REMARK 465 ALA A 317
REMARK 465 LEU A 318
REMARK 465 GLU A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 ALA B 304
REMARK 465 GLU B 305
REMARK 465 LEU B 306
REMARK 465 ASN B 307
REMARK 465 SER B 308
REMARK 465 SER B 309
REMARK 465 SER B 310
REMARK 465 VAL B 311
REMARK 465 ASP B 312
REMARK 465 LYS B 313
REMARK 465 LEU B 314
REMARK 465 ALA B 315
REMARK 465 ALA B 316
REMARK 465 ALA B 317
REMARK 465 LEU B 318
REMARK 465 GLU B 319
REMARK 465 HIS B 320
REMARK 465 HIS B 321
REMARK 465 HIS B 322
REMARK 465 HIS B 323
REMARK 465 HIS B 324
REMARK 465 HIS B 325
REMARK 465 ALA C 304
REMARK 465 GLU C 305
REMARK 465 LEU C 306
REMARK 465 ASN C 307
REMARK 465 SER C 308
REMARK 465 SER C 309
REMARK 465 SER C 310
REMARK 465 VAL C 311
REMARK 465 ASP C 312
REMARK 465 LYS C 313
REMARK 465 LEU C 314
REMARK 465 ALA C 315
REMARK 465 ALA C 316
REMARK 465 ALA C 317
REMARK 465 LEU C 318
REMARK 465 GLU C 319
REMARK 465 HIS C 320
REMARK 465 HIS C 321
REMARK 465 HIS C 322
REMARK 465 HIS C 323
REMARK 465 HIS C 324
REMARK 465 HIS C 325
REMARK 465 ALA D 304
REMARK 465 GLU D 305
REMARK 465 LEU D 306
REMARK 465 ASN D 307
REMARK 465 SER D 308
REMARK 465 SER D 309
REMARK 465 SER D 310
REMARK 465 VAL D 311
REMARK 465 ASP D 312
REMARK 465 LYS D 313
REMARK 465 LEU D 314
REMARK 465 ALA D 315
REMARK 465 ALA D 316
REMARK 465 ALA D 317
REMARK 465 LEU D 318
REMARK 465 GLU D 319
REMARK 465 HIS D 320
REMARK 465 HIS D 321
REMARK 465 HIS D 322
REMARK 465 HIS D 323
REMARK 465 HIS D 324
REMARK 465 HIS D 325
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 ARG A 22 CZ NH1 NH2
REMARK 470 ARG A 43 CD NE CZ NH1 NH2
REMARK 470 SER A 44 OG
REMARK 470 ASP A 45 OD1 OD2
REMARK 470 GLU A 191 CG CD OE1 OE2
REMARK 470 LYS A 230 CD CE NZ
REMARK 470 ARG A 268 CD NE CZ NH1 NH2
REMARK 470 ARG A 288 CD NE CZ NH1 NH2
REMARK 470 ARG B 22 CZ NH1 NH2
REMARK 470 ASP B 27 OD1 OD2
REMARK 470 ASP B 30 CG OD1 OD2
REMARK 470 ARG B 43 CD NE CZ NH1 NH2
REMARK 470 GLU B 159 CD OE1 OE2
REMARK 470 LYS B 230 CD CE NZ
REMARK 470 ARG B 303 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 9 CD OE1 OE2
REMARK 470 ARG C 22 CZ NH1 NH2
REMARK 470 GLU C 159 CG CD OE1 OE2
REMARK 470 LYS C 166 NZ
REMARK 470 GLU C 191 CG CD OE1 OE2
REMARK 470 LYS C 230 CE NZ
REMARK 470 ARG C 268 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 288 CD NE CZ NH1 NH2
REMARK 470 ARG C 303 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 2 CG OD1 OD2
REMARK 470 ARG D 22 CZ NH1 NH2
REMARK 470 ARG D 43 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 159 CG CD OE1 OE2
REMARK 470 LYS D 230 CE NZ
REMARK 470 ARG D 288 CZ NH1 NH2
REMARK 470 ARG D 303 CG CD NE CZ NH1 NH2
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 PRO A 18 51.36 -90.64
REMARK 500 PRO A 56 53.12 -101.42
REMARK 500 SER A 57 -165.46 -101.41
REMARK 500 ASP A 123 -138.38 53.79
REMARK 500 LYS A 286 46.41 -144.38
REMARK 500 PRO B 56 53.52 -101.13
REMARK 500 SER B 57 -164.00 -101.13
REMARK 500 ASP B 123 -138.24 53.81
REMARK 500 LYS B 286 46.68 -143.40
REMARK 500 PRO C 18 51.58 -90.39
REMARK 500 PRO C 56 53.64 -103.29
REMARK 500 SER C 57 -163.77 -100.01
REMARK 500 ASP C 123 -140.41 56.17
REMARK 500 LYS C 286 45.65 -144.50
REMARK 500 PRO D 56 54.78 -101.65
REMARK 500 SER D 57 -166.38 -101.77
REMARK 500 ASP D 123 -139.57 53.99
REMARK 500 LYS D 286 44.46 -142.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 696 DISTANCE = 5.27 ANGSTROMS
REMARK 525 HOH B 697 DISTANCE = 7.00 ANGSTROMS
