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HEADER HYDROLASE 20-FEB-14 4P08
TITLE ENGINEERED THERMOSTABLE DIMERIC COCAINE ESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COCAINE ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.84;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE 3 ORGANISM_TAXID: 51612;
SOURCE 4 STRAIN: MB1;
SOURCE 5 GENE: COCE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3)
KEYWDS ESTERASE, DISULFIDE-LINKED DIMER, COCAINE, MUTANT, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.W.RODGERS,K.-M.CHOW,L.FANG,C.-G.ZHAN
REVDAT 1 16-JUL-14 4P08 0
JRNL AUTH L.FANG,K.M.CHOW,S.HOU,L.XUE,X.CHEN,D.W.RODGERS,F.ZHENG,
JRNL AUTH 2 C.G.ZHAN
JRNL TITL RATIONAL DESIGN, PREPARATION, AND CHARACTERIZATION OF A
JRNL TITL 2 THERAPEUTIC ENZYME MUTANT WITH IMPROVED STABILITY AND
JRNL TITL 3 FUNCTION FOR COCAINE DETOXIFICATION.
JRNL REF ACS CHEM.BIOL. 2014
JRNL REFN ESSN 1554-8937
JRNL PMID 24919140
JRNL DOI 10.1021/CB500257S
REMARK 2
REMARK 2 RESOLUTION. 2.34 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.28
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 30503
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1525
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 33.2838 - 5.2012 1.00 3013 159 0.1771 0.1857
REMARK 3 2 5.2012 - 4.1308 0.99 2812 147 0.1368 0.1826
REMARK 3 3 4.1308 - 3.6094 0.99 2764 147 0.1515 0.2046
REMARK 3 4 3.6094 - 3.2797 0.99 2727 142 0.1676 0.2328
REMARK 3 5 3.2797 - 3.0448 0.98 2689 142 0.1916 0.2020
REMARK 3 6 3.0448 - 2.8654 0.97 2649 141 0.1934 0.2208
REMARK 3 7 2.8654 - 2.7219 0.96 2586 140 0.1899 0.2615
REMARK 3 8 2.7219 - 2.6035 0.93 2544 126 0.1968 0.2597
REMARK 3 9 2.6035 - 2.5033 0.92 2505 129 0.2164 0.2966
REMARK 3 10 2.5033 - 2.4170 0.89 2407 127 0.2327 0.2961
REMARK 3 11 2.4170 - 2.3414 0.84 2282 125 0.2498 0.3322
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.990
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.84
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 4473
REMARK 3 ANGLE : 0.893 6114
REMARK 3 CHIRALITY : 0.062 684
REMARK 3 PLANARITY : 0.004 807
REMARK 3 DIHEDRAL : 11.991 1583
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 103 )
REMARK 3 ORIGIN FOR THE GROUP (A): 59.6931 33.8643 -4.9778
REMARK 3 T TENSOR
REMARK 3 T11: -0.0378 T22: 0.0163
REMARK 3 T33: 0.0407 T12: -0.2085
REMARK 3 T13: -0.0991 T23: -0.2574
REMARK 3 L TENSOR
REMARK 3 L11: 0.0103 L22: 0.0093
REMARK 3 L33: 0.0271 L12: 0.0067
REMARK 3 L13: 0.0040 L23: 0.0073
REMARK 3 S TENSOR
REMARK 3 S11: 0.0359 S12: -0.0130 S13: -0.0478
REMARK 3 S21: -0.0199 S22: 0.1014 S23: -0.0973
REMARK 3 S31: -0.0249 S32: 0.1768 S33: 0.1250
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 104 THROUGH 213 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.7612 21.7951 0.1091
REMARK 3 T TENSOR
REMARK 3 T11: 0.0675 T22: 0.0289
REMARK 3 T33: 0.2479 T12: -0.0016
REMARK 3 T13: -0.0936 T23: -0.0550
REMARK 3 L TENSOR
REMARK 3 L11: 0.0864 L22: 0.1035
REMARK 3 L33: 0.2659 L12: -0.0092
REMARK 3 L13: -0.0484 L23: 0.0570
REMARK 3 S TENSOR
REMARK 3 S11: 0.1391 S12: -0.1358 S13: -0.1621
REMARK 3 S21: -0.0005 S22: 0.1402 S23: -0.1603
REMARK 3 S31: -0.0129 S32: 0.1323 S33: 0.4708
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 214 THROUGH 535 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.4200 27.5718 0.3155
REMARK 3 T TENSOR
REMARK 3 T11: 0.0928 T22: 0.1235
REMARK 3 T33: 0.0622 T12: -0.0200
REMARK 3 T13: -0.0070 T23: 0.0237
REMARK 3 L TENSOR
REMARK 3 L11: 0.2756 L22: 0.3014
REMARK 3 L33: 0.3793 L12: 0.0145
REMARK 3 L13: 0.1511 L23: 0.1500
REMARK 3 S TENSOR
REMARK 3 S11: 0.1270 S12: -0.1831 S13: -0.0176
REMARK 3 S21: 0.0078 S22: -0.0575 S23: -0.1085
REMARK 3 S31: -0.0362 S32: -0.2168 S33: 0.2804
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 536 THROUGH 574 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.2864 17.2187 10.3504
REMARK 3 T TENSOR
REMARK 3 T11: 0.2252 T22: 0.2930
REMARK 3 T33: 0.2184 T12: -0.0923
REMARK 3 T13: -0.0504 T23: 0.0850
REMARK 3 L TENSOR
REMARK 3 L11: 0.0065 L22: 0.0160
REMARK 3 L33: 0.0257 L12: -0.0056
REMARK 3 L13: 0.0207 L23: -0.0172
REMARK 3 S TENSOR
REMARK 3 S11: 0.0993 S12: -0.2065 S13: -0.1063
REMARK 3 S21: 0.1443 S22: -0.1030 S23: -0.0262
REMARK 3 S31: 0.0757 S32: -0.1741 S33: -0.0487
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4P08 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-14.
