| 5tyn-pdb | HEADER HYDROLASE/HYDROLASE INHIBITOR 21-NOV-16 5TYN
TITLE ALPHA-ESTERASE-7 IN COMPLEX WITH [3-BROMO-5-(PYRROLIDIN-1-YL)
TITLE 2 PHENYL]BORINIC 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 5TYN 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. 1.53 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) : 1.53
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.23
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 84196
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 4231
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 38.2400 - 4.7545 0.96 2779 134 0.1571 0.1740
REMARK 3 2 4.7545 - 3.7749 0.98 2719 133 0.1451 0.1646
REMARK 3 3 3.7749 - 3.2980 0.98 2669 156 0.1540 0.1876
REMARK 3 4 3.2980 - 2.9966 0.99 2716 141 0.1759 0.2186
REMARK 3 5 2.9966 - 2.7819 1.00 2670 176 0.1823 0.2363
REMARK 3 6 2.7819 - 2.6179 0.99 2689 148 0.1879 0.2345
REMARK 3 7 2.6179 - 2.4868 1.00 2681 132 0.1857 0.2185
REMARK 3 8 2.4868 - 2.3786 1.00 2672 164 0.1949 0.2581
REMARK 3 9 2.3786 - 2.2870 1.00 2692 133 0.1899 0.2238
REMARK 3 10 2.2870 - 2.2081 1.00 2686 142 0.1930 0.2498
REMARK 3 11 2.2081 - 2.1391 1.00 2677 138 0.1971 0.2245
REMARK 3 12 2.1391 - 2.0780 1.00 2654 146 0.1973 0.2316
REMARK 3 13 2.0780 - 2.0233 1.00 2685 143 0.2048 0.2330
REMARK 3 14 2.0233 - 1.9739 1.00 2672 137 0.2102 0.2580
REMARK 3 15 1.9739 - 1.9290 1.00 2654 136 0.2123 0.2400
REMARK 3 16 1.9290 - 1.8880 1.00 2674 133 0.2143 0.2834
REMARK 3 17 1.8880 - 1.8502 1.00 2679 134 0.2199 0.2741
REMARK 3 18 1.8502 - 1.8153 1.00 2632 139 0.2375 0.3184
REMARK 3 19 1.8153 - 1.7829 1.00 2685 134 0.2384 0.3081
REMARK 3 20 1.7829 - 1.7527 1.00 2685 117 0.2445 0.2964
REMARK 3 21 1.7527 - 1.7244 1.00 2642 143 0.2498 0.2610
REMARK 3 22 1.7244 - 1.6978 0.99 2617 146 0.2578 0.3114
REMARK 3 23 1.6978 - 1.6729 1.00 2672 138 0.2639 0.3667
REMARK 3 24 1.6729 - 1.6493 0.99 2583 153 0.2771 0.3456
REMARK 3 25 1.6493 - 1.6270 0.99 2671 155 0.2796 0.3123
REMARK 3 26 1.6270 - 1.6059 0.99 2575 137 0.2762 0.3031
REMARK 3 27 1.6059 - 1.5858 0.99 2680 147 0.2880 0.3527
REMARK 3 28 1.5858 - 1.5667 0.99 2608 128 0.2918 0.3227
REMARK 3 29 1.5667 - 1.5485 0.99 2639 138 0.3012 0.3400
REMARK 3 30 1.5485 - 1.5311 0.98 2608 130 0.3138 0.3576
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.880
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 4761
REMARK 3 ANGLE : 1.041 6451
REMARK 3 CHIRALITY : 0.042 683
REMARK 3 PLANARITY : 0.005 836
REMARK 3 DIHEDRAL : 12.872 1785
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 5TYN 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_1000225043.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
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 : 84196
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.530
REMARK 200 RESOLUTION RANGE LOW (A) : 38.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.16000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.53
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 1.60000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.000
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: 5CH3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM ACETATE PH 5.0, 15% PEG
REMARK 280 2000 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 111.30200
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 111.30200
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 24.85250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.53550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 24.85250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.53550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 111.30200
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 24.85250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 50.53550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 111.30200
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 24.85250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 50.53550
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 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 A1005 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1118 LIES ON A SPECIAL POSITION.
