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HEADER HYDROLASE 08-MAR-24 8YMA
TITLE CRYSTAL STRUCTURE OF A NOVEL PU PLASTIC DEGRADATION ENZYME FROM
TITLE 2 THERMAEROBACTER MARIANENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLIC ESTER HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: THE SEQUENCE OF ORGANISM THERMAEROBACTER MARIANENSIS
COMPND 7 IS NOT AVAILABLE, REPLACED BY E6SHQ4 TEMPORARILY.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMAEROBACTER MARIANENSIS;
SOURCE 3 ORGANISM_TAXID: 73919;
SOURCE 4 GENE: TMAR_0630;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS PU PLASTIC, DEGRADATION, CATALYSIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.S.LI,H.WANG,J.GAO,Y.Y.CHEN,H.L.WEI,X.HAN,R.WEI,U.T.BORNSCHEUER,
AUTHOR 2 W.D.LIU
REVDAT 1 12-MAR-25 8YMA 0
JRNL AUTH Z.S.LI,H.WANG,J.GAO,Y.Y.CHEN,H.L.WEI,X.HAN,R.WEI,
JRNL AUTH 2 U.T.BORNSCHEUER,W.D.LIU
JRNL TITL CRYSTAL STRUCTURE OF A NOVEL PU PLASTIC DEGRADATION ENZYME
JRNL TITL 2 FROM THERMAEROBACTER MARIANENSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.07 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0425
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.07
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 145412
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7698
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.07
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.12
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10676
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.1990
REMARK 3 BIN FREE R VALUE SET COUNT : 581
REMARK 3 BIN FREE R VALUE : 0.2860
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14893
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 479
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 11.84000
REMARK 3 B22 (A**2) : 11.84000
REMARK 3 B33 (A**2) : -23.68000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.035
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.033
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.089
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.063
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15311 ; 0.010 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 14325 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 20931 ; 1.510 ; 1.814
REMARK 3 BOND ANGLES OTHERS (DEGREES): 32697 ; 0.523 ; 1.732
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1977 ; 6.491 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 175 ;11.860 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2091 ;18.607 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2250 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 19202 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 3806 ; 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): 7920 ; 6.407 ; 5.066
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 7919 ; 6.407 ; 5.066
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9893 ; 8.718 ; 9.117
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 9894 ; 8.718 ; 9.117
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7391 ; 5.964 ; 5.183
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 7388 ; 5.962 ; 5.183
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 11033 ; 8.100 ; 9.460
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 67633 ;12.901 ;61.070
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 67453 ;12.897 ;61.120
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 8YMA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 12-MAR-24.
REMARK 100 THE DEPOSITION ID IS D_1300045901.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-SEP-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL10U2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 153365
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.070
REMARK 200 RESOLUTION RANGE LOW (A) : 48.590
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 21.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 21.30
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M (NH4)2HPO4, 0.1M IMIDAZOLE PH
REMARK 280 8.0, 0.2M NACL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 222.45700
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 444.91400
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 333.68550