REMARK 525 HOH B 709 DISTANCE = 7.72 ANGSTROMS
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 K B 402 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 186 O
REMARK 620 2 ASN B 181 O 118.3
REMARK 620 3 SER B 184 O 89.2 70.8
REMARK 620 4 ASN B 181 OD1 79.7 75.1 133.2
REMARK 620 5 HOH B 537 O 90.2 142.4 138.0 87.7
REMARK 620 6 HOH B 665 O 91.2 137.3 80.3 144.5 57.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C 402 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER C 186 O
REMARK 620 2 SER C 184 O 91.2
REMARK 620 3 ASN C 181 O 117.8 72.0
REMARK 620 4 GLY D 182 O 146.8 78.2 88.9
REMARK 620 5 ASN C 181 OD1 77.9 132.7 73.1 131.7
REMARK 620 6 HOH C 553 O 88.5 135.7 143.8 78.2 90.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K D 403 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN D 181 O
REMARK 620 2 SER D 186 O 117.7
REMARK 620 3 GLY C 182 O 85.1 151.4
REMARK 620 4 SER D 184 O 71.8 86.7 84.3
REMARK 620 5 ASN D 181 OD1 75.7 79.1 125.9 132.9
REMARK 620 6 HOH D 525 O 143.0 91.6 76.6 136.2 89.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K D 402 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY D 182 O
REMARK 620 2 GLY C 182 O 111.5
REMARK 620 3 SER D 184 O 107.7 83.1
REMARK 620 4 SER C 184 O 75.7 102.2 172.4
REMARK 620 5 HOH D 645 O 67.0 177.9 95.8 79.0
REMARK 620 6 HOH C 586 O 169.7 73.2 81.7 94.5 108.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 403 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 182 O
REMARK 620 2 SER B 184 O 103.7
REMARK 620 3 HOH B 515 O 67.7 95.0
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 403
DBREF 4MJ3 A 1 305 UNP G4I2J6 G4I2J6_MYCRH 1 305
DBREF 4MJ3 B 1 305 UNP G4I2J6 G4I2J6_MYCRH 1 305
DBREF 4MJ3 C 1 305 UNP G4I2J6 G4I2J6_MYCRH 1 305
DBREF 4MJ3 D 1 305 UNP G4I2J6 G4I2J6_MYCRH 1 305
SEQADV 4MJ3 LEU A 306 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 ASN A 307 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 SER A 308 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 SER A 309 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 SER A 310 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 VAL A 311 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 ASP A 312 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 LYS A 313 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 LEU A 314 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 ALA A 315 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 ALA A 316 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 ALA A 317 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 LEU A 318 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 GLU A 319 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS A 320 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS A 321 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS A 322 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS A 323 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS A 324 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS A 325 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 LEU B 306 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 ASN B 307 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 SER B 308 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 SER B 309 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 SER B 310 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 VAL B 