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HEADER HYDROLASE 21-OCT-24 9K48
TITLE BACETRIAL COCAINE ESTERASE WITH MUTATIONS T172R/G173Q/V116K/S117A/A51K
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. (STRAIN MB1 BRESLER);
SOURCE 3 ORGANISM_TAXID: 104109;
SOURCE 4 GENE: COCE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PLASMID
KEYWDS COCAINE ESTERASE, BE SPECIFICITY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHANG,J.S.TONG
REVDAT 1 18-DEC-24 9K48 0
JRNL AUTH X.CHEN,Y.ZHANG,J.TONG,P.OUYANG,X.DENG,J.ZHANG,H.LIU,Y.HU,
JRNL AUTH 2 W.YAO,J.WANG,X.WANG,S.HOU,J.YAO
JRNL TITL CATALYTIC MECHANISM, COMPUTATIONAL DESIGN, AND CRYSTAL
JRNL TITL 2 STRUCTURE OF A HIGHLY SPECIFIC AND EFFICIENT BENZOYLECGONINE
JRNL TITL 3 HYDROLASE.
JRNL REF INT.J.BIOL.MACROMOL. V. 283 37767 2024
JRNL REFN ISSN 0141-8130
JRNL PMID 39561846
JRNL DOI 10.1016/J.IJBIOMAC.2024.137767
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.19
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 35453
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.640
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 25.1890 - 5.4049 0.93 2457 147 0.1673 0.1957
REMARK 3 2 5.4049 - 4.2970 0.99 2473 148 0.1365 0.1689
REMARK 3 3 4.2970 - 3.7558 1.00 2442 146 0.1328 0.1670
REMARK 3 4 3.7558 - 3.4133 1.00 2408 143 0.1467 0.1888
REMARK 3 5 3.4133 - 3.1692 1.00 2412 145 0.1650 0.2074
REMARK 3 6 3.1692 - 2.9826 1.00 2388 143 0.1725 0.2170
REMARK 3 7 2.9826 - 2.8335 1.00 2385 142 0.1708 0.2205
REMARK 3 8 2.8335 - 2.7103 1.00 2366 141 0.1767 0.2380
REMARK 3 9 2.7103 - 2.6061 1.00 2390 144 0.1769 0.2240
REMARK 3 10 2.6061 - 2.5162 1.00 2345 140 0.1752 0.2450
REMARK 3 11 2.5162 - 2.4376 1.00 2354 141 0.1718 0.2497
REMARK 3 12 2.4376 - 2.3680 0.99 2359 140 0.1762 0.1976
REMARK 3 13 2.3680 - 2.3057 0.99 2331 140 0.1911 0.2550
REMARK 3 14 2.3057 - 2.2495 0.99 2343 140 0.1837 0.2346
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.640
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.007 4505
REMARK 3 ANGLE : 0.884 6156
REMARK 3 CHIRALITY : 0.053 688
REMARK 3 PLANARITY : 0.005 812
REMARK 3 DIHEDRAL : 14.273 2644
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 9K48 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 22-OCT-24.