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 556.14250
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 111.22850
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 MET A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 GLU A 1
REMARK 465 ASN A 2
REMARK 465 LEU A 3
REMARK 465 TYR A 4
REMARK 465 PHE A 5
REMARK 465 GLN A 6
REMARK 465 GLY A 7
REMARK 465 ALA A 8
REMARK 465 GLY A 9
REMARK 465 ALA A 10
REMARK 465 GLY A 11
REMARK 465 ALA A 12
REMARK 465 GLY A 13
REMARK 465 ALA A 14
REMARK 465 GLY A 15
REMARK 465 ALA A 16
REMARK 465 MET A 17
REMARK 465 ALA A 18
REMARK 465 THR A 19
REMARK 465 ALA A 20
REMARK 465 ARG A 21
REMARK 465 ALA A 516
REMARK 465 GLY A 517
REMARK 465 VAL A 518
REMARK 465 GLY A 519
REMARK 465 ALA A 520
REMARK 465 MET B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 GLU B 1
REMARK 465 ASN B 2
REMARK 465 LEU B 3
REMARK 465 TYR B 4
REMARK 465 PHE B 5
REMARK 465 GLN B 6
REMARK 465 GLY B 7
REMARK 465 ALA B 8
REMARK 465 GLY B 9
REMARK 465 ALA B 10
REMARK 465 GLY B 11
REMARK 465 ALA B 12
REMARK 465 GLY B 13
REMARK 465 ALA B 14
REMARK 465 GLY B 15
REMARK 465 ALA B 16
REMARK 465 MET B 17
REMARK 465 ALA B 18
REMARK 465 THR B 19
REMARK 465 ALA B 20
REMARK 465 ARG B 21
REMARK 465 ALA B 520
REMARK 465 MET C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 HIS C 0
REMARK 465 GLU C 1
REMARK 465 ASN C 2
REMARK 465 LEU C 3
REMARK 465 TYR C 4
REMARK 465 PHE C 5
REMARK 465 GLN C 6
REMARK 465 GLY C 7
REMARK 465 ALA C 8
REMARK 465 GLY C 9
REMARK 465 ALA C 10
REMARK 465 GLY C 11
REMARK 465 ALA C 12
REMARK 465 GLY C 13
REMARK 465 ALA C 14
REMARK 465 GLY C 15
REMARK 465 ALA C 16
REMARK 465 MET C 17
REMARK 465 ALA C 18
REMARK 465 THR C 19
REMARK 465 ALA C 20
REMARK 465 ARG C 21
REMARK 465 GLU C 22
REMARK 465 ALA C 516
REMARK 465 GLY C 517
REMARK 465 VAL C 518
REMARK 465 GLY C 519
REMARK 465 ALA C 520
REMARK 465 MET D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 HIS D -1
REMARK 465 HIS D 0
REMARK 465 GLU D 1
REMARK 465 ASN D 2
REMARK 465 LEU D 3
REMARK 465 TYR D 4
REMARK 465 PHE D 5
REMARK 465 GLN D 6
REMARK 465 GLY D 7
REMARK 465 ALA D 8
REMARK 465 GLY D 9
REMARK 465 ALA D 10
REMARK 465 GLY D 11
REMARK 465 ALA D 12
REMARK 465 GLY D 13
REMARK 465 ALA D 14
REMARK 465 GLY D 15
REMARK 465 ALA D 16
REMARK 465 MET D 17
REMARK 465 ALA D 18
REMARK 465 THR D 19
REMARK 465 ALA D 20
REMARK 465 ARG D 21
REMARK 465 VAL D 518
REMARK 465 GLY D 519
REMARK 465 ALA D 520
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 31 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 89 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 90 CG CD1 CD2
REMARK 470 GLU A 176 CG CD OE1 OE2
REMARK 470 GLN A 263 CG CD OE1 NE2
REMARK 470 ARG A 272 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 294 CG CD1 CD2
REMARK 470 GLU A 367 CG CD OE1 OE2
REMARK 470 ARG A 403 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 488 CG CD OE1 OE2
REMARK 470 GLU A 511 CG CD OE1 OE2
REMARK 470 ARG B 89 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 91 CG1 CG2 CD1
REMARK 470 LEU B 94 CG CD1 CD2
REMARK 470 ARG B 364 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 176 CG CD OE1 OE2
REMARK 470 ARG C 196 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 231 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 268 CG CD OE1 OE2
REMARK 470 ARG C 276 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 294 CG CD1 CD2
REMARK 470 ARG D 89 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 94 CG CD1 CD2
REMARK 470 ASP D 345 CG OD1 OD2
REMARK 470 ASP D 346 CG OD1 OD2
REMARK 470 ARG D 351 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 364 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 372 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 440 CG OD1 OD2
REMARK 470 ARG D 446 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 ASP A 88 71.53 32.39
REMARK 500 ARG A 208 77.03 -115.92
REMARK 500 SER A 215 -123.82 59.73
REMARK 500 THR A 303 -76.83 -115.58
REMARK 500 PHE A 390 -52.72 -120.41
REMARK 500 ALA A 429 -2.48 82.49
REMARK 500 SER B 215 -124.47 61.80
REMARK 500 THR B 303 -80.32 -114.28
REMARK 500 PHE B 390 -54.51 -121.93
REMARK 500 ALA B 429 -7.75 87.76
REMARK 500 SER C 215 -122.33 59.28
REMARK 500 THR C 303 -77.46 -114.66
REMARK 500 PHE C 390 -58.28 -121.33
REMARK 500 ALA C 429 -1.86 81.47