311 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 ASP B 312 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 LYS B 313 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 LEU B 314 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 ALA B 315 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 ALA B 316 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 ALA B 317 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 LEU B 318 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 GLU B 319 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS B 320 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS B 321 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS B 322 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS B 323 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS B 324 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS B 325 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 LEU C 306 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 ASN C 307 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 SER C 308 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 SER C 309 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 SER C 310 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 VAL C 311 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 ASP C 312 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 LYS C 313 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 LEU C 314 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 ALA C 315 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 ALA C 316 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 ALA C 317 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 LEU C 318 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 GLU C 319 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS C 320 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS C 321 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS C 322 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS C 323 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS C 324 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS C 325 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 LEU D 306 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 ASN D 307 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 SER D 308 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 SER D 309 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 SER D 310 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 VAL D 311 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 ASP D 312 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 LYS D 313 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 LEU D 314 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 ALA D 315 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 ALA D 316 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 ALA D 317 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 LEU D 318 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 GLU D 319 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS D 320 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS D 321 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS D 322 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS D 323 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS D 324 UNP G4I2J6 EXPRESSION TAG
SEQADV 4MJ3 HIS D 325 UNP G4I2J6 EXPRESSION TAG
SEQRES 1 A 325 MSE ASP VAL LEU ARG THR PRO ASP GLU ARG PHE THR ALA
SEQRES 2 A 325 LEU PRO ASP PHE PRO PHE ALA PRO ARG TYR VAL GLU VAL
SEQRES 3 A 325 ASP SER GLY ASP GLY GLY THR LEU ARG MSE HIS TYR LEU
SEQRES 4 A 325 ASP GLU GLY ARG SER ASP GLY GLU VAL VAL LEU LEU LEU
SEQRES 5 A 325 HIS GLY GLU PRO SER TRP SER TYR LEU TYR ARG TRP MSE
SEQRES 6 A 325 ILE PRO VAL LEU VAL GLU ALA GLY LEU ARG ALA VAL ALA
SEQRES 7 A 325 ILE ASP LEU VAL GLY PHE GLY ARG SER ASP LYS PRO THR
SEQRES 8 A 325 SER ARG ASP ASP TYR THR TYR GLN ALA HIS VAL ASP TRP
SEQRES 9 A 325 MSE TRP ALA ALA ILE GLU GLU ILE GLY LEU ALA ASP VAL
SEQRES 10 A 325 THR LEU VAL CYS GLN ASP TRP GLY GLY LEU ILE GLY LEU
SEQRES 11 A 325 ARG LEU VAL GLY GLU HIS PRO ASP ARG PHE ALA ARG VAL
SEQRES 12 A 325 VAL ALA ALA ASN THR MSE LEU PRO THR GLY ASP HIS HIS
SEQRES 13 A 325 PRO GLY GLU ALA PHE LEU ALA TRP GLN LYS PHE SER GLN
SEQRES 14 A 325 GLU VAL PRO LEU PHE PRO ALA GLY GLN ILE VAL ASN GLY
SEQRES 15 A 325 GLY SER LEU SER THR LEU SER ALA GLU THR ILE ALA ALA
SEQRES 16 A 325 TYR ASP ALA PRO PHE PRO ASP ALA SER TYR GLN ALA GLY
SEQRES 17 A 325 ALA ARG GLN PHE PRO MSE LEU VAL PRO ILE SER PRO ASP
SEQRES 18 A 325 ASP PRO ALA THR PRO ALA ASN ARG LYS ALA TRP ALA ALA
SEQRES 19 A 325 LEU GLY ARG PHE GLU LYS PRO PHE LEU SER ALA PHE SER
SEQRES 20 A 325 ASP SER ASP PRO ILE THR GLY ALA ALA GLU PRO VAL LEU
SEQRES 21 A 325 ARG GLY HIS VAL PRO GLY ALA ARG GLY GLN SER HIS VAL
SEQRES 22 A 325 THR ILE ALA GLY ALA GLY HIS PHE LEU GLN GLU ASP LYS
SEQRES 23 A 325 GLY ARG GLU LEU ALA GLU ALA VAL VAL THR PHE VAL ARG
SEQRES 24 A 325 ALA ASN PRO ARG ALA GLU LEU ASN SER SER SER VAL ASP
SEQRES 25 A 325 LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 325 MSE ASP VAL LEU ARG THR PRO ASP GLU ARG PHE THR ALA
SEQRES 2 B 325 LEU PRO ASP PHE PRO PHE ALA PRO ARG TYR VAL GLU VAL
SEQRES 3 B 325 ASP SER GLY ASP GLY GLY THR LEU ARG MSE HIS TYR LEU
SEQRES 4 B 325 ASP GLU GLY ARG SER ASP GLY GLU VAL VAL LEU LEU LEU
SEQRES 5 B 325 HIS GLY GLU PRO SER TRP SER TYR LEU TYR ARG TRP MSE
SEQRES 6 B 325 ILE PRO VAL LEU VAL GLU ALA GLY LEU ARG ALA VAL ALA
SEQRES 7 B 325 ILE ASP LEU VAL GLY PHE GLY ARG SER ASP LYS PRO THR
SEQRES 8 B 325 SER ARG ASP ASP TYR THR TYR GLN ALA HIS VAL ASP TRP
SEQRES 9 B 325 MSE TRP ALA ALA ILE GLU GLU ILE GLY LEU ALA ASP VAL
SEQRES 10 B 325 THR LEU VAL CYS GLN ASP TRP GLY GLY LEU ILE GLY LEU
SEQRES 11 B 325 ARG LEU VAL GLY GLU HIS PRO ASP ARG PHE ALA ARG VAL
SEQRES 12 B 325 VAL ALA ALA ASN THR MSE LEU PRO THR GLY ASP HIS HIS
SEQRES 13 B 325 PRO GLY GLU ALA PHE LEU ALA TRP GLN LYS PHE SER GLN
SEQRES 14 B 325 GLU VAL PRO LEU PHE PRO ALA GLY GLN ILE VAL ASN GLY
SEQRES 15 B 325 GLY SER LEU SER THR LEU SER ALA GLU THR ILE ALA ALA
SEQRES 16 B 325 TYR ASP ALA PRO PHE PRO ASP ALA SER TYR GLN ALA GLY
SEQRES 17 B 325 ALA ARG GLN PHE PRO MSE LEU VAL PRO ILE SER PRO ASP
SEQRES 18 B 325 ASP PRO ALA THR PRO ALA ASN ARG LYS ALA TRP ALA ALA
SEQRES 19 B 325 LEU GLY ARG PHE GLU LYS PRO PHE LEU SER ALA PHE SER
SEQRES 20 B 325 ASP SER ASP PRO ILE THR GLY ALA ALA GLU PRO VAL LEU
SEQRES 21 B 325 ARG GLY HIS VAL PRO GLY ALA ARG GLY GLN SER HIS VAL
SEQRES 22 B 325 THR ILE ALA GLY ALA GLY HIS PHE LEU GLN GLU ASP LYS
SEQRES 23 B 325 GLY ARG GLU LEU ALA GLU ALA VAL VAL THR PHE VAL ARG
SEQRES 24 B 325 ALA ASN PRO ARG ALA GLU LEU ASN SER SER SER VAL ASP
SEQRES 25 B 325 LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 325 MSE ASP VAL LEU ARG THR PRO ASP GLU ARG PHE THR ALA
