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HEADER HYDROLASE/HYDROLASE INHIBITOR 23-AUG-17 6ARY
TITLE CRYSTAL STRUCTURE OF AN INSECTICIDE-RESISTANT ACETYLCHOLINESTERASE
TITLE 2 MUTANT FROM THE MALARIA VECTOR ANOPHELES GAMBIAE IN COMPLEX WITH A
TITLE 3 DIFLUOROMETHYL KETONE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 162 TO 702;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ANOPHELES GAMBIAE;
SOURCE 3 ORGANISM_COMMON: AFRICAN MALARIA MOSQUITO;
SOURCE 4 ORGANISM_TAXID: 7165;
SOURCE 5 GENE: ACE, ACE1, ACHE1, AGAP001356;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACLOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: MODIFIED PFASTBAC
KEYWDS HYDROLASE, DIFLUOROMETHYL KETONE, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.CHEUNG,A.MAHMOOD,R.KALATHUR,L.LIXUAN,P.R.CARLIER
REVDAT 1 10-JAN-18 6ARY 0
JRNL AUTH J.CHEUNG,A.MAHMOOD,R.KALATHUR,L.LIU,P.R.CARLIER
JRNL TITL STRUCTURE OF THE G119S MUTANT ACETYLCHOLINESTERASE OF THE
JRNL TITL 2 MALARIA VECTOR ANOPHELES GAMBIAE REVEALS BASIS OF
JRNL TITL 3 INSECTICIDE RESISTANCE.
JRNL REF STRUCTURE V. 26 130 2018
JRNL REFN ISSN 1878-4186
JRNL PMID 29276037
JRNL DOI 10.1016/J.STR.2017.11.021
REMARK 2
REMARK 2 RESOLUTION. 2.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 134527
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) : 0.162
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 6662
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 49.3109 - 7.0077 1.00 4367 204 0.1407 0.1571
REMARK 3 2 7.0077 - 5.5647 1.00 4315 215 0.1298 0.1472
REMARK 3 3 5.5647 - 4.8620 1.00 4312 220 0.1186 0.1251
REMARK 3 4 4.8620 - 4.4178 1.00 4272 253 0.1062 0.1262
REMARK 3 5 4.4178 - 4.1013 1.00 4292 250 0.1137 0.1300
REMARK 3 6 4.1013 - 3.8596 1.00 4325 200 0.1294 0.1431
REMARK 3 7 3.8596 - 3.6663 1.00 4286 209 0.1485 0.1837
REMARK 3 8 3.6663 - 3.5068 1.00 4266 267 0.1622 0.1903
REMARK 3 9 3.5068 - 3.3718 1.00 4294 240 0.1749 0.2018
REMARK 3 10 3.3718 - 3.2555 1.00 4261 232 0.2033 0.2341
REMARK 3 11 3.2555 - 3.1537 1.00 4287 237 0.2072 0.2554
REMARK 3 12 3.1537 - 3.0636 1.00 4248 234 0.2020 0.2558
REMARK 3 13 3.0636 - 2.9829 1.00 4301 234 0.2056 0.2406
REMARK 3 14 2.9829 - 2.9102 1.00 4303 228 0.2125 0.2617
REMARK 3 15 2.9102 - 2.8440 1.00 4305 180 0.2229 0.2933
REMARK 3 16 2.8440 - 2.7835 1.00 4242 232 0.2156 0.2505
REMARK 3 17 2.7835 - 2.7278 1.00 4271 233 0.2195 0.2587
REMARK 3 18 2.7278 - 2.6764 1.00 4331 182 0.2294 0.2364
REMARK 3 19 2.6764 - 2.6286 1.00 4320 219 0.2339 0.2704
REMARK 3 20 2.6286 - 2.5840 1.00 4273 225 0.2252 0.2653
REMARK 3 21 2.5840 - 2.5423 1.00 4242 227 0.2273 0.2575
REMARK 3 22 2.5423 - 2.5032 1.00 4258 261 0.2318 0.2692
REMARK 3 23 2.5032 - 2.4664 1.00 4268 219 0.2515 0.2838
REMARK 3 24 2.4664 - 2.4317 1.00 4271 235 0.2532 0.2745
REMARK 3 25 2.4317 - 2.3988 1.00 4319 204 0.2632 0.2749
REMARK 3 26 2.3988 - 2.3677 1.00 4283 210 0.2677 0.2978
REMARK 3 27 2.3677 - 2.3381 1.00 4285 231 0.2809 0.3044
