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HEADER HYDROLASE/HYDROLASE INHIBITOR 20-NOV-16 5TYJ
TITLE ALPHA-ESTERASE-7 IN COMPLEX WITH (3-BROMO-5-PHENOXYLPHENYL)BORONIC
TITLE 2 ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLIC ESTER HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LUCILIA CUPRINA;
SOURCE 3 ORGANISM_COMMON: GREEN BOTTLE FLY;
SOURCE 4 ORGANISM_TAXID: 7375;
SOURCE 5 GENE: LCAE7;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CARBOXYLESTERASE, INSECTICIDE RESISTANCE, COVALENT INHIBITOR,
KEYWDS 2 ORGANOPHOSPHATE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.J.CORREY,C.J.JACKSON
REVDAT 1 06-DEC-17 5TYJ 0
JRNL AUTH G.J.CORREY,C.J.JACKSON
JRNL TITL COMPUTATIONAL DESIGN OF COVALENT CARBOXYLESTERASE INHIBITORS
JRNL TITL 2 THAT ABOLISH ORGANOPHOSPHATE INSECTICIDE RESISTANCE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.26
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 57007
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 2900
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 42.2734 - 4.8258 1.00 2755 156 0.1635 0.1913
REMARK 3 2 4.8258 - 3.8312 1.00 2646 142 0.1544 0.1984
REMARK 3 3 3.8312 - 3.3472 1.00 2630 125 0.1679 0.2235
REMARK 3 4 3.3472 - 3.0412 1.00 2601 133 0.1869 0.2023
REMARK 3 5 3.0412 - 2.8233 1.00 2587 139 0.1934 0.2574
REMARK 3 6 2.8233 - 2.6569 1.00 2606 148 0.1967 0.2196
REMARK 3 7 2.6569 - 2.5238 1.00 2564 131 0.2137 0.2643
REMARK 3 8 2.5238 - 2.4140 1.00 2583 126 0.2167 0.2702
REMARK 3 9 2.4140 - 2.3210 1.00 2550 148 0.2206 0.2778
REMARK 3 10 2.3210 - 2.2410 1.00 2575 127 0.2173 0.2790
REMARK 3 11 2.2410 - 2.1709 1.00 2540 144 0.2304 0.2788
REMARK 3 12 2.1709 - 2.1088 1.00 2519 156 0.2381 0.2587
REMARK 3 13 2.1088 - 2.0533 1.00 2573 157 0.2468 0.2671
REMARK 3 14 2.0533 - 2.0032 1.00 2559 132 0.2514 0.3207
REMARK 3 15 2.0032 - 1.9577 1.00 2541 123 0.2620 0.3132
REMARK 3 16 1.9577 - 1.9160 1.00 2563 147 0.2797 0.3446
REMARK 3 17 1.9160 - 1.8777 1.00 2549 114 0.2871 0.3386
REMARK 3 18 1.8777 - 1.8423 1.00 2569 129 0.3069 0.3564
REMARK 3 19 1.8423 - 1.8094 1.00 2504 158 0.3250 0.3600
REMARK 3 20 1.8094 - 1.7787 1.00 2530 139 0.3432 0.3991
REMARK 3 21 1.7787 - 1.7500 1.00 2563 126 0.3690 0.4266
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.540
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 : 0.008 4716
REMARK 3 ANGLE : 1.075 6388
REMARK 3 CHIRALITY : 0.044 678
REMARK 3 PLANARITY : 0.005 825
REMARK 3 DIHEDRAL : 14.698 1762
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 5TYJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1000225039.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-NOV-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57007
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 42.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.40