SEQRES 2 C 325 LEU PRO ASP PHE PRO PHE ALA PRO ARG TYR VAL GLU VAL
SEQRES 3 C 325 ASP SER GLY ASP GLY GLY THR LEU ARG MSE HIS TYR LEU
SEQRES 4 C 325 ASP GLU GLY ARG SER ASP GLY GLU VAL VAL LEU LEU LEU
SEQRES 5 C 325 HIS GLY GLU PRO SER TRP SER TYR LEU TYR ARG TRP MSE
SEQRES 6 C 325 ILE PRO VAL LEU VAL GLU ALA GLY LEU ARG ALA VAL ALA
SEQRES 7 C 325 ILE ASP LEU VAL GLY PHE GLY ARG SER ASP LYS PRO THR
SEQRES 8 C 325 SER ARG ASP ASP TYR THR TYR GLN ALA HIS VAL ASP TRP
SEQRES 9 C 325 MSE TRP ALA ALA ILE GLU GLU ILE GLY LEU ALA ASP VAL
SEQRES 10 C 325 THR LEU VAL CYS GLN ASP TRP GLY GLY LEU ILE GLY LEU
SEQRES 11 C 325 ARG LEU VAL GLY GLU HIS PRO ASP ARG PHE ALA ARG VAL
SEQRES 12 C 325 VAL ALA ALA ASN THR MSE LEU PRO THR GLY ASP HIS HIS
SEQRES 13 C 325 PRO GLY GLU ALA PHE LEU ALA TRP GLN LYS PHE SER GLN
SEQRES 14 C 325 GLU VAL PRO LEU PHE PRO ALA GLY GLN ILE VAL ASN GLY
SEQRES 15 C 325 GLY SER LEU SER THR LEU SER ALA GLU THR ILE ALA ALA
SEQRES 16 C 325 TYR ASP ALA PRO PHE PRO ASP ALA SER TYR GLN ALA GLY
SEQRES 17 C 325 ALA ARG GLN PHE PRO MSE LEU VAL PRO ILE SER PRO ASP
SEQRES 18 C 325 ASP PRO ALA THR PRO ALA ASN ARG LYS ALA TRP ALA ALA
SEQRES 19 C 325 LEU GLY ARG PHE GLU LYS PRO PHE LEU SER ALA PHE SER
SEQRES 20 C 325 ASP SER ASP PRO ILE THR GLY ALA ALA GLU PRO VAL LEU
SEQRES 21 C 325 ARG GLY HIS VAL PRO GLY ALA ARG GLY GLN SER HIS VAL
SEQRES 22 C 325 THR ILE ALA GLY ALA GLY HIS PHE LEU GLN GLU ASP LYS
SEQRES 23 C 325 GLY ARG GLU LEU ALA GLU ALA VAL VAL THR PHE VAL ARG
SEQRES 24 C 325 ALA ASN PRO ARG ALA GLU LEU ASN SER SER SER VAL ASP
SEQRES 25 C 325 LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 325 MSE ASP VAL LEU ARG THR PRO ASP GLU ARG PHE THR ALA
SEQRES 2 D 325 LEU PRO ASP PHE PRO PHE ALA PRO ARG TYR VAL GLU VAL
SEQRES 3 D 325 ASP SER GLY ASP GLY GLY THR LEU ARG MSE HIS TYR LEU
SEQRES 4 D 325 ASP GLU GLY ARG SER ASP GLY GLU VAL VAL LEU LEU LEU
SEQRES 5 D 325 HIS GLY GLU PRO SER TRP SER TYR LEU TYR ARG TRP MSE
SEQRES 6 D 325 ILE PRO VAL LEU VAL GLU ALA GLY LEU ARG ALA VAL ALA
SEQRES 7 D 325 ILE ASP LEU VAL GLY PHE GLY ARG SER ASP LYS PRO THR
SEQRES 8 D 325 SER ARG ASP ASP TYR THR TYR GLN ALA HIS VAL ASP TRP
SEQRES 9 D 325 MSE TRP ALA ALA ILE GLU GLU ILE GLY LEU ALA ASP VAL
SEQRES 10 D 325 THR LEU VAL CYS GLN ASP TRP GLY GLY LEU ILE GLY LEU
SEQRES 11 D 325 ARG LEU VAL GLY GLU HIS PRO ASP ARG PHE ALA ARG VAL
SEQRES 12 D 325 VAL ALA ALA ASN THR MSE LEU PRO THR GLY ASP HIS HIS
SEQRES 13 D 325 PRO GLY GLU ALA PHE LEU ALA TRP GLN LYS PHE SER GLN
SEQRES 14 D 325 GLU VAL PRO LEU PHE PRO ALA GLY GLN ILE VAL ASN GLY
SEQRES 15 D 325 GLY SER LEU SER THR LEU SER ALA GLU THR ILE ALA ALA
SEQRES 16 D 325 TYR ASP ALA PRO PHE PRO ASP ALA SER TYR GLN ALA GLY
SEQRES 17 D 325 ALA ARG GLN PHE PRO MSE LEU VAL PRO ILE SER PRO ASP
SEQRES 18 D 325 ASP PRO ALA THR PRO ALA ASN ARG LYS ALA TRP ALA ALA
SEQRES 19 D 325 LEU GLY ARG PHE GLU LYS PRO PHE LEU SER ALA PHE SER
SEQRES 20 D 325 ASP SER ASP PRO ILE THR GLY ALA ALA GLU PRO VAL LEU
SEQRES 21 D 325 ARG GLY HIS VAL PRO GLY ALA ARG GLY GLN SER HIS VAL
SEQRES 22 D 325 THR ILE ALA GLY ALA GLY HIS PHE LEU GLN GLU ASP LYS
SEQRES 23 D 325 GLY ARG GLU LEU ALA GLU ALA VAL VAL THR PHE VAL ARG
SEQRES 24 D 325 ALA ASN PRO ARG ALA GLU LEU ASN SER SER SER VAL ASP
SEQRES 25 D 325 LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 4MJ3 MSE A 1 MET SELENOMETHIONINE
MODRES 4MJ3 MSE A 36 MET SELENOMETHIONINE