REMARK 3 28 2.3381 - 2.3099 1.00 4272 189 0.2993 0.3266
REMARK 3 29 2.3099 - 2.2830 1.00 4256 228 0.3134 0.3508
REMARK 3 30 2.2830 - 2.2574 0.81 3540 164 0.3212 0.3509
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 60.62
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.76
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 : 0.011 8967
REMARK 3 ANGLE : 1.068 12262
REMARK 3 CHIRALITY : 0.176 1299
REMARK 3 PLANARITY : 0.007 1618
REMARK 3 DIHEDRAL : 11.858 5274
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 : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 163 THROUGH 337 OR
REMARK 3 RESID 339 THROUGH 351 OR RESID 353
REMARK 3 THROUGH 569 OR RESID 571 THROUGH 659 OR
REMARK 3 RESID 661 THROUGH 699))
REMARK 3 SELECTION : (CHAIN B AND (RESID 163 THROUGH 337 OR
REMARK 3 RESID 339 THROUGH 351 OR RESID 353
REMARK 3 THROUGH 569 OR RESID 571 THROUGH 659 OR
REMARK 3 RESID 661 THROUGH 699))
REMARK 3 ATOM PAIRS NUMBER : 5175
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6ARY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1000229276.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAR-17
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 : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 134751
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 200.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 22.10
REMARK 200 R MERGE (I) : 0.15700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 3.7000
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.10
REMARK 200 R MERGE FOR SHELL (I) : 2.53400
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: 4EY4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 79.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.9 - 1.0M TRI-AMMONIUM CITRATE PH
REMARK 280 6.5, 1 - 3% ISOPROPANOL, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 75.49267
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 150.98533
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 113.23900
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 188.73167
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 37.74633
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: 3410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 -75.16650
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 130.19220
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 75.49267
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 SER A 161
REMARK 465 ASP A 162
REMARK 465 LEU A 700
REMARK 465 PRO A 701
REMARK 465 GLY A 702
REMARK 465 SER B 161
REMARK 465 ASP B 162
REMARK 465 LEU B 700
REMARK 465 PRO B 701
REMARK 465 GLY B 702
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 ASP B 292 O HOH B 901 2.05
REMARK 500 O HOH B 1050 O HOH B 1061 2.15
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 PHE A 206 -7.93 72.64
REMARK 500 THR A 221 78.90 -115.51
REMARK 500 ALA A 312 -159.72 60.88