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 14.50
REMARK 200 R MERGE FOR SHELL (I) : 3.08000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.900
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: 5CH3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM ACETATE PH 4.6, 26% PEG
REMARK 280 550 MME, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 112.17650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 112.17650
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 24.29100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.22450
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 24.29100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.22450
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 112.17650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 24.29100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 51.22450
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 112.17650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 24.29100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 51.22450
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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 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 -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 MET A 1
REMARK 465 ASN A 2
REMARK 465 PHE A 3
REMARK 465 ASN A 4
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 ASN A 120 104.65 -160.59
REMARK 500 ASN A 122 73.22 -116.88
REMARK 500 ASN A 204 1.81 -65.15
REMARK 500 SER A 218 -126.31 60.59
REMARK 500 TYR A 350 59.22 -147.32
REMARK 500 PHE A 421 -60.23 -127.41
REMARK 500 HIS A 435 18.31 -145.26
REMARK 500 THR A 472 -3.60 76.72
REMARK 500 SER A 542 -148.02 -127.16
REMARK 500 HIS A 566 56.87 -146.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7ND A 601
DBREF 5TYJ A 1 570 UNP Q25252 Q25252_LUCCU 1 570
SEQADV 5TYJ MET A -6 UNP Q25252 INITIATING METHIONINE
SEQADV 5TYJ HIS A -5 UNP Q25252 EXPRESSION TAG
SEQADV 5TYJ HIS A -4 UNP Q25252 EXPRESSION TAG
SEQADV 5TYJ HIS A -3 UNP Q25252 EXPRESSION TAG
SEQADV 5TYJ HIS A -2 UNP Q25252 EXPRESSION TAG
SEQADV 5TYJ HIS A -1 UNP Q25252 EXPRESSION TAG
SEQADV 5TYJ HIS A 0 UNP Q25252 EXPRESSION TAG
SEQADV 5TYJ ALA A 83 UNP Q25252 ASP 83 ENGINEERED MUTATION
SEQADV 5TYJ ASP A 137 UNP Q25252 GLY 137 ENGINEERED MUTATION
SEQADV 5TYJ LEU A 364 UNP Q25252 MET 364 ENGINEERED MUTATION
SEQADV 5TYJ PHE A 419 UNP Q25252 ILE 419 ENGINEERED MUTATION
SEQADV 5TYJ THR A 472 UNP Q25252 ALA 472 ENGINEERED MUTATION
SEQADV 5TYJ THR A 505 UNP Q25252 ILE 505 ENGINEERED MUTATION
SEQADV 5TYJ GLU A 530 UNP Q25252 LYS 530 ENGINEERED MUTATION
SEQADV 5TYJ GLY A 554 UNP Q25252 ASP 554 ENGINEERED MUTATION
SEQRES 1 A 577 MET HIS HIS HIS HIS HIS HIS MET ASN PHE ASN VAL SER
SEQRES 2 A 577 LEU MET GLU LYS LEU LYS TRP LYS ILE LYS CYS ILE GLU