MODRES 4MJ3 MSE A 65 MET SELENOMETHIONINE
MODRES 4MJ3 MSE A 105 MET SELENOMETHIONINE
MODRES 4MJ3 MSE A 149 MET SELENOMETHIONINE
MODRES 4MJ3 MSE A 214 MET SELENOMETHIONINE
MODRES 4MJ3 MSE B 1 MET SELENOMETHIONINE
MODRES 4MJ3 MSE B 36 MET SELENOMETHIONINE
MODRES 4MJ3 MSE B 65 MET SELENOMETHIONINE
MODRES 4MJ3 MSE B 105 MET SELENOMETHIONINE
MODRES 4MJ3 MSE B 149 MET SELENOMETHIONINE
MODRES 4MJ3 MSE B 214 MET SELENOMETHIONINE
MODRES 4MJ3 MSE C 1 MET SELENOMETHIONINE
MODRES 4MJ3 MSE C 36 MET SELENOMETHIONINE
MODRES 4MJ3 MSE C 65 MET SELENOMETHIONINE
MODRES 4MJ3 MSE C 105 MET SELENOMETHIONINE
MODRES 4MJ3 MSE C 149 MET SELENOMETHIONINE
MODRES 4MJ3 MSE C 214 MET SELENOMETHIONINE
MODRES 4MJ3 MSE D 1 MET SELENOMETHIONINE
MODRES 4MJ3 MSE D 36 MET SELENOMETHIONINE
MODRES 4MJ3 MSE D 65 MET SELENOMETHIONINE
MODRES 4MJ3 MSE D 105 MET SELENOMETHIONINE
MODRES 4MJ3 MSE D 149 MET SELENOMETHIONINE
MODRES 4MJ3 MSE D 214 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 36 8
HET MSE A 65 8
HET MSE A 105 8
HET MSE A 149 16
HET MSE A 214 8
HET MSE B 1 8
HET MSE B 36 8
HET MSE B 65 8
HET MSE B 105 8
HET MSE B 149 16
HET MSE B 214 8
HET MSE C 1 8
HET MSE C 36 8
HET MSE C 65 8
HET MSE C 105 8
HET MSE C 149 16
HET MSE C 214 8
HET MSE D 1 8
HET MSE D 36 8
HET MSE D 65 8
HET MSE D 105 8
HET MSE D 149 16
HET MSE D 214 8
HET CL A 401 1
HET CL B 401 1
HET K B 402 1
HET K B 403 1
HET K B 404 1
HET CL C 401 1
HET K C 402 1
HET CL D 401 1
HET K D 402 1
HET K D 403 1
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM K POTASSIUM ION
FORMUL 1 MSE 24(C5 H11 N O2 SE)
FORMUL 5 CL 4(CL 1-)
FORMUL 7 K 6(K 1+)
FORMUL 15 HOH *1051(H2 O)
HELIX 1 1 PRO A 7 THR A 12 5 6
HELIX 2 2 TRP A 58 ARG A 63 5 6
HELIX 3 3 MSE A 65 ALA A 72 1 8
HELIX 4 4 SER A 92 TYR A 96 5 5
HELIX 5 5 THR A 97 GLY A 113 1 17
HELIX 6 6 ASP A 123 HIS A 136 1 14
HELIX 7 7 GLY A 158 VAL A 171 1 14
HELIX 8 8 PRO A 175 GLY A 183 1 9
HELIX 9 9 SER A 189 ALA A 198 1 10
HELIX 10 10 ASP A 202 TYR A 205 5 4
HELIX 11 11 GLN A 206 PHE A 212 1 7
HELIX 12 12 PRO A 213 VAL A 216 5 4
HELIX 13 13 ALA A 224 GLY A 236 1 13
HELIX 14 14 ALA A 255 VAL A 264 1 10
HELIX 15 15 PRO A 265 ARG A 268 5 4
HELIX 16 16 PHE A 281 ASN A 301 1 21
HELIX 17 17 PRO B 7 THR B 12 5 6
HELIX 18 18 TRP B 58 ARG B 63 5 6
HELIX 19 19 MSE B 65 ALA B 72 1 8
HELIX 20 20 SER B 92 TYR B 96 5 5
HELIX 21 21 THR B 97 GLY B 113 1 17
HELIX 22 22 ASP B 123 HIS B 136 1 14
HELIX 23 23 GLY B 158 VAL B 171 1 14
HELIX 24 24 PRO B 175 GLY B 183 1 9
HELIX 25 25 SER B 189 ALA B 198 1 10
HELIX 26 26 ASP B 202 TYR B 205 5 4
HELIX 27 27 GLN B 206 PHE B 212 1 7
HELIX 28 28 PRO B 213 VAL B 216 5 4
HELIX 29 29 ALA B 224 GLY B 236 1 13
HELIX 30 30 THR B 253 ALA B 255 5 3
HELIX 31 31 ALA B 256 VAL B 264 1 9
HELIX 32 32 PRO B 265 ARG B 268 5 4
HELIX 33 33 PHE B 281 ASN B 301 1 21
HELIX 34 34 PRO C 7 THR C 12 5 6
HELIX 35 35 TRP C 58 ARG C 63 5 6
HELIX 36 36 MSE C 65 ALA C 72 1 8
HELIX 37 37 SER C 92 TYR C 96 5 5
HELIX 38 38 THR C 97 GLY C 113 1 17
HELIX 39 39 ASP C 123 HIS C 136 1 14
HELIX 40 40 GLY C 158 VAL C 171 1 14
HELIX 41 41 PRO C 175 GLY C 183 1 9
HELIX 42 42 SER C 189 ALA C 198 1 10
HELIX 43 43 ASP C 202 TYR C 205 5 4
HELIX 44 44 GLN C 206 PHE C 212 1 7
HELIX 45 45 PRO C 213 VAL C 216 5 4
HELIX 46 46 ALA C 224 GLY C 236 1 13
HELIX 47 47 ALA C 255 VAL C 264 1 10
HELIX 48 48 PRO C 265 ARG C 268 5 4
HELIX 49 49 PHE C 281 ASN C 301 1 21
HELIX 50 50 PRO D 7 THR D 12 5 6