REMARK 100 THE DEPOSITION ID IS D_1300052319.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JAN-22
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 : SSRF
REMARK 200 BEAMLINE : BL17B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35828
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.249
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY : 14.10
REMARK 200 R MERGE (I) : 0.26100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.99900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
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 (%): 57.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES, PH 6.5, 1.8 M AMS, 10%
REMARK 280 GLYCEROL, EVAPORATION, TEMPERATURE 292K
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 147.99800
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 73.99900
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 110.99850
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 36.99950
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 184.99750
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 147.99800
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 73.99900
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 36.99950
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 110.99850
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 184.99750
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 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 -36.99950
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 1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 1015 O HOH A 1057 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 45 107.09 81.57
REMARK 500 SER A 56 -87.97 -125.79
REMARK 500 PHE A 78 -120.47 52.31
REMARK 500 HIS A 87 -38.89 77.70
REMARK 500 ALA A 117 -119.16 62.30
REMARK 500 TYR A 152 -120.84 -119.26
REMARK 500 ASP A 198 73.61 -150.58
REMARK 500 GLN A 224 -64.10 -95.78
REMARK 500 HIS A 228 75.26 -118.86
REMARK 500 PRO A 284 35.50 -88.86
REMARK 500 ASP A 355 40.30 -106.62
REMARK 500 THR A 371 165.67 64.21
REMARK 500 ASN A 413 49.70 -148.42
REMARK 500 LEU A 476 -87.16 -111.45
REMARK 500 LEU A 508 -119.46 62.61
REMARK 500 SER A 525 -159.39 -159.62
REMARK 500 ASN A 528 82.22 -163.70
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9K48 A 1 574 UNP Q9L9D7 COCE_RHOSM 1 574
SEQADV 9K48 LYS A 51 UNP Q9L9D7 ALA 51 ENGINEERED MUTATION
SEQADV 9K48 LYS A 116 UNP Q9L9D7 VAL 116 ENGINEERED MUTATION
SEQADV 9K48 ALA A 117 UNP Q9L9D7 SER 117 ENGINEERED MUTATION
SEQADV 9K48 ARG A 172 UNP Q9L9D7 THR 172 ENGINEERED MUTATION
SEQADV 9K48 GLN A 173 UNP Q9L9D7 GLY 173 ENGINEERED MUTATION
SEQRES 1 A 574 MET VAL ASP GLY ASN TYR SER VAL ALA SER ASN VAL MET
SEQRES 2 A 574 VAL PRO MET ARG ASP GLY VAL ARG LEU ALA VAL ASP LEU
SEQRES 3 A 574 TYR ARG PRO ASP ALA ASP GLY PRO VAL PRO VAL LEU LEU
SEQRES 4 A 574 VAL ARG ASN PRO TYR ASP LYS PHE ASP VAL PHE LYS TRP
SEQRES 5 A 574 SER THR GLN SER THR ASN TRP LEU GLU PHE VAL ARG ASP
SEQRES 6 A 574 GLY TYR ALA VAL VAL ILE GLN ASP THR ARG GLY LEU PHE
SEQRES 7 A 574 ALA SER GLU GLY GLU PHE VAL PRO HIS VAL ASP ASP GLU
SEQRES 8 A 574 ALA ASP ALA GLU ASP THR LEU SER TRP ILE LEU GLU GLN
SEQRES 9 A 574 ALA TRP CYS ASP GLY ASN VAL GLY MET PHE GLY LYS ALA
SEQRES 10 A 574 TYR LEU GLY VAL THR GLN TRP GLN ALA ALA VAL SER GLY
SEQRES 11 A 574 VAL GLY GLY LEU LYS ALA ILE ALA PRO SER MET ALA SER
SEQRES 12 A 574 ALA ASP LEU TYR ARG ALA PRO TRP TYR GLY PRO GLY GLY
SEQRES 13 A 574 ALA LEU SER VAL GLU ALA LEU LEU GLY TRP SER ALA LEU
SEQRES 14 A 574 ILE GLY ARG GLN LEU ILE THR SER ARG SER ASP ALA ARG
SEQRES 15 A 574 PRO GLU ASP ALA ALA ASP PHE VAL GLN LEU ALA ALA ILE