REMARK 500 GLU C 488 -79.34 -72.55
REMARK 500 SER D 215 -122.65 61.86
REMARK 500 THR D 303 -78.46 -115.49
REMARK 500 ALA D 429 -2.10 83.36
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 A 714 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH A 715 DISTANCE = 7.39 ANGSTROMS
REMARK 525 HOH A 716 DISTANCE = 24.58 ANGSTROMS
REMARK 525 HOH B 717 DISTANCE = 6.52 ANGSTROMS
REMARK 525 HOH C 825 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH C 826 DISTANCE = 6.72 ANGSTROMS
REMARK 525 HOH D 720 DISTANCE = 7.98 ANGSTROMS
DBREF 8YMA A 17 520 UNP E6SHQ4 E6SHQ4_THEM7 1 504
DBREF 8YMA B 17 520 UNP E6SHQ4 E6SHQ4_THEM7 1 504
DBREF 8YMA C 17 520 UNP E6SHQ4 E6SHQ4_THEM7 1 504
DBREF 8YMA D 17 520 UNP E6SHQ4 E6SHQ4_THEM7 1 504
SEQADV 8YMA MET A -6 UNP E6SHQ4 INITIATING METHIONINE
SEQADV 8YMA HIS A -5 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA HIS A -4 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA HIS A -3 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA HIS A -2 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA HIS A -1 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA HIS A 0 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLU A 1 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ASN A 2 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA LEU A 3 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA TYR A 4 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA PHE A 5 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLN A 6 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLY A 7 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ALA A 8 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLY A 9 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ALA A 10 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLY A 11 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ALA A 12 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLY A 13 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ALA A 14 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLY A 15 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ALA A 16 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA MET B -6 UNP E6SHQ4 INITIATING METHIONINE
SEQADV 8YMA HIS B -5 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA HIS B -4 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA HIS B -3 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA HIS B -2 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA HIS B -1 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA HIS B 0 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLU B 1 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ASN B 2 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA LEU B 3 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA TYR B 4 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA PHE B 5 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLN B 6 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLY B 7 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ALA B 8 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLY B 9 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ALA B 10 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLY B 11 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ALA B 12 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLY B 13 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ALA B 14 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLY B 15 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ALA B 16 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA MET C -6 UNP E6SHQ4 INITIATING METHIONINE
SEQADV 8YMA HIS C -5 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA HIS C -4 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA HIS C -3 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA HIS C -2 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA HIS C -1 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA HIS C 0 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLU C 1 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ASN C 2 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA LEU C 3 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA TYR C 4 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA PHE C 5 