HELIX 51 51 TRP D 58 ARG D 63 5 6
HELIX 52 52 MSE D 65 ALA D 72 1 8
HELIX 53 53 SER D 92 TYR D 96 5 5
HELIX 54 54 THR D 97 GLY D 113 1 17
HELIX 55 55 ASP D 123 HIS D 136 1 14
HELIX 56 56 GLY D 158 VAL D 171 1 14
HELIX 57 57 PRO D 175 GLY D 183 1 9
HELIX 58 58 SER D 189 ALA D 198 1 10
HELIX 59 59 ASP D 202 TYR D 205 5 4
HELIX 60 60 GLN D 206 PHE D 212 1 7
HELIX 61 61 PRO D 213 VAL D 216 5 4
HELIX 62 62 ALA D 224 GLY D 236 1 13
HELIX 63 63 ALA D 255 VAL D 264 1 10
HELIX 64 64 PRO D 265 ARG D 268 5 4
HELIX 65 65 PHE D 281 ASN D 301 1 21
SHEET 1 A 2 VAL A 3 LEU A 4 0
SHEET 2 A 2 LYS A 89 PRO A 90 -1 O LYS A 89 N LEU A 4
SHEET 1 B 7 ARG A 22 ASP A 27 0
SHEET 2 B 7 THR A 33 GLU A 41 -1 O MSE A 36 N VAL A 24
SHEET 3 B 7 ARG A 75 ILE A 79 -1 O ALA A 76 N GLU A 41
SHEET 4 B 7 VAL A 48 LEU A 52 1 N LEU A 51 O VAL A 77
SHEET 5 B 7 VAL A 117 CYS A 121 1 O VAL A 120 N LEU A 50
SHEET 6 B 7 PHE A 140 ALA A 145 1 O VAL A 144 N LEU A 119
SHEET 7 B 7 PHE A 242 SER A 244 1 O LEU A 243 N VAL A 143
SHEET 1 C 2 VAL B 3 LEU B 4 0
SHEET 2 C 2 LYS B 89 PRO B 90 -1 O LYS B 89 N LEU B 4
SHEET 1 D 7 ARG B 22 ASP B 27 0
SHEET 2 D 7 THR B 33 GLU B 41 -1 O MSE B 36 N VAL B 24
SHEET 3 D 7 ARG B 75 ILE B 79 -1 O ALA B 76 N GLU B 41
SHEET 4 D 7 VAL B 48 LEU B 52 1 N LEU B 51 O VAL B 77
SHEET 5 D 7 VAL B 117 CYS B 121 1 O VAL B 120 N LEU B 50
SHEET 6 D 7 PHE B 140 ALA B 145 1 O VAL B 144 N LEU B 119
SHEET 7 D 7 PHE B 242 SER B 244 1 O LEU B 243 N VAL B 143
SHEET 1 E 2 VAL C 3 LEU C 4 0
SHEET 2 E 2 LYS C 89 PRO C 90 -1 O LYS C 89 N LEU C 4
SHEET 1 F 7 ARG C 22 ASP C 27 0
SHEET 2 F 7 THR C 33 GLU C 41 -1 O MSE C 36 N VAL C 24
SHEET 3 F 7 ARG C 75 ILE C 79 -1 O ALA C 76 N GLU C 41
SHEET 4 F 7 VAL C 48 LEU C 52 1 N LEU C 51 O VAL C 77
SHEET 5 F 7 VAL C 117 CYS C 121 1 O VAL C 120 N LEU C 50
SHEET 6 F 7 PHE C 140 ALA C 145 1 O VAL C 144 N LEU C 119
SHEET 7 F 7 PHE C 242 SER C 244 1 O LEU C 243 N VAL C 143
SHEET 1 G 2 VAL D 3 LEU D 4 0
SHEET 2 G 2 LYS D 89 PRO D 90 -1 O LYS D 89 N LEU D 4
SHEET 1 H 7 ARG D 22 ASP D 27 0
SHEET 2 H 7 THR D 33 GLU D 41 -1 O LEU D 34 N VAL D 26
SHEET 3 H 7 ARG D 75 ILE D 79 -1 O ALA D 76 N GLU D 41
SHEET 4 H 7 VAL D 48 LEU D 52 1 N LEU D 51 O VAL D 77
SHEET 5 H 7 VAL D 117 CYS D 121 1 O VAL D 120 N LEU D 50
SHEET 6 H 7 PHE D 140 ALA D 145 1 O VAL D 144 N LEU D 119
SHEET 7 H 7 PHE D 242 SER D 244 1 O LEU D 243 N VAL D 143
LINK C MSE A 1 N ASP A 2 1555 1555 1.32
LINK C ARG A 35 N MSE A 36 1555 1555 1.34
LINK C MSE A 36 N HIS A 37 1555 1555 1.32
LINK C TRP A 64 N MSE A 65 1555 1555 1.33
LINK C MSE A 65 N ILE A 66 1555 1555 1.33
LINK C TRP A 104 N MSE A 105 1555 1555 1.33
LINK C MSE A 105 N TRP A 106 1555 1555 1.33
LINK C THR A 148 N AMSE A 149 1555 1555 1.33
LINK C THR A 148 N BMSE A 149 1555 1555 1.33
LINK C AMSE A 149 N LEU A 150 1555 1555 1.33
LINK C BMSE A 149 N LEU A 150 1555 1555 1.33
LINK C PRO A 213 N MSE A 214 1555 1555 1.33
LINK C MSE A 214 N LEU A 215 1555 1555 1.33
LINK C MSE B 1 N ASP B 2 1555 1555 1.32
LINK C ARG B 35 N MSE B 36 1555 1555 1.34
LINK C MSE B 36 N HIS B 37 1555 1555 1.32
LINK C TRP B 64 N MSE B 65 1555 1555 1.32
LINK C MSE B 65 N ILE B 66 1555 1555 1.33
LINK C TRP B 104 N MSE B 105 1555 1555 1.33
LINK C MSE B 105 N TRP B 106 1555 1555 1.34
LINK C THR B 148 N AMSE B 149 1555 1555 1.34
LINK C THR B 148 N BMSE B 149 1555 1555 1.34
LINK C AMSE B 149 N LEU B 150 1555 1555 1.33
LINK C BMSE B 149 N LEU B 150 1555 1555 1.33
LINK C PRO B 213 N MSE B 214 1555 1555 1.33
