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HEADER HYDROLASE 24-JUN-21 7F65
TITLE BACETRIAL COCAINE ESTERASE WITH MUTATIONS
TITLE 2 T172R/G173Q/V116K/S117A/A51L, BOUND TO BENZOIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COCAINE ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: COCAINE ESTERASE;
COMPND 5 EC: 3.1.1.84;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP. MB1 'BRESLER 1999';
SOURCE 3 ORGANISM_TAXID: 104109;
SOURCE 4 STRAIN: MB1 BRESLER;
SOURCE 5 GENE: COCE;
SOURCE 6 EXPRESSION_SYSTEM: RHODOCOCCUS SP. MB1;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 51612
KEYWDS COCAINE ESTERASE, MUTANTIONS, BENZOYLECGONINE METABOLISM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.F.OUYANG,Y.ZHANG,J.TONG
REVDAT 1 15-SEP-21 7F65 0
JRNL AUTH X.CHEN,X.DENG,Y.ZHANG,Y.WU,K.YANG,Q.LI,J.WANG,W.YAO,J.TONG,
JRNL AUTH 2 T.XIE,S.HOU,J.YAO
JRNL TITL COMPUTATIONAL DESIGN AND CRYSTAL STRUCTURE OF A HIGHLY
JRNL TITL 2 EFFICIENT BENZOYLECGONINE HYDROLASE.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. 2021
JRNL REFN ESSN 1521-3773
JRNL PMID 34351032
JRNL DOI 10.1002/ANIE.202108559
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.08
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 38084
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.250
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 24.0830 - 5.2891 0.98 2771 154 0.1624 0.2076
REMARK 3 2 5.2891 - 4.2054 1.00 2654 147 0.1402 0.1602
REMARK 3 3 4.2054 - 3.6759 1.00 2609 144 0.1480 0.1687
REMARK 3 4 3.6759 - 3.3408 1.00 2590 144 0.1650 0.1880
REMARK 3 5 3.3408 - 3.1019 1.00 2585 143 0.1796 0.2381
REMARK 3 6 3.1019 - 2.9193 1.00 2568 143 0.1903 0.2427
REMARK 3 7 2.9193 - 2.7733 1.00 2557 141 0.1849 0.1967
REMARK 3 8 2.7733 - 2.6528 1.00 2541 141 0.1889 0.2270
REMARK 3 9 2.6528 - 2.5508 1.00 2550 141 0.1930 0.2634
REMARK 3 10 2.5508 - 2.4628 1.00 2542 142 0.1922 0.2441
REMARK 3 11 2.4628 - 2.3859 1.00 2536 140 0.1913 0.2484
REMARK 3 12 2.3859 - 2.3178 1.00 2541 140 0.1979 0.2227
REMARK 3 13 2.3178 - 2.2568 1.00 2514 140 0.1894 0.2083
REMARK 3 14 2.2568 - 2.2020 1.00 2526 140 0.2031 0.2674
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.720
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.72
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.68
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 : 0.006 4508
REMARK 3 ANGLE : 0.853 6162
REMARK 3 CHIRALITY : 0.053 689
REMARK 3 PLANARITY : 0.005 812
REMARK 3 DIHEDRAL : 13.766 2642
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 37.0389 26.7890 -0.2906
REMARK 3 T TENSOR
REMARK 3 T11: 0.1335 T22: 0.1072
REMARK 3 T33: 0.1223 T12: 0.0059
REMARK 3 T13: -0.0152 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.2703 L22: 0.2493
REMARK 3 L33: 0.3337 L12: 0.1208
REMARK 3 L13: -0.0780 L23: -0.0151
REMARK 3 S TENSOR
REMARK 3 S11: 0.0200 S12: -0.0456 S13: -0.0064
REMARK 3 S21: 0.0301 S22: -0.0016 S23: -0.0357
REMARK 3 S31: -0.0121 S32: 0.0051 S33: -0.0000
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 7F65 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-JUN-21.
REMARK 100 THE DEPOSITION ID IS D_1300022964.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUN-21
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) : 0.987
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-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38298
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 33.70
REMARK 200 R MERGE (I) : 0.31600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 1.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 21.20
REMARK 200 R MERGE FOR SHELL (I) : 1.10400
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 2.6.0
REMARK 200 STARTING MODEL: 1JU4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 1.75 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 148.18933
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 74.09467
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 111.14200
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 37.04733
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 185.23667
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 148.18933
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 74.09467
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 37.04733
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 111.14200
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 185.23667
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 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: 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 45 106.02 80.74
REMARK 500 SER A 56 -84.85 -130.98
REMARK 500 PHE A 78 -117.73 52.26
REMARK 500 HIS A 87 -40.33 76.23
REMARK 500 ALA A 117 -118.21 61.52
REMARK 500 ALA A 136 149.97 -170.38
REMARK 500 TYR A 152 -116.35 -118.55
REMARK 500 SER A 179 -79.50 -41.81
REMARK 500 ASP A 198 72.51 -153.55
REMARK 500 GLN A 224 -63.69 -97.63
REMARK 500 PRO A 284 36.63 -88.21
REMARK 500 ASP A 355 40.70 -109.85
REMARK 500 THR A 371 166.40 64.01
REMARK 500 ASN A 413 51.79 -146.29
REMARK 500 LEU A 476 -88.31 -108.42
REMARK 500 LEU A 508 -123.08 59.14
REMARK 500 ASN A 528 83.30 -163.78
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7F65 A 1 574 UNP Q9L9D7 COCE_RHOSM 1 574
SEQADV 7F65 LEU A 51 UNP Q9L9D7 ALA 51 ENGINEERED MUTATION
SEQADV 7F65 LYS A 116 UNP Q9L9D7 VAL 116 ENGINEERED MUTATION
SEQADV 7F65 ALA A 117 UNP Q9L9D7 SER 117 ENGINEERED MUTATION
SEQADV 7F65 ARG A 172 UNP Q9L9D7 THR 172 ENGINEERED MUTATION
SEQADV 7F65 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 LEU 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 SO4 A 601 5
HET BEZ A 602 9
HETNAM SO4 SULFATE ION
HETNAM BEZ BENZOIC ACID
FORMUL 2 SO4 O4 S 2-
FORMUL 3 BEZ C7 H6 O2
FORMUL 4 HOH *342(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 239 1 8
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 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 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 THR A 461 O SER A 525
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 11.07
CISPEP 2 THR A 206 PRO A 207 0 1.90
CISPEP 3 TRP A 351 PRO A 352 0 -6.72
CISPEP 4 PHE A 529 PRO A 530 0 7.28
CRYST1 106.022 106.022 222.284 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 0.009432 0.005446 0.000000 0.00000
SCALE2 0.000000 0.010891 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004499 0.00000
TER 4388 ARG A 574
MASTER 294 0 2 18 29 0 0 6 4743 1 14 45
END |