REMARK 100 THE DEPOSITION ID IS D_1000200394.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32017
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.340
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 17.50
REMARK 200 R MERGE (I) : 0.16100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 9.90
REMARK 200 R MERGE FOR SHELL (I) : 0.84500
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 (%): 57.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M PHOSPHATE-CITRATE (PH 4.2), 1.6
REMARK 280 M SODIUM DIHYDROGEN PHOSPHATE, AND 0.4 M DI-POTASSIUM HYDROGEN
REMARK 280 PHOSPHATE (JCSG IV # 94)
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 147.02133
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 73.51067
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 110.26600
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 36.75533
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 183.77667
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 147.02133
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 73.51067
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 36.75533
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 110.26600
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 183.77667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
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 BIOMT1 2 0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -36.75533
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 694 LIES ON A SPECIAL POSITION.
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 30 97.42 -69.23
REMARK 500 ASP A 45 110.21 73.78
REMARK 500 SER A 56 -92.43 -128.14
REMARK 500 PHE A 78 -121.48 55.10
REMARK 500 HIS A 87 -43.79 72.83
REMARK 500 SER A 117 -116.09 66.36
REMARK 500 TYR A 152 -108.94 -117.57
REMARK 500 ASP A 198 76.84 -151.20
REMARK 500 LEU A 213 -71.24 -80.38
REMARK 500 ILE A 218 85.69 -150.23
REMARK 500 ASP A 277 99.89 -66.69
REMARK 500 PRO A 284 37.21 -86.95
REMARK 500 GLU A 325 89.99 -67.11
REMARK 500 TYR A 358 98.62 -68.15
REMARK 500 THR A 371 168.31 64.55
REMARK 500 ASN A 413 52.02 -147.40
REMARK 500 LEU A 476 -77.51 -110.57
REMARK 500 LEU A 508 -122.98 57.56
REMARK 500 SER A 525 -159.81 -152.51
REMARK 500 ASN A 528 80.05 -161.57
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4P08 A 4 574 UNP Q9L9D7 COCE_RHOSM 4 574
SEQADV 4P08 ARG A 172 UNP Q9L9D7 THR 172 ENGINEERED MUTATION
SEQADV 4P08 GLN A 173 UNP Q9L9D7 GLY 173 ENGINEERED MUTATION
SEQADV 4P08 CYS A 196 UNP Q9L9D7 LEU 196 ENGINEERED MUTATION
SEQADV 4P08 CYS A 301 UNP Q9L9D7 ILE 301 ENGINEERED MUTATION
SEQRES 1 A 571 GLY ASN TYR SER VAL ALA SER ASN VAL MET VAL PRO MET
SEQRES 2 A 571 ARG ASP GLY VAL ARG LEU ALA VAL ASP LEU TYR ARG PRO
SEQRES 3 A 571 ASP ALA ASP GLY PRO VAL PRO VAL LEU LEU VAL ARG ASN