REMARK 500 SER A 360 -123.45 65.69
REMARK 500 HIS A 416 42.68 -147.17
REMARK 500 ALA A 458 -50.35 -123.19
REMARK 500 GLU A 485 69.97 -119.35
REMARK 500 LEU A 495 73.51 -105.06
REMARK 500 LEU A 499 73.43 -103.72
REMARK 500 GLU A 540 76.69 -157.37
REMARK 500 PHE A 560 -73.73 -130.25
REMARK 500 ASN A 670 63.72 -105.54
REMARK 500 SER A 672 26.67 -142.62
REMARK 500 LYS A 688 -51.85 -122.12
REMARK 500 PHE B 206 -8.98 73.27
REMARK 500 THR B 221 77.71 -111.49
REMARK 500 ALA B 312 -158.42 59.22
REMARK 500 SER B 360 -123.67 65.41
REMARK 500 HIS B 416 41.99 -146.82
REMARK 500 GLU B 485 68.91 -118.94
REMARK 500 LEU B 495 71.70 -103.47
REMARK 500 LEU B 499 73.21 -106.75
REMARK 500 GLU B 540 78.28 -155.66
REMARK 500 PHE B 560 -72.53 -129.00
REMARK 500 ASN B 670 66.39 -107.95
REMARK 500 SER B 672 26.58 -142.09
REMARK 500 LYS B 688 -52.71 -122.72
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 BT7 A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 802 bound
REMARK 800 to ASN A 220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 803 bound
REMARK 800 to ASN A 670
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 802 bound
REMARK 800 to ASN B 220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BT7 B 801 and SER B
REMARK 800 360
DBREF 6ARY A 162 702 UNP Q869C3 ACES_ANOGA 162 702
DBREF 6ARY B 162 702 UNP Q869C3 ACES_ANOGA 162 702
SEQADV 6ARY SER A 161 UNP Q869C3 EXPRESSION TAG
SEQADV 6ARY SER A 280 UNP Q869C3 GLY 280 ENGINEERED MUTATION
SEQADV 6ARY SER B 161 UNP Q869C3 EXPRESSION TAG
SEQADV 6ARY SER B 280 UNP Q869C3 GLY 280 ENGINEERED MUTATION
SEQRES 1 A 542 SER ASP ASN ASP PRO LEU VAL VAL ASN THR ASP LYS GLY
SEQRES 2 A 542 ARG ILE ARG GLY ILE THR VAL ASP ALA PRO SER GLY LYS
SEQRES 3 A 542 LYS VAL ASP VAL TRP LEU GLY ILE PRO TYR ALA GLN PRO
SEQRES 4 A 542 PRO VAL GLY PRO LEU ARG PHE ARG HIS PRO ARG PRO ALA
SEQRES 5 A 542 GLU LYS TRP THR GLY VAL LEU ASN THR THR THR PRO PRO
SEQRES 6 A 542 ASN SER CYS VAL GLN ILE VAL ASP THR VAL PHE GLY ASP
SEQRES 7 A 542 PHE PRO GLY ALA THR MET TRP ASN PRO ASN THR PRO LEU
SEQRES 8 A 542 SER GLU ASP CYS LEU TYR ILE ASN VAL VAL ALA PRO ARG
SEQRES 9 A 542 PRO ARG PRO LYS ASN ALA ALA VAL MET LEU TRP ILE PHE
SEQRES 10 A 542 GLY GLY SER PHE TYR SER GLY THR ALA THR LEU ASP VAL
SEQRES 11 A 542 TYR ASP HIS ARG ALA LEU ALA SER GLU GLU ASN VAL ILE
SEQRES 12 A 542 VAL VAL SER LEU GLN TYR ARG VAL ALA SER LEU GLY PHE
SEQRES 13 A 542 LEU PHE LEU GLY THR PRO GLU ALA PRO GLY ASN ALA GLY
SEQRES 14 A 542 LEU PHE ASP GLN ASN LEU ALA LEU ARG TRP VAL ARG ASP
SEQRES 15 A 542 ASN ILE HIS ARG PHE GLY GLY ASP PRO SER ARG VAL THR
SEQRES 16 A 542 LEU PHE GLY GLU SER ALA GLY ALA VAL SER VAL SER LEU
SEQRES 17 A 542 HIS LEU LEU SER ALA LEU SER ARG ASP LEU PHE GLN ARG
SEQRES 18 A 542 ALA ILE LEU GLN SER GLY SER PRO THR ALA PRO TRP ALA
SEQRES 19 A 542 LEU VAL SER ARG GLU GLU ALA THR LEU ARG ALA LEU ARG
SEQRES 20 A 542 LEU ALA GLU ALA VAL GLY CYS PRO HIS GLU PRO SER LYS