SEQRES 16 A 574 LEU ASN ASP VAL ALA GLY ALA ALA SER VAL THR PRO LEU
SEQRES 17 A 574 ALA GLU GLN PRO LEU LEU GLY ARG LEU ILE PRO TRP VAL
SEQRES 18 A 574 ILE ASP GLN VAL VAL ASP HIS PRO ASP ASN ASP GLU SER
SEQRES 19 A 574 TRP GLN SER ILE SER LEU PHE GLU ARG LEU GLY GLY LEU
SEQRES 20 A 574 ALA THR PRO ALA LEU ILE THR ALA GLY TRP TYR ASP GLY
SEQRES 21 A 574 PHE VAL GLY GLU SER LEU ARG THR PHE VAL ALA VAL LYS
SEQRES 22 A 574 ASP ASN ALA ASP ALA ARG LEU VAL VAL GLY PRO TRP SER
SEQRES 23 A 574 HIS SER ASN LEU THR GLY ARG ASN ALA ASP ARG LYS PHE
SEQRES 24 A 574 GLY ILE ALA ALA THR TYR PRO ILE GLN GLU ALA THR THR
SEQRES 25 A 574 MET HIS LYS ALA PHE PHE ASP ARG HIS LEU ARG GLY GLU
SEQRES 26 A 574 THR ASP ALA LEU ALA GLY VAL PRO LYS VAL ARG LEU PHE
SEQRES 27 A 574 VAL MET GLY ILE ASP GLU TRP ARG ASP GLU THR ASP TRP
SEQRES 28 A 574 PRO LEU PRO ASP THR ALA TYR THR PRO PHE TYR LEU GLY
SEQRES 29 A 574 GLY SER GLY ALA ALA ASN THR SER THR GLY GLY GLY THR
SEQRES 30 A 574 LEU SER THR SER ILE SER GLY THR GLU SER ALA ASP THR
SEQRES 31 A 574 TYR LEU TYR ASP PRO ALA ASP PRO VAL PRO SER LEU GLY
SEQRES 32 A 574 GLY THR LEU LEU PHE HIS ASN GLY ASP ASN GLY PRO ALA
SEQRES 33 A 574 ASP GLN ARG PRO ILE HIS ASP ARG ASP ASP VAL LEU CYS
SEQRES 34 A 574 TYR SER THR GLU VAL LEU THR ASP PRO VAL GLU VAL THR
SEQRES 35 A 574 GLY THR VAL SER ALA ARG LEU PHE VAL SER SER SER ALA
SEQRES 36 A 574 VAL ASP THR ASP PHE THR ALA LYS LEU VAL ASP VAL PHE
SEQRES 37 A 574 PRO ASP GLY ARG ALA ILE ALA LEU CYS ASP GLY ILE VAL
SEQRES 38 A 574 ARG MET ARG TYR ARG GLU THR LEU VAL ASN PRO THR LEU
SEQRES 39 A 574 ILE GLU ALA GLY GLU ILE TYR GLU VAL ALA ILE ASP MET
SEQRES 40 A 574 LEU ALA THR SER ASN VAL PHE LEU PRO GLY HIS ARG ILE
SEQRES 41 A 574 MET VAL GLN VAL SER SER SER ASN PHE PRO LYS TYR ASP
SEQRES 42 A 574 ARG ASN SER ASN THR GLY GLY VAL ILE ALA ARG GLU GLN
SEQRES 43 A 574 LEU GLU GLU MET CYS THR ALA VAL ASN ARG ILE HIS ARG
SEQRES 44 A 574 GLY PRO GLU HIS PRO SER HIS ILE VAL LEU PRO ILE ILE
SEQRES 45 A 574 LYS ARG
HET BEZ A 601 9
HETNAM BEZ BENZOIC ACID
FORMUL 2 BEZ C7 H6 O2
FORMUL 3 HOH *450(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 ALA 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 SER A 204 1 7
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 LEU A 240 GLY A 245 1 6
HELIX 12 AB3 PHE A 261 LYS A 273 1 13
HELIX 13 AB4 GLY A 300 THR A 304 5 5
HELIX 14 AB5 PRO A 306 ARG A 323 1 18
HELIX 15 AB6 GLN A 418 HIS A 422 5 5
HELIX 16 AB7 ARG A 484 ARG A 486 5 3
HELIX 17 AB8 VAL A 541 GLU A 545 5 5
HELIX 18 AB9 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 GLY A 112 N LEU A 39
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 LYS 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 ARG A 279 N ILE A 253
SHEET 3 AA3 4 VAL A 335 VAL A 339 1 O PHE A 338 N VAL A 282
SHEET 4 AA3 4 GLU A 344 GLU A 348 -1 O GLU A 344 N VAL A 339
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 TYR A 362 O SER A 379
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 453 -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 SER A 387 O ARG A 559
SHEET 1 AA6 5 THR A 377 SER A 379 0
SHEET 2 AA6 5 ALA A 357 GLY A 364 -1 N TYR A 362 O SER A 379
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 453 -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
CISPEP 1 ALA A 149 PRO A 150 0 11.20
CISPEP 2 THR A 206 PRO A 207 0 -1.40
CISPEP 3 TRP A 351 PRO A 352 0 -7.31
CISPEP 4 PHE A 529 PRO A 530 0 5.84
CRYST1 105.959 105.959 221.997 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 0.009438 0.005449 0.000000 0.00000
SCALE2 0.000000 0.010898 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004505 0.00000
TER 4389 ARG A 574
MASTER 298 0 1 18 29 0 0 6 4847 1 9 45
END |