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLN C 6 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLY C 7 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ALA C 8 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLY C 9 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ALA C 10 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLY C 11 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ALA C 12 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLY C 13 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ALA C 14 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLY C 15 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ALA C 16 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA MET D -6 UNP E6SHQ4 INITIATING METHIONINE
SEQADV 8YMA HIS D -5 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA HIS D -4 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA HIS D -3 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA HIS D -2 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA HIS D -1 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA HIS D 0 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLU D 1 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ASN D 2 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA LEU D 3 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA TYR D 4 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA PHE D 5 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLN D 6 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLY D 7 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ALA D 8 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLY D 9 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ALA D 10 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLY D 11 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ALA D 12 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLY D 13 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ALA D 14 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA GLY D 15 UNP E6SHQ4 EXPRESSION TAG
SEQADV 8YMA ALA D 16 UNP E6SHQ4 EXPRESSION TAG
SEQRES 1 A 527 MET HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN
SEQRES 2 A 527 GLY ALA GLY ALA GLY ALA GLY ALA GLY ALA MET ALA THR
SEQRES 3 A 527 ALA ARG GLU LEU HIS ASP VAL ILE VAL GLU THR ARG TYR
SEQRES 4 A 527 GLY ALA VAL ARG GLY ARG SER ASP GLY THR VAL CYS VAL
SEQRES 5 A 527 TRP LYS GLY VAL PRO PHE ALA ARG PRO PRO VAL GLY PRO
SEQRES 6 A 527 LEU ARG PHE ARG PRO PRO GLU PRO PRO GLU PRO TRP SER
SEQRES 7 A 527 GLY VAL ARG ASP ALA THR ARG PHE GLY PRO ALA SER VAL
SEQRES 8 A 527 GLN PRO GLU ASP ARG LEU ILE SER ASN LEU THR GLY GLY
SEQRES 9 A 527 ALA THR LEU PRO GLN ASP GLU ASP CYS LEU TYR LEU ASN
SEQRES 10 A 527 ILE TRP SER PRO SER PRO ASP GLY ARG ARG PRO VAL MET
SEQRES 11 A 527 VAL TRP ILE HIS GLY GLY ALA TYR LEU THR GLY ALA GLY
SEQRES 12 A 527 SER ILE PRO TRP TYR ASP GLY THR ALA LEU ALA ARG GLU
SEQRES 13 A 527 GLY ASP VAL VAL VAL VAL THR LEU ASN TYR ARG LEU GLY
SEQRES 14 A 527 ALA LEU GLY PHE LEU TYR LEU GLU ASP ALA PHE GLY PRO
SEQRES 15 A 527 GLU PHE THR GLY SER GLY ASN LEU GLY ILE LEU ASP GLN
SEQRES 16 A 527 ILE ALA ALA LEU ARG TRP VAL ARG GLU ASN ILE ALA ALA
SEQRES 17 A 527 PHE GLY GLY ASP PRO ASP ARG VAL THR ILE PHE GLY GLU
SEQRES 18 A 527 SER ALA GLY ALA GLY SER VAL GLY VAL LEU LEU ALA ALA
SEQRES 19 A 527 PRO ALA ALA ARG GLY LEU PHE HIS ARG ALA ILE LEU GLN
SEQRES 20 A 527 SER GLY SER GLY ALA LEU GLY VAL ARG THR ALA ALA SER
SEQRES 21 A 527 ALA ALA ARG VAL ALA ALA ARG VAL LEU GLN HIS ALA GLY
SEQRES 22 A 527 VAL GLU PRO GLY ASP ARG GLU ALA LEU ARG SER LEU PRO
SEQRES 23 A 527 ALA ARG ALA TRP ALA ASN ALA VAL ALA ALA LEU GLY PRO
SEQRES 24 A 527 GLY LEU PRO LEU GLY PRO VAL VAL ASP GLY THR VAL LEU
SEQRES 25 A 527 PRO GLU HIS PRO MET ALA ALA LEU ALA ARG GLY ALA ALA
SEQRES 26 A 527 ARG ASP VAL ALA VAL LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 27 A 527 TYR ASN LEU PHE ALA LEU GLN ASP PRO ALA TRP LEU GLY
SEQRES 28 A 527 ASP ASP GLU ALA ALA LEU ARG GLN ARG VAL GLU ALA VAL
SEQRES 29 A 527 VAL GLY PRO ALA ALA GLY ARG LEU ILE GLU PHE TYR ARG
SEQRES 30 A 527 SER ARG GLY GLU GLY SER LEU GLY ARG ARG LEU LEU PRO
SEQRES 31 A 527 LEU MET SER TYR ALA VAL PHE VAL ARG GLY MET LEU ALA
SEQRES 32 A 527 THR ALA ASP ALA GLN ALA ARG VAL GLY ALA PRO VAL TRP