SEQRES 3 A 577 ASN LYS PHE LEU ASN TYR ARG LEU THR THR ASN GLU THR
SEQRES 4 A 577 VAL VAL ALA GLU THR GLU TYR GLY LYS VAL LYS GLY VAL
SEQRES 5 A 577 LYS ARG LEU THR VAL TYR ASP ASP SER TYR TYR SER PHE
SEQRES 6 A 577 GLU GLY ILE PRO TYR ALA GLN PRO PRO VAL GLY GLU LEU
SEQRES 7 A 577 ARG PHE LYS ALA PRO GLN ARG PRO THR PRO TRP ALA GLY
SEQRES 8 A 577 VAL ARG ASP CYS CYS ASN HIS LYS ASP LYS SER VAL GLN
SEQRES 9 A 577 VAL ASP PHE ILE THR GLY LYS VAL CYS GLY SER GLU ASP
SEQRES 10 A 577 CYS LEU TYR LEU SER VAL TYR THR ASN ASN LEU ASN PRO
SEQRES 11 A 577 GLU THR LYS ARG PRO VAL LEU VAL TYR ILE HIS GLY GLY
SEQRES 12 A 577 ASP PHE ILE ILE GLY GLU ASN HIS ARG ASP MET TYR GLY
SEQRES 13 A 577 PRO ASP TYR PHE ILE LYS LYS ASP VAL VAL LEU ILE ASN
SEQRES 14 A 577 ILE GLN TYR ARG LEU GLY ALA LEU GLY PHE LEU SER LEU
SEQRES 15 A 577 ASN SER GLU ASP LEU ASN VAL PRO GLY ASN ALA GLY LEU
SEQRES 16 A 577 LYS ASP GLN VAL MET ALA LEU ARG TRP ILE LYS ASN ASN
SEQRES 17 A 577 CYS ALA ASN PHE GLY GLY ASN PRO ASP ASN ILE THR VAL
SEQRES 18 A 577 PHE GLY GLU SER ALA GLY ALA ALA SER THR HIS TYR MET
SEQRES 19 A 577 MET LEU THR GLU GLN THR ARG GLY LEU PHE HIS ARG GLY
SEQRES 20 A 577 ILE LEU MET SER GLY ASN ALA ILE CYS PRO TRP ALA ASN
SEQRES 21 A 577 THR GLN CYS GLN HIS ARG ALA PHE THR LEU ALA LYS LEU
SEQRES 22 A 577 ALA GLY TYR LYS GLY GLU ASP ASN ASP LYS ASP VAL LEU
SEQRES 23 A 577 GLU PHE LEU MET LYS ALA LYS PRO GLN ASP LEU ILE LYS
SEQRES 24 A 577 LEU GLU GLU LYS VAL LEU THR LEU GLU GLU ARG THR ASN
SEQRES 25 A 577 LYS VAL MET PHE PRO PHE GLY PRO THR VAL GLU PRO TYR
SEQRES 26 A 577 GLN THR ALA ASP CYS VAL LEU PRO LYS HIS PRO ARG GLU
SEQRES 27 A 577 MET VAL LYS THR ALA TRP GLY ASN SER ILE PRO THR MET
SEQRES 28 A 577 MET GLY ASN THR SER TYR GLU GLY LEU PHE PHE THR SER
SEQRES 29 A 577 ILE LEU LYS GLN MET PRO LEU LEU VAL LYS GLU LEU GLU
SEQRES 30 A 577 THR CYS VAL ASN PHE VAL PRO SER GLU LEU ALA ASP ALA
SEQRES 31 A 577 GLU ARG THR ALA PRO GLU THR LEU GLU MET GLY ALA LYS
SEQRES 32 A 577 ILE LYS LYS ALA HIS VAL THR GLY GLU THR PRO THR ALA
SEQRES 33 A 577 ASP ASN PHE MET ASP LEU CYS SER HIS PHE TYR PHE TRP
SEQRES 34 A 577 PHE PRO MET HIS ARG LEU LEU GLN LEU ARG PHE ASN HIS
SEQRES 35 A 577 THR SER GLY THR PRO VAL TYR LEU TYR ARG PHE ASP PHE
SEQRES 36 A 577 ASP SER GLU ASP LEU ILE ASN PRO TYR ARG ILE MET ARG
SEQRES 37 A 577 SER GLY ARG GLY VAL LYS GLY VAL SER HIS THR ASP GLU
SEQRES 38 A 577 LEU THR TYR PHE PHE TRP ASN GLN LEU ALA LYS ARG MET
SEQRES 39 A 577 PRO LYS GLU SER ARG GLU TYR LYS THR ILE GLU ARG MET
SEQRES 40 A 577 THR GLY ILE TRP THR GLN PHE ALA THR THR GLY ASN PRO
SEQRES 41 A 577 TYR SER ASN GLU ILE GLU GLY MET GLU ASN VAL SER TRP
SEQRES 42 A 577 ASP PRO ILE GLU LYS SER ASP GLU VAL TYR LYS CYS LEU
SEQRES 43 A 577 ASN ILE SER ASP GLU LEU LYS MET ILE ASP VAL PRO GLU