SEQRES 4 A 571 PRO TYR ASP LYS PHE ASP VAL PHE ALA TRP SER THR GLN
SEQRES 5 A 571 SER THR ASN TRP LEU GLU PHE VAL ARG ASP GLY TYR ALA
SEQRES 6 A 571 VAL VAL ILE GLN ASP THR ARG GLY LEU PHE ALA SER GLU
SEQRES 7 A 571 GLY GLU PHE VAL PRO HIS VAL ASP ASP GLU ALA ASP ALA
SEQRES 8 A 571 GLU ASP THR LEU SER TRP ILE LEU GLU GLN ALA TRP CYS
SEQRES 9 A 571 ASP GLY ASN VAL GLY MET PHE GLY VAL SER TYR LEU GLY
SEQRES 10 A 571 VAL THR GLN TRP GLN ALA ALA VAL SER GLY VAL GLY GLY
SEQRES 11 A 571 LEU LYS ALA ILE ALA PRO SER MET ALA SER ALA ASP LEU
SEQRES 12 A 571 TYR ARG ALA PRO TRP TYR GLY PRO GLY GLY ALA LEU SER
SEQRES 13 A 571 VAL GLU ALA LEU LEU GLY TRP SER ALA LEU ILE GLY ARG
SEQRES 14 A 571 GLN LEU ILE THR SER ARG SER ASP ALA ARG PRO GLU ASP
SEQRES 15 A 571 ALA ALA ASP PHE VAL GLN LEU ALA ALA ILE CYS ASN ASP
SEQRES 16 A 571 VAL ALA GLY ALA ALA SER VAL THR PRO LEU ALA GLU GLN
SEQRES 17 A 571 PRO LEU LEU GLY ARG LEU ILE PRO TRP VAL ILE ASP GLN
SEQRES 18 A 571 VAL VAL ASP HIS PRO ASP ASN ASP GLU SER TRP GLN SER
SEQRES 19 A 571 ILE SER LEU PHE GLU ARG LEU GLY GLY LEU ALA THR PRO
SEQRES 20 A 571 ALA LEU ILE THR ALA GLY TRP TYR ASP GLY PHE VAL GLY
SEQRES 21 A 571 GLU SER LEU ARG THR PHE VAL ALA VAL LYS ASP ASN ALA
SEQRES 22 A 571 ASP ALA ARG LEU VAL VAL GLY PRO TRP SER HIS SER ASN
SEQRES 23 A 571 LEU THR GLY ARG ASN ALA ASP ARG LYS PHE GLY CYS ALA
SEQRES 24 A 571 ALA THR TYR PRO ILE GLN GLU ALA THR THR MET HIS LYS
SEQRES 25 A 571 ALA PHE PHE ASP ARG HIS LEU ARG GLY GLU THR ASP ALA
SEQRES 26 A 571 LEU ALA GLY VAL PRO LYS VAL ARG LEU PHE VAL MET GLY
SEQRES 27 A 571 ILE ASP GLU TRP ARG ASP GLU THR ASP TRP PRO LEU PRO
SEQRES 28 A 571 ASP THR ALA TYR THR PRO PHE TYR LEU GLY GLY SER GLY
SEQRES 29 A 571 ALA ALA ASN THR SER THR GLY GLY GLY THR LEU SER THR
SEQRES 30 A 571 SER ILE SER GLY THR GLU SER ALA ASP THR TYR LEU TYR
SEQRES 31 A 571 ASP PRO ALA ASP PRO VAL PRO SER LEU GLY GLY THR LEU
SEQRES 32 A 571 LEU PHE HIS ASN GLY ASP ASN GLY PRO ALA ASP GLN ARG
SEQRES 33 A 571 PRO ILE HIS ASP ARG ASP ASP VAL LEU CYS TYR SER THR
SEQRES 34 A 571 GLU VAL LEU THR ASP PRO VAL GLU VAL THR GLY THR VAL
SEQRES 35 A 571 SER ALA ARG LEU PHE VAL SER SER SER ALA VAL ASP THR
SEQRES 36 A 571 ASP PHE THR ALA LYS LEU VAL ASP VAL PHE PRO ASP GLY
SEQRES 37 A 571 ARG ALA ILE ALA LEU CYS ASP GLY ILE VAL ARG MET ARG
SEQRES 38 A 571 TYR ARG GLU THR LEU VAL ASN PRO THR LEU ILE GLU ALA
SEQRES 39 A 571 GLY GLU ILE TYR GLU VAL ALA ILE ASP MET LEU ALA THR
SEQRES 40 A 571 SER ASN VAL PHE LEU PRO GLY HIS ARG ILE MET VAL GLN
SEQRES 41 A 571 VAL SER SER SER ASN PHE PRO LYS TYR ASP ARG ASN SER
SEQRES 42 A 571 ASN THR GLY GLY VAL ILE ALA ARG GLU GLN LEU GLU GLU
SEQRES 43 A 571 MET CYS THR ALA VAL ASN ARG ILE HIS ARG GLY PRO GLU
SEQRES 44 A 571 HIS PRO SER HIS ILE VAL LEU PRO ILE ILE LYS ARG
FORMUL 2 HOH *429(H2 O)