SEQRES 33 A 527 ALA TYR ARG PHE ASP PHE GLU THR PRO VAL LEU GLY GLY
SEQRES 34 A 527 VAL LEU GLY ALA CYS HIS ALA LEU GLU ILE PRO PHE VAL
SEQRES 35 A 527 PHE ASN THR LEU ASP ARG ALA GLY ALA ASP ARG PHE THR
SEQRES 36 A 527 GLY THR ALA PRO GLU ARG TYR ALA VAL ALA GLN ALA MET
SEQRES 37 A 527 HIS ARG ALA TRP ILE ALA PHE ALA ARG GLU GLY ASN PRO
SEQRES 38 A 527 GLN HIS ASP GLY LEU PRO GLU TRP PRO ARG TYR ASP LEU
SEQRES 39 A 527 GLU GLU ARG ALA VAL MET VAL PHE ALA VAL GLU PRO ARG
SEQRES 40 A 527 VAL GLU ARG ASP PRO TRP ARG ALA GLU ARG GLU VAL TRP
SEQRES 41 A 527 ALA ALA ALA GLY VAL GLY ALA
SEQRES 1 B 527 MET HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN
SEQRES 2 B 527 GLY ALA GLY ALA GLY ALA GLY ALA GLY ALA MET ALA THR
SEQRES 3 B 527 ALA ARG GLU LEU HIS ASP VAL ILE VAL GLU THR ARG TYR
SEQRES 4 B 527 GLY ALA VAL ARG GLY ARG SER ASP GLY THR VAL CYS VAL
SEQRES 5 B 527 TRP LYS GLY VAL PRO PHE ALA ARG PRO PRO VAL GLY PRO
SEQRES 6 B 527 LEU ARG PHE ARG PRO PRO GLU PRO PRO GLU PRO TRP SER
SEQRES 7 B 527 GLY VAL ARG ASP ALA THR ARG PHE GLY PRO ALA SER VAL
SEQRES 8 B 527 GLN PRO GLU ASP ARG LEU ILE SER ASN LEU THR GLY GLY
SEQRES 9 B 527 ALA THR LEU PRO GLN ASP GLU ASP CYS LEU TYR LEU ASN
SEQRES 10 B 527 ILE TRP SER PRO SER PRO ASP GLY ARG ARG PRO VAL MET
SEQRES 11 B 527 VAL TRP ILE HIS GLY GLY ALA TYR LEU THR GLY ALA GLY
SEQRES 12 B 527 SER ILE PRO TRP TYR ASP GLY THR ALA LEU ALA ARG GLU
SEQRES 13 B 527 GLY ASP VAL VAL VAL VAL THR LEU ASN TYR ARG LEU GLY
SEQRES 14 B 527 ALA LEU GLY PHE LEU TYR LEU GLU ASP ALA PHE GLY PRO
SEQRES 15 B 527 GLU PHE THR GLY SER GLY ASN LEU GLY ILE LEU ASP GLN
SEQRES 16 B 527 ILE ALA ALA LEU ARG TRP VAL ARG GLU ASN ILE ALA ALA
SEQRES 17 B 527 PHE GLY GLY ASP PRO ASP ARG VAL THR ILE PHE GLY GLU
SEQRES 18 B 527 SER ALA GLY ALA GLY SER VAL GLY VAL LEU LEU ALA ALA
SEQRES 19 B 527 PRO ALA ALA ARG GLY LEU PHE HIS ARG ALA ILE LEU GLN
SEQRES 20 B 527 SER GLY SER GLY ALA LEU GLY VAL ARG THR ALA ALA SER
SEQRES 21 B 527 ALA ALA ARG VAL ALA ALA ARG VAL LEU GLN HIS ALA GLY
SEQRES 22 B 527 VAL GLU PRO GLY ASP ARG GLU ALA LEU ARG SER LEU PRO
SEQRES 23 B 527 ALA ARG ALA TRP ALA ASN ALA VAL ALA ALA LEU GLY PRO
SEQRES 24 B 527 GLY LEU PRO LEU GLY PRO VAL VAL ASP GLY THR VAL LEU
SEQRES 25 B 527 PRO GLU HIS PRO MET ALA ALA LEU ALA ARG GLY ALA ALA
SEQRES 26 B 527 ARG ASP VAL ALA VAL LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 27 B 527 TYR ASN LEU PHE ALA LEU GLN ASP PRO ALA TRP LEU GLY
SEQRES 28 B 527 ASP ASP GLU ALA ALA LEU ARG GLN ARG VAL GLU ALA VAL
SEQRES 29 B 527 VAL GLY PRO ALA ALA GLY ARG LEU ILE GLU PHE TYR ARG
SEQRES 30 B 527 SER ARG GLY GLU GLY SER LEU GLY ARG ARG LEU LEU PRO
SEQRES 31 B 527 LEU MET SER TYR ALA VAL PHE VAL ARG GLY MET LEU ALA
SEQRES 32 B 527 THR ALA ASP ALA GLN ALA ARG VAL GLY ALA PRO VAL TRP
SEQRES 33 B 527 ALA TYR ARG PHE ASP PHE GLU THR PRO VAL LEU GLY GLY
SEQRES 34 B 527 VAL LEU GLY ALA CYS HIS ALA LEU GLU ILE PRO PHE VAL
SEQRES 35 B 527 PHE ASN THR LEU ASP ARG ALA GLY ALA ASP ARG PHE THR
SEQRES 36 B 527 GLY THR ALA PRO GLU ARG TYR ALA VAL ALA GLN ALA MET
SEQRES 37 B 527 HIS ARG ALA TRP ILE ALA PHE ALA ARG GLU GLY ASN PRO
SEQRES 38 B 527 GLN HIS ASP GLY LEU PRO GLU TRP PRO ARG TYR ASP LEU
SEQRES 39 B 527 GLU GLU ARG ALA VAL MET VAL PHE ALA VAL GLU PRO ARG
SEQRES 40 B 527 VAL GLU ARG ASP PRO TRP ARG ALA GLU ARG GLU VAL TRP
SEQRES 41 B 527 ALA ALA ALA GLY VAL GLY ALA
SEQRES 1 C 527 MET HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN
SEQRES 2 C 527 GLY ALA GLY ALA GLY ALA GLY ALA GLY ALA MET ALA THR
SEQRES 3 C 527 ALA ARG GLU LEU HIS ASP VAL ILE VAL GLU THR ARG TYR
SEQRES 4 C 527 GLY ALA VAL ARG GLY ARG SER ASP GLY THR VAL CYS VAL
SEQRES 5 C 527 TRP LYS GLY VAL PRO PHE ALA ARG PRO PRO VAL GLY PRO
SEQRES 6 C 527 LEU ARG PHE ARG PRO PRO GLU PRO PRO GLU PRO TRP SER
SEQRES 7 C 527 GLY VAL ARG ASP ALA THR ARG PHE GLY PRO ALA SER VAL
SEQRES 8 C 527 GLN PRO GLU ASP ARG LEU ILE SER ASN LEU THR GLY GLY
SEQRES 9 C 527 ALA THR LEU PRO GLN ASP GLU ASP CYS LEU TYR LEU ASN
SEQRES 10 C 527 ILE TRP SER PRO SER PRO ASP GLY ARG ARG PRO VAL MET
SEQRES 11 C 527 VAL TRP ILE HIS GLY GLY ALA TYR LEU THR GLY ALA GLY
SEQRES 12 C 527 SER ILE PRO TRP TYR ASP GLY THR ALA LEU ALA ARG GLU
SEQRES 13 C 527 GLY ASP VAL VAL VAL VAL THR LEU ASN TYR ARG LEU GLY