SEQRES 44 A 577 MET GLY LYS ILE LYS GLN TRP GLU SER MET PHE GLU LYS
SEQRES 45 A 577 HIS ARG ASP LEU PHE
HET 7ND A 601 17
HETNAM 7ND (3-BROMO-5-PHENOXYPHENYL)BORONIC ACID
FORMUL 2 7ND C12 H10 B BR O3
FORMUL 3 HOH *205(H2 O)
HELIX 1 AA1 SER A 6 LEU A 27 1 22
HELIX 2 AA2 VAL A 68 ARG A 72 5 5
HELIX 3 AA3 HIS A 144 GLY A 149 1 6
HELIX 4 AA4 TYR A 152 LYS A 156 5 5
HELIX 5 AA5 LEU A 167 LEU A 173 1 7
HELIX 6 AA6 SER A 177 ASN A 181 5 5
HELIX 7 AA7 ASN A 185 CYS A 202 1 18
HELIX 8 AA8 ALA A 203 PHE A 205 5 3
HELIX 9 AA9 SER A 218 THR A 230 1 13
HELIX 10 AB1 GLU A 231 ARG A 234 5 4
HELIX 11 AB2 CYS A 249 ASN A 253 5 5
HELIX 12 AB3 HIS A 258 ALA A 267 1 10
HELIX 13 AB4 ASN A 274 ALA A 285 1 12
HELIX 14 AB5 LYS A 286 GLU A 294 1 9
HELIX 15 AB6 GLU A 295 VAL A 297 5 3
HELIX 16 AB7 THR A 299 ASN A 305 1 7
HELIX 17 AB8 HIS A 328 LYS A 334 1 7
HELIX 18 AB9 THR A 335 ILE A 341 5 7
HELIX 19 AC1 TYR A 350 PHE A 354 5 5
HELIX 20 AC2 PHE A 355 MET A 362 1 8
HELIX 21 AC3 PRO A 363 THR A 371 5 9
HELIX 22 AC4 CYS A 372 VAL A 376 5 5
HELIX 23 AC5 ALA A 387 VAL A 402 1 16
HELIX 24 AC6 THR A 408 PHE A 421 1 14
HELIX 25 AC7 PHE A 421 ASN A 434 1 14
HELIX 26 AC8 PRO A 456 ARG A 461 1 6
HELIX 27 AC9 THR A 472 PHE A 478 5 7
HELIX 28 AD1 SER A 491 GLY A 511 1 21
HELIX 29 AD2 GLU A 552 SER A 561 1 10
HELIX 30 AD3 MET A 562 GLU A 564 5 3
HELIX 31 AD4 HIS A 566 PHE A 570 5 5
SHEET 1 AA1 3 THR A 28 THR A 37 0
SHEET 2 AA1 3 GLY A 40 LEU A 48 -1 O GLY A 40 N THR A 37
SHEET 3 AA1 3 VAL A 85 ASP A 87 1 O ARG A 86 N LYS A 41
SHEET 1 AA212 THR A 28 THR A 37 0
SHEET 2 AA212 GLY A 40 LEU A 48 -1 O GLY A 40 N THR A 37
SHEET 3 AA212 SER A 54 PRO A 62 -1 O TYR A 55 N ARG A 47
SHEET 4 AA212 TYR A 113 THR A 118 -1 O THR A 118 N TYR A 56
SHEET 5 AA212 VAL A 159 ILE A 163 -1 O LEU A 160 N TYR A 117
SHEET 6 AA212 ARG A 127 ILE A 133 1 N LEU A 130 O VAL A 159
SHEET 7 AA212 GLY A 207 GLU A 217 1 O ASN A 208 N ARG A 127
SHEET 8 AA212 ARG A 239 MET A 243 1 O MET A 243 N GLY A 216
SHEET 9 AA212 THR A 343 THR A 348 1 O MET A 344 N LEU A 242
SHEET 10 AA212 VAL A 441 PHE A 446 1 O PHE A 446 N ASN A 347
SHEET 11 AA212 LYS A 537 ILE A 541 1 O ILE A 541 N ARG A 445
SHEET 12 AA212 LEU A 545 ASP A 549 -1 O LYS A 546 N ASN A 540
SHEET 1 AA3 2 GLN A 97 VAL A 98 0
SHEET 2 AA3 2 VAL A 105 CYS A 106 -1 O CYS A 106 N GLN A 97
LINK OG SER A 218 B05 7ND A 601 1555 1555 1.47
SITE 1 AC1 10 GLY A 136 ASP A 137 SER A 218 ALA A 219
SITE 2 AC1 10 PHE A 354 ILE A 358 TYR A 420 HIS A 471
SITE 3 AC1 10 HOH A 824 HOH A 869
CRYST1 48.582 102.449 224.353 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.020584 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009761 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004457 0.00000
TER 4580 PHE A 570
MASTER 275 0 1 31 17 0 3 6 4783 1 18 45
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