LINK C MSE B 214 N LEU B 215 1555 1555 1.34
LINK C MSE C 1 N ASP C 2 1555 1555 1.32
LINK C ARG C 35 N MSE C 36 1555 1555 1.34
LINK C MSE C 36 N HIS C 37 1555 1555 1.33
LINK C TRP C 64 N MSE C 65 1555 1555 1.33
LINK C MSE C 65 N ILE C 66 1555 1555 1.33
LINK C TRP C 104 N MSE C 105 1555 1555 1.32
LINK C MSE C 105 N TRP C 106 1555 1555 1.33
LINK C THR C 148 N AMSE C 149 1555 1555 1.33
LINK C THR C 148 N BMSE C 149 1555 1555 1.33
LINK C AMSE C 149 N LEU C 150 1555 1555 1.33
LINK C BMSE C 149 N LEU C 150 1555 1555 1.34
LINK C PRO C 213 N MSE C 214 1555 1555 1.33
LINK C MSE C 214 N LEU C 215 1555 1555 1.33
LINK C MSE D 1 N ASP D 2 1555 1555 1.33
LINK C ARG D 35 N MSE D 36 1555 1555 1.33
LINK C MSE D 36 N HIS D 37 1555 1555 1.33
LINK C TRP D 64 N MSE D 65 1555 1555 1.33
LINK C MSE D 65 N ILE D 66 1555 1555 1.33
LINK C TRP D 104 N MSE D 105 1555 1555 1.33
LINK C MSE D 105 N TRP D 106 1555 1555 1.34
LINK C THR D 148 N AMSE D 149 1555 1555 1.33
LINK C THR D 148 N BMSE D 149 1555 1555 1.33
LINK C AMSE D 149 N LEU D 150 1555 1555 1.33
LINK C BMSE D 149 N LEU D 150 1555 1555 1.34
LINK C PRO D 213 N MSE D 214 1555 1555 1.34
LINK C MSE D 214 N LEU D 215 1555 1555 1.34
LINK O SER B 186 K K B 402 1555 1555 2.62
LINK O SER C 186 K K C 402 1555 1555 2.63
LINK O ASN D 181 K K D 403 1555 1555 2.68
LINK O SER C 184 K K C 402 1555 1555 2.68
LINK O SER D 186 K K D 403 1555 1555 2.70
LINK O ASN B 181 K K B 402 1555 1555 2.71
LINK O ASN C 181 K K C 402 1555 1555 2.71
LINK O GLY C 182 K K D 403 1555 1555 2.74
LINK O GLY D 182 K K D 402 1555 1555 2.74
LINK O GLY C 182 K K D 402 1555 1555 2.75
LINK O GLY D 182 K K C 402 1555 1555 2.75
LINK O SER D 184 K K D 403 1555 1555 2.76
LINK O SER B 184 K K B 402 1555 1555 2.76
LINK O GLY B 182 K K B 404 1555 1555 2.78
LINK O GLY B 182 K K B 403 1555 1555 2.78
LINK O SER B 184 K K B 403 1555 1555 2.80
LINK O SER D 184 K K D 402 1555 1555 2.81
LINK OD1 ASN D 181 K K D 403 1555 1555 2.82
LINK OD1 ASN B 181 K K B 402 1555 1555 2.84
LINK O SER C 184 K K D 402 1555 1555 2.85
LINK OD1 ASN C 181 K K C 402 1555 1555 2.93
LINK K K D 402 O HOH D 645 1555 1555 2.53
LINK K K D 402 O HOH C 586 1555 1555 2.54
LINK K K B 403 O HOH B 515 1555 1555 2.72
LINK K K D 403 O HOH D 525 1555 1555 2.73
LINK K K C 402 O HOH C 553 1555 1555 2.77
LINK K K B 402 O HOH B 537 1555 1555 2.80
LINK K K B 402 O HOH B 665 1555 1555 3.16
CISPEP 1 GLU A 55 PRO A 56 0 -19.78
CISPEP 2 GLU B 55 PRO B 56 0 -18.91
CISPEP 3 GLU C 55 PRO C 56 0 -18.09
CISPEP 4 GLU D 55 PRO D 56 0 -19.21
SITE 1 AC1 4 TRP A 124 TRP A 164 PRO A 213 HOH A 631
SITE 1 AC2 3 TRP B 124 TRP B 164 PRO B 213
SITE 1 AC3 4 ASN B 181 SER B 184 SER B 186 HOH B 537
SITE 1 AC4 3 GLY B 182 SER B 184 HOH B 515
SITE 1 AC5 1 GLY B 182
SITE 1 AC6 3 TRP C 124 TRP C 164 PRO C 213
SITE 1 AC7 5 ASN C 181 SER C 184 SER C 186 HOH C 553
SITE 2 AC7 5 GLY D 182
SITE 1 AC8 3 TRP D 124 TRP D 164 PRO D 213
SITE 1 AC9 6 GLY C 182 SER C 184 HOH C 586 GLY D 182
SITE 2 AC9 6 SER D 184 HOH D 645
SITE 1 BC1 5 GLY C 182 ASN D 181 SER D 184 SER D 186
SITE 2 BC1 5 HOH D 525
CRYST1 84.220 79.079 95.761 90.00 92.52 90.00 P 1 21 1 8
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 0.011874 0.000000 0.000522 0.00000
SCALE2 0.000000 0.012646 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010453 0.00000
TER 2306 PRO A 302
TER 4626 ARG B 303
TER 6937 ARG C 303
TER 9255 ARG D 303
MASTER 616 0 34 65 36 0 13 610280 4 300 100
END |