SEQRES 14 C 527 ALA LEU GLY PHE LEU TYR LEU GLU ASP ALA PHE GLY PRO
SEQRES 15 C 527 GLU PHE THR GLY SER GLY ASN LEU GLY ILE LEU ASP GLN
SEQRES 16 C 527 ILE ALA ALA LEU ARG TRP VAL ARG GLU ASN ILE ALA ALA
SEQRES 17 C 527 PHE GLY GLY ASP PRO ASP ARG VAL THR ILE PHE GLY GLU
SEQRES 18 C 527 SER ALA GLY ALA GLY SER VAL GLY VAL LEU LEU ALA ALA
SEQRES 19 C 527 PRO ALA ALA ARG GLY LEU PHE HIS ARG ALA ILE LEU GLN
SEQRES 20 C 527 SER GLY SER GLY ALA LEU GLY VAL ARG THR ALA ALA SER
SEQRES 21 C 527 ALA ALA ARG VAL ALA ALA ARG VAL LEU GLN HIS ALA GLY
SEQRES 22 C 527 VAL GLU PRO GLY ASP ARG GLU ALA LEU ARG SER LEU PRO
SEQRES 23 C 527 ALA ARG ALA TRP ALA ASN ALA VAL ALA ALA LEU GLY PRO
SEQRES 24 C 527 GLY LEU PRO LEU GLY PRO VAL VAL ASP GLY THR VAL LEU
SEQRES 25 C 527 PRO GLU HIS PRO MET ALA ALA LEU ALA ARG GLY ALA ALA
SEQRES 26 C 527 ARG ASP VAL ALA VAL LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 27 C 527 TYR ASN LEU PHE ALA LEU GLN ASP PRO ALA TRP LEU GLY
SEQRES 28 C 527 ASP ASP GLU ALA ALA LEU ARG GLN ARG VAL GLU ALA VAL
SEQRES 29 C 527 VAL GLY PRO ALA ALA GLY ARG LEU ILE GLU PHE TYR ARG
SEQRES 30 C 527 SER ARG GLY GLU GLY SER LEU GLY ARG ARG LEU LEU PRO
SEQRES 31 C 527 LEU MET SER TYR ALA VAL PHE VAL ARG GLY MET LEU ALA
SEQRES 32 C 527 THR ALA ASP ALA GLN ALA ARG VAL GLY ALA PRO VAL TRP
SEQRES 33 C 527 ALA TYR ARG PHE ASP PHE GLU THR PRO VAL LEU GLY GLY
SEQRES 34 C 527 VAL LEU GLY ALA CYS HIS ALA LEU GLU ILE PRO PHE VAL
SEQRES 35 C 527 PHE ASN THR LEU ASP ARG ALA GLY ALA ASP ARG PHE THR
SEQRES 36 C 527 GLY THR ALA PRO GLU ARG TYR ALA VAL ALA GLN ALA MET
SEQRES 37 C 527 HIS ARG ALA TRP ILE ALA PHE ALA ARG GLU GLY ASN PRO
SEQRES 38 C 527 GLN HIS ASP GLY LEU PRO GLU TRP PRO ARG TYR ASP LEU
SEQRES 39 C 527 GLU GLU ARG ALA VAL MET VAL PHE ALA VAL GLU PRO ARG
SEQRES 40 C 527 VAL GLU ARG ASP PRO TRP ARG ALA GLU ARG GLU VAL TRP
SEQRES 41 C 527 ALA ALA ALA GLY VAL GLY ALA
SEQRES 1 D 527 MET HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN
SEQRES 2 D 527 GLY ALA GLY ALA GLY ALA GLY ALA GLY ALA MET ALA THR
SEQRES 3 D 527 ALA ARG GLU LEU HIS ASP VAL ILE VAL GLU THR ARG TYR
SEQRES 4 D 527 GLY ALA VAL ARG GLY ARG SER ASP GLY THR VAL CYS VAL
SEQRES 5 D 527 TRP LYS GLY VAL PRO PHE ALA ARG PRO PRO VAL GLY PRO
SEQRES 6 D 527 LEU ARG PHE ARG PRO PRO GLU PRO PRO GLU PRO TRP SER
SEQRES 7 D 527 GLY VAL ARG ASP ALA THR ARG PHE GLY PRO ALA SER VAL
SEQRES 8 D 527 GLN PRO GLU ASP ARG LEU ILE SER ASN LEU THR GLY GLY
SEQRES 9 D 527 ALA THR LEU PRO GLN ASP GLU ASP CYS LEU TYR LEU ASN
SEQRES 10 D 527 ILE TRP SER PRO SER PRO ASP GLY ARG ARG PRO VAL MET
SEQRES 11 D 527 VAL TRP ILE HIS GLY GLY ALA TYR LEU THR GLY ALA GLY
SEQRES 12 D 527 SER ILE PRO TRP TYR ASP GLY THR ALA LEU ALA ARG GLU
SEQRES 13 D 527 GLY ASP VAL VAL VAL VAL THR LEU ASN TYR ARG LEU GLY
SEQRES 14 D 527 ALA LEU GLY PHE LEU TYR LEU GLU ASP ALA PHE GLY PRO
SEQRES 15 D 527 GLU PHE THR GLY SER GLY ASN LEU GLY ILE LEU ASP GLN
SEQRES 16 D 527 ILE ALA ALA LEU ARG TRP VAL ARG GLU ASN ILE ALA ALA
SEQRES 17 D 527 PHE GLY GLY ASP PRO ASP ARG VAL THR ILE PHE GLY GLU
SEQRES 18 D 527 SER ALA GLY ALA GLY SER VAL GLY VAL LEU LEU ALA ALA
SEQRES 19 D 527 PRO ALA ALA ARG GLY LEU PHE HIS ARG ALA ILE LEU GLN
SEQRES 20 D 527 SER GLY SER GLY ALA LEU GLY VAL ARG THR ALA ALA SER
SEQRES 21 D 527 ALA ALA ARG VAL ALA ALA ARG VAL LEU GLN HIS ALA GLY
SEQRES 22 D 527 VAL GLU PRO GLY ASP ARG GLU ALA LEU ARG SER LEU PRO
SEQRES 23 D 527 ALA ARG ALA TRP ALA ASN ALA VAL ALA ALA LEU GLY PRO
SEQRES 24 D 527 GLY LEU PRO LEU GLY PRO VAL VAL ASP GLY THR VAL LEU
SEQRES 25 D 527 PRO GLU HIS PRO MET ALA ALA LEU ALA ARG GLY ALA ALA
SEQRES 26 D 527 ARG ASP VAL ALA VAL LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 27 D 527 TYR ASN LEU PHE ALA LEU GLN ASP PRO ALA TRP LEU GLY
SEQRES 28 D 527 ASP ASP GLU ALA ALA LEU ARG GLN ARG VAL GLU ALA VAL
SEQRES 29 D 527 VAL GLY PRO ALA ALA GLY ARG LEU ILE GLU PHE TYR ARG
SEQRES 30 D 527 SER ARG GLY GLU GLY SER LEU GLY ARG ARG LEU LEU PRO
SEQRES 31 D 527 LEU MET SER TYR ALA VAL PHE VAL ARG GLY MET LEU ALA
SEQRES 32 D 527 THR ALA ASP ALA GLN ALA ARG VAL GLY ALA PRO VAL TRP
SEQRES 33 D 527 ALA TYR ARG PHE ASP PHE GLU THR PRO VAL LEU GLY GLY
SEQRES 34 D 527 VAL LEU GLY ALA CYS HIS ALA LEU GLU ILE PRO PHE VAL
SEQRES 35 D 527 PHE ASN THR LEU ASP ARG ALA GLY ALA ASP ARG PHE THR