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 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 SER A 218 -121.73 57.53
REMARK 500 CYS A 372 16.01 59.09
REMARK 500 PHE A 421 -60.82 -132.65
REMARK 500 HIS A 435 63.94 -152.65
REMARK 500 HIS A 471 129.96 -39.65
REMARK 500 THR A 472 -5.27 80.15
REMARK 500 SER A 542 -144.75 -131.94
REMARK 500 SER A 542 -147.35 -128.98
REMARK 500 HIS A 566 49.62 -148.60
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 A1122 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH A1123 DISTANCE = 6.90 ANGSTROMS
REMARK 525 HOH A1124 DISTANCE = 7.40 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7NS A 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5TYM RELATED DB: PDB
REMARK 900 RELATED ID: 5TYJ RELATED DB: PDB
REMARK 900 RELATED ID: 5TYK RELATED DB: PDB
REMARK 900 RELATED ID: 5TYL RELATED DB: PDB
REMARK 900 RELATED ID: 5TYO RELATED DB: PDB
REMARK 900 RELATED ID: 5TYP RELATED DB: PDB
DBREF 5TYN A 1 570 UNP Q25252 Q25252_LUCCU 1 570
SEQADV 5TYN MET A -6 UNP Q25252 INITIATING METHIONINE
SEQADV 5TYN HIS A -5 UNP Q25252 EXPRESSION TAG
SEQADV 5TYN HIS A -4 UNP Q25252 EXPRESSION TAG
SEQADV 5TYN HIS A -3 UNP Q25252 EXPRESSION TAG
SEQADV 5TYN HIS A -2 UNP Q25252 EXPRESSION TAG
SEQADV 5TYN HIS A -1 UNP Q25252 EXPRESSION TAG
SEQADV 5TYN HIS A 0 UNP Q25252 EXPRESSION TAG
SEQADV 5TYN ALA A 83 UNP Q25252 ASP 83 ENGINEERED MUTATION
SEQADV 5TYN LEU A 364 UNP Q25252 MET 364 ENGINEERED MUTATION
SEQADV 5TYN PHE A 419 UNP Q25252 ILE 419 ENGINEERED MUTATION
SEQADV 5TYN THR A 472 UNP Q25252 ALA 472 ENGINEERED MUTATION
SEQADV 5TYN THR A 505 UNP Q25252 ILE 505 ENGINEERED MUTATION
SEQADV 5TYN GLU A 530 UNP Q25252 LYS 530 ENGINEERED MUTATION
SEQADV 5TYN 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 GLY 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 7NS A 601 14
HETNAM 7NS [3-BROMO-5-(PYRROLIDIN-1-YL)PHENYL]BORINIC ACID
FORMUL 2 7NS C10 H13 B BR N O
FORMUL 3 HOH *424(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 TYR A 152 LYS A 156 5 5
HELIX 4 AA4 LEU A 167 LEU A 173 1 7
HELIX 5 AA5 SER A 177 ASN A 181 5 5
HELIX 6 AA6 ASN A 185 CYS A 202 1 18
HELIX 7 AA7 ALA A 203 PHE A 205 5 3
HELIX 8 AA8 SER A 218 THR A 230 1 13
HELIX 9 AA9 GLU A 231 ARG A 234 5 4
HELIX 10 AB1 CYS A 249 ASN A 253 5 5
HELIX 11 AB2 HIS A 258 ALA A 267 1 10
HELIX 12 AB3 ASN A 274 ALA A 285 1 12
HELIX 13 AB4 LYS A 286 GLU A 294 1 9
HELIX 14 AB5 GLU A 295 VAL A 297 5 3
HELIX 15 AB6 THR A 299 ASN A 305 1 7
HELIX 16 AB7 HIS A 328 LYS A 334 1 7
HELIX 17 AB8 THR A 335 ILE A 341 5 7
HELIX 18 AB9 TYR A 350 PHE A 354 5 5
HELIX 19 AC1 PHE A 355 MET A 362 1 8
HELIX 20 AC2 PRO A 363 THR A 371 5 9
HELIX 21 AC3 CYS A 372 VAL A 376 5 5
HELIX 22 AC4 ALA A 387 VAL A 402 1 16
HELIX 23 AC5 THR A 408 PHE A 421 1 14
HELIX 24 AC6 PHE A 421 PHE A 433 1 13
HELIX 25 AC7 PRO A 456 ARG A 461 1 6
HELIX 26 AC8 THR A 472 PHE A 478 5 7
HELIX 27 AC9 SER A 491 GLY A 511 1 21
HELIX 28 AD1 GLU A 552 SER A 561 1 10
HELIX 29 AD2 MET A 562 GLU A 564 5 3
HELIX 30 AD3 HIS A 566 PHE A 570 5 5
SHEET 1 AA1 3 THR A 28 ALA A 35 0
SHEET 2 AA1 3 LYS A 41 LEU A 48 -1 O VAL A 42 N ALA A 35
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 ALA A 35 0
SHEET 2 AA212 LYS A 41 LEU A 48 -1 O VAL A 42 N ALA A 35
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 THR A 213 N VAL A 129
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 TYR A 442 N MET A 345
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 ILE A 548 N CYS A 538
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 7NS A 601 1555 1555 1.36
SITE 1 AC1 6 GLY A 135 GLY A 136 GLY A 137 SER A 218
SITE 2 AC1 6 ALA A 219 MET A 308
CRYST1 49.705 101.071 222.604 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 0.020119 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009894 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004492 0.00000
TER 4623 PHE A 570
MASTER 313 0 1 30 17 0 2 6 5014 1 15 45
END
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