HELIX 1 AA1 VAL A 49 THR A 54 1 6
HELIX 2 AA2 TRP A 59 ASP A 65 1 7
HELIX 3 AA3 ASP A 89 GLN A 104 1 16
HELIX 4 AA4 SER A 117 VAL A 128 1 12
HELIX 5 AA5 SER A 159 SER A 177 1 19
HELIX 6 AA6 GLU A 184 ASP A 198 1 15
HELIX 7 AA7 ASP A 198 VAL A 205 1 8
HELIX 8 AA8 LEU A 213 ILE A 218 1 6
HELIX 9 AA9 PRO A 219 GLN A 224 1 6
HELIX 10 AB1 ASP A 232 SER A 237 1 6
HELIX 11 AB2 ILE A 238 SER A 239 5 2
HELIX 12 AB3 LEU A 240 LEU A 247 5 8
HELIX 13 AB4 PHE A 261 LYS A 273 1 13
HELIX 14 AB5 GLY A 300 THR A 304 5 5
HELIX 15 AB6 PRO A 306 ARG A 323 1 18
HELIX 16 AB7 GLN A 418 HIS A 422 5 5
HELIX 17 AB8 ARG A 484 ARG A 486 5 3
HELIX 18 AB9 VAL A 541 GLU A 545 5 5
HELIX 19 AC1 GLN A 546 MET A 550 5 5
SHEET 1 AA1 6 TYR A 6 PRO A 15 0
SHEET 2 AA1 6 ARG A 21 PRO A 29 -1 O LEU A 22 N VAL A 14
SHEET 3 AA1 6 ALA A 68 ASP A 73 -1 O VAL A 69 N TYR A 27
SHEET 4 AA1 6 VAL A 35 ASN A 42 1 N LEU A 38 O VAL A 70
SHEET 5 AA1 6 CYS A 107 MET A 113 1 O ASN A 110 N VAL A 37
SHEET 6 AA1 6 LEU A 134 ALA A 136 1 O LYS A 135 N VAL A 111
SHEET 1 AA2 2 GLY A 115 VAL A 116 0
SHEET 2 AA2 2 PRO A 139 SER A 140 1 O SER A 140 N GLY A 115
SHEET 1 AA3 4 ALA A 251 TYR A 258 0
SHEET 2 AA3 4 ALA A 278 SER A 286 1 O GLY A 283 N TRP A 257
SHEET 3 AA3 4 VAL A 335 VAL A 339 1 O ARG A 336 N LEU A 280
SHEET 4 AA3 4 GLU A 344 GLU A 348 -1 O GLU A 348 N VAL A 335
SHEET 1 AA4 2 ARG A 293 ASN A 294 0
SHEET 2 AA4 2 ARG A 297 LYS A 298 -1 O ARG A 297 N ASN A 294
SHEET 1 AA5 6 THR A 377 SER A 379 0
SHEET 2 AA5 6 ALA A 357 GLY A 364 -1 N GLY A 364 O THR A 377
SHEET 3 AA5 6 HIS A 566 ILE A 572 -1 O LEU A 569 N THR A 359
SHEET 4 AA5 6 VAL A 439 SER A 452 -1 N SER A 446 O VAL A 568
SHEET 5 AA5 6 ALA A 553 ARG A 559 -1 O HIS A 558 N PHE A 450
SHEET 6 AA5 6 SER A 387 TYR A 393 -1 N ASP A 389 O ILE A 557
SHEET 1 AA6 5 THR A 377 SER A 379 0
SHEET 2 AA6 5 ALA A 357 GLY A 364 -1 N GLY A 364 O THR A 377
SHEET 3 AA6 5 HIS A 566 ILE A 572 -1 O LEU A 569 N THR A 359
SHEET 4 AA6 5 VAL A 439 SER A 452 -1 N SER A 446 O VAL A 568
SHEET 5 AA6 5 TYR A 501 PHE A 514 -1 O PHE A 514 N VAL A 439
SHEET 1 AA7 4 CYS A 429 SER A 431 0
SHEET 2 AA7 4 ARG A 519 SER A 525 -1 O VAL A 522 N TYR A 430
SHEET 3 AA7 4 ASP A 459 VAL A 467 -1 N VAL A 465 O MET A 521
SHEET 4 AA7 4 ALA A 473 ARG A 482 -1 O CYS A 477 N LEU A 464
SSBOND 1 CYS A 196 CYS A 301 1555 12554 2.04
CISPEP 1 ALA A 149 PRO A 150 0 8.93
CISPEP 2 THR A 206 PRO A 207 0 -3.17
CISPEP 3 TRP A 351 PRO A 352 0 -2.81
CISPEP 4 PHE A 529 PRO A 530 0 5.33
CRYST1 106.647 106.647 220.532 90.00 90.00 120.00 P 65 2 2 12
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 0.009377 0.005414 0.000000 0.00000
SCALE2 0.000000 0.010827 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004534 0.00000
TER 4365 ARG A 574
MASTER 343 0 0 19 29 0 0 6 4793 1 0 44
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