SEQRES 36 D 527 GLY THR ALA PRO GLU ARG TYR ALA VAL ALA GLN ALA MET
SEQRES 37 D 527 HIS ARG ALA TRP ILE ALA PHE ALA ARG GLU GLY ASN PRO
SEQRES 38 D 527 GLN HIS ASP GLY LEU PRO GLU TRP PRO ARG TYR ASP LEU
SEQRES 39 D 527 GLU GLU ARG ALA VAL MET VAL PHE ALA VAL GLU PRO ARG
SEQRES 40 D 527 VAL GLU ARG ASP PRO TRP ARG ALA GLU ARG GLU VAL TRP
SEQRES 41 D 527 ALA ALA ALA GLY VAL GLY ALA
HET SO4 C 601 5
HETNAM SO4 SULFATE ION
FORMUL 5 SO4 O4 S 2-
FORMUL 6 HOH *479(H2 O)
HELIX 1 AA1 VAL A 56 ARG A 60 5 5
HELIX 2 AA2 ARG A 89 THR A 95 1 7
HELIX 3 AA3 ILE A 138 ASP A 142 5 5
HELIX 4 AA4 GLY A 143 ASP A 151 1 9
HELIX 5 AA5 LEU A 161 LEU A 167 1 7
HELIX 6 AA6 LEU A 169 GLY A 174 1 6
HELIX 7 AA7 PRO A 175 THR A 178 5 4
HELIX 8 AA8 GLY A 179 GLY A 181 5 3
HELIX 9 AA9 ASN A 182 ILE A 199 1 18
HELIX 10 AB1 ALA A 200 PHE A 202 5 3
HELIX 11 AB2 SER A 215 ALA A 227 1 13
HELIX 12 AB3 PRO A 228 ARG A 231 5 4
HELIX 13 AB4 ALA A 251 GLY A 266 1 16
HELIX 14 AB5 ASP A 271 LEU A 278 1 8
HELIX 15 AB6 PRO A 279 GLY A 291 1 13
HELIX 16 AB7 HIS A 308 GLY A 316 1 9
HELIX 17 AB8 ASP A 330 GLN A 338 5 9
HELIX 18 AB9 ASP A 339 GLY A 344 5 6
HELIX 19 AC1 ASP A 346 GLY A 359 1 14
HELIX 20 AC2 ALA A 361 ARG A 372 1 12
HELIX 21 AC3 SER A 376 PHE A 390 1 15
HELIX 22 AC4 PHE A 390 GLY A 405 1 16
HELIX 23 AC5 PRO A 418 VAL A 423 5 6
HELIX 24 AC6 GLU A 431 ASN A 437 1 7
HELIX 25 AC7 GLY A 443 GLY A 449 1 7
HELIX 26 AC8 PRO A 452 GLY A 472 1 21
HELIX 27 AC9 TRP A 506 ALA A 515 1 10
HELIX 28 AD1 VAL B 56 ARG B 60 5 5
HELIX 29 AD2 ASP B 88 THR B 95 1 8
HELIX 30 AD3 ILE B 138 ASP B 142 5 5
HELIX 31 AD4 GLY B 143 ASP B 151 1 9
HELIX 32 AD5 GLY B 162 LEU B 167 1 6
HELIX 33 AD6 LEU B 169 GLY B 174 1 6
HELIX 34 AD7 PRO B 175 THR B 178 5 4
HELIX 35 AD8 GLY B 179 GLY B 181 5 3
HELIX 36 AD9 ASN B 182 ILE B 199 1 18
HELIX 37 AE1 ALA B 200 PHE B 202 5 3
HELIX 38 AE2 SER B 215 ALA B 227 1 13
HELIX 39 AE3 PRO B 228 ARG B 231 5 4
HELIX 40 AE4 ALA B 251 GLY B 266 1 16
HELIX 41 AE5 ASP B 271 LEU B 278 1 8
HELIX 42 AE6 PRO B 279 ALA B 289 1 11
HELIX 43 AE7 HIS B 308 ARG B 315 1 8
HELIX 44 AE8 ASP B 330 GLN B 338 5 9
HELIX 45 AE9 ASP B 339 GLY B 344 5 6
HELIX 46 AF1 ASP B 346 GLY B 359 1 14
HELIX 47 AF2 ALA B 361 ARG B 372 1 12
HELIX 48 AF3 SER B 376 PHE B 390 1 15
HELIX 49 AF4 PHE B 390 GLY B 405 1 16
HELIX 50 AF5 PRO B 418 VAL B 423 5 6
HELIX 51 AF6 GLU B 431 ASN B 437 1 7
HELIX 52 AF7 GLY B 443 GLY B 449 1 7
HELIX 53 AF8 GLU B 453 GLY B 472 1 20
HELIX 54 AF9 TRP B 506 ALA B 516 1 11
HELIX 55 AG1 VAL C 56 ARG C 60 5 5
HELIX 56 AG2 ASP C 88 GLY C 96 1 9
HELIX 57 AG3 ILE C 138 ASP C 142 5 5
HELIX 58 AG4 GLY C 143 ASP C 151 1 9
HELIX 59 AG5 LEU C 161 LEU C 167 1 7
HELIX 60 AG6 LEU C 169 GLY C 174 1 6
HELIX 61 AG7 PRO C 175 THR C 178 5 4
HELIX 62 AG8 GLY C 179 GLY C 181 5 3
HELIX 63 AG9 ASN C 182 ILE C 199 1 18
HELIX 64 AH1 ALA C 200 PHE C 202 5 3
HELIX 65 AH2 SER C 215 ALA C 227 1 13
HELIX 66 AH3 PRO C 228 ARG C 231 5 4
HELIX 67 AH4 ALA C 251 GLY C 266 1 16
HELIX 68 AH5 ASP C 271 LEU C 278 1 8
HELIX 69 AH6 PRO C 279 GLY C 291 1 13
HELIX 70 AH7 HIS C 308 GLY C 316 1 9
HELIX 71 AH8 ASP C 330 GLN C 338 5 9
HELIX 72 AH9 ASP C 339 LEU C 343 5 5
HELIX 73 AI1 ASP C 346 GLY C 359 1 14
HELIX 74 AI2 ALA C 361 ARG C 372 1 12
HELIX 75 AI3 SER C 376 PHE C 390 1 15
HELIX 76 AI4 PHE C 390 GLY C 405 1 16
HELIX 77 AI5 PRO C 418 VAL C 423 5 6
HELIX 78 AI6 GLU C 431 ASN C 437 1 7
HELIX 79 AI7 GLY C 443 GLY C 449 1 7
HELIX 80 AI8 GLU C 453 GLY C 472 1 20
HELIX 81 AI9 TRP C 506 ALA C 515 1 10
HELIX 82 AJ1 VAL D 56 ARG D 60 5 5
HELIX 83 AJ2 ASP D 88 THR D 95 1 8
HELIX 84 AJ3 ILE D 138 ASP D 142 5 5
HELIX 85 AJ4 GLY D 143 ASP D 151 1 9
HELIX 86 AJ5 GLY D 162 LEU D 167 1 6
HELIX 87 AJ6 LEU D 169 GLY D 174 1 6
HELIX 88 AJ7 PRO D 175 THR D 178 5 4
HELIX 89 AJ8 GLY D 179 GLY D 181 5 3
HELIX 90 AJ9 ASN D 182 ILE D 199 1 18
HELIX 91 AK1 ALA D 200 PHE D 202 5 3
HELIX 92 AK2 SER D 215 ALA D 227 1 13
HELIX 93 AK3 PRO D 228 ARG D 231 5 4
HELIX 94 AK4 ALA D 251 GLY D 266 1 16
HELIX 95 AK5 ASP D 271 LEU D 278 1 8
HELIX 96 AK6 PRO D 279 ALA D 289 1 11
HELIX 97 AK7 HIS D 308 GLY D 316 1 9
HELIX 98 AK8 TYR D 332 ASP D 339 1 8
HELIX 99 AK9 PRO D 340 LEU D 343 5 4
HELIX 100 AL1 GLU D 347 GLY D 359 1 13
HELIX 101 AL2 ALA D 361 ARG D 372 1 12
HELIX 102 AL3 SER D 376 PHE D 390 1 15
HELIX 103 AL4 PHE D 390 GLY D 405 1 16
HELIX 104 AL5 PRO D 418 VAL D 423 5 6
HELIX 105 AL6 GLU D 431 ASN D 437 1 7
HELIX 106 AL7 ARG D 441 GLY D 449 1 9
HELIX 107 AL8 PRO D 452 GLY D 472 1 21
HELIX 108 AL9 TRP D 506 ALA D 516 1 11
SHEET 1 AA1 3 HIS A 24 GLU A 29 0
SHEET 2 AA1 3 ALA A 34 SER A 39 -1 O GLY A 37 N VAL A 26
SHEET 3 AA1 3 VAL A 73 ASP A 75 1 O ARG A 74 N ARG A 36
SHEET 1 AA212 HIS A 24 GLU A 29 0
SHEET 2 AA212 ALA A 34 SER A 39 -1 O GLY A 37 N VAL A 26
SHEET 3 AA212 CYS A 44 PRO A 50 -1 O VAL A 45 N ARG A 38
SHEET 4 AA212 TYR A 108 SER A 113 -1 O SER A 113 N CYS A 44
SHEET 5 AA212 VAL A 153 LEU A 157 -1 O THR A 156 N ASN A 110
SHEET 6 AA212 ARG A 120 ILE A 126 1 N TRP A 125 O VAL A 155
SHEET 7 AA212 GLY A 204 GLU A 214 1 O THR A 210 N VAL A 122
SHEET 8 AA212 ARG A 236 GLN A 240 1 O ILE A 238 N ILE A 211
SHEET 9 AA212 ALA A 322 ASN A 328 1 O LEU A 324 N LEU A 239
SHEET 10 AA212 VAL A 408 PHE A 413 1 O TRP A 409 N VAL A 325
SHEET 11 AA212 ALA A 491 PHE A 495 1 O MET A 493 N ALA A 410
SHEET 12 AA212 ARG A 500 ARG A 503 -1 O ARG A 500 N VAL A 494
SHEET 1 AA3 2 ARG A 249 THR A 250 0
SHEET 2 AA3 2 VAL A 299 VAL A 300 1 O VAL A 300 N ARG A 249
SHEET 1 AA4 3 HIS B 24 GLU B 29 0
SHEET 2 AA4 3 ALA B 34 SER B 39 -1 O GLY B 37 N VAL B 26
SHEET 3 AA4 3 VAL B 73 ASP B 75 1 O ARG B 74 N ARG B 36
SHEET 1 AA512 HIS B 24 GLU B 29 0
SHEET 2 AA512 ALA B 34 SER B 39 -1 O GLY B 37 N VAL B 26
SHEET 3 AA512 CYS B 44 PRO B 50 -1 O VAL B 45 N ARG B 38
SHEET 4 AA512 TYR B 108 SER B 113 -1 O SER B 113 N CYS B 44
SHEET 5 AA512 VAL B 153 LEU B 157 -1 O THR B 156 N ASN B 110
SHEET 6 AA512 ARG B 120 ILE B 126 1 N TRP B 125 O VAL B 155
SHEET 7 AA512 GLY B 204 GLU B 214 1 O THR B 210 N VAL B 122
SHEET 8 AA512 ARG B 236 GLN B 240 1 O ILE B 238 N ILE B 211
SHEET 9 AA512 ALA B 322 ASN B 328 1 O LEU B 324 N LEU B 239
SHEET 10 AA512 VAL B 408 PHE B 413 1 O TRP B 409 N VAL B 325
SHEET 11 AA512 ALA B 491 PHE B 495 1 O PHE B 495 N ARG B 412
SHEET 12 AA512 ARG B 500 ARG B 503 -1 O GLU B 502 N VAL B 492
SHEET 1 AA6 2 ARG B 249 THR B 250 0
SHEET 2 AA6 2 VAL B 299 VAL B 300 1 O VAL B 300 N ARG B 249
SHEET 1 AA7 3 HIS C 24 GLU C 29 0
SHEET 2 AA7 3 ALA C 34 SER C 39 -1 O GLY C 37 N VAL C 26
SHEET 3 AA7 3 VAL C 73 ASP C 75 1 O ARG C 74 N ARG C 36
SHEET 1 AA812 HIS C 24 GLU C 29 0
SHEET 2 AA812 ALA C 34 SER C 39 -1 O GLY C 37 N VAL C 26
SHEET 3 AA812 CYS C 44 PRO C 50 -1 O VAL C 45 N ARG C 38
SHEET 4 AA812 TYR C 108 SER C 113 -1 O SER C 113 N CYS C 44
SHEET 5 AA812 VAL C 153 LEU C 157 -1 O THR C 156 N ASN C 110
SHEET 6 AA812 ARG C 120 ILE C 126 1 N TRP C 125 O VAL C 155
SHEET 7 AA812 GLY C 204 GLU C 214 1 O ASP C 205 N ARG C 120
SHEET 8 AA812 ARG C 236 GLN C 240 1 O ARG C 236 N ILE C 211
SHEET 9 AA812 ALA C 322 ASN C 328 1 O LEU C 324 N LEU C 239
SHEET 10 AA812 VAL C 408 PHE C 413 1 O TRP C 409 N VAL C 325
SHEET 11 AA812 ALA C 491 PHE C 495 1 O MET C 493 N ALA C 410
SHEET 12 AA812 ARG C 500 ARG C 503 -1 O ARG C 500 N VAL C 494
SHEET 1 AA9 2 ARG C 249 THR C 250 0
SHEET 2 AA9 2 VAL C 299 VAL C 300 1 O VAL C 300 N ARG C 249
SHEET 1 AB1 3 HIS D 24 GLU D 29 0
SHEET 2 AB1 3 ALA D 34 SER D 39 -1 O GLY D 37 N VAL D 26
SHEET 3 AB1 3 VAL D 73 ASP D 75 1 O ARG D 74 N ALA D 34
SHEET 1 AB212 HIS D 24 GLU D 29 0
SHEET 2 AB212 ALA D 34 SER D 39 -1 O GLY D 37 N VAL D 26
SHEET 3 AB212 CYS D 44 PRO D 50 -1 O VAL D 45 N ARG D 38
SHEET 4 AB212 TYR D 108 SER D 113 -1 O SER D 113 N CYS D 44
SHEET 5 AB212 VAL D 153 LEU D 157 -1 O THR D 156 N ASN D 110
SHEET 6 AB212 ARG D 120 ILE D 126 1 N TRP D 125 O VAL D 155
SHEET 7 AB212 GLY D 204 GLU D 214 1 O THR D 210 N VAL D 122
SHEET 8 AB212 ARG D 236 GLN D 240 1 O ILE D 238 N ILE D 211
SHEET 9 AB212 ALA D 322 ASN D 328 1 O LEU D 324 N LEU D 239
SHEET 10 AB212 VAL D 408 PHE D 413 1 O TRP D 409 N VAL D 325
SHEET 11 AB212 ALA D 491 PHE D 495 1 O MET D 493 N ALA D 410
SHEET 12 AB212 ARG D 500 ARG D 503 -1 O ARG D 500 N VAL D 494
SHEET 1 AB3 2 ARG D 249 THR D 250 0
SHEET 2 AB3 2 VAL D 299 VAL D 300 1 O VAL D 300 N ARG D 249
CRYST1 81.834 81.834 667.371 90.00 90.00 120.00 P 61 24
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 0.012220 0.007055 0.000000 0.00000
SCALE2 0.000000 0.014110 0.000000 0.00000
SCALE3 0.000000 0.000000 0.001498 0.00000
TER 3704 ALA A 515
TER 7460 GLY B 519
TER 11176 ALA C 515
TER 14897 GLY D 517
MASTER 487 0 1 108 68 0 0 615377 4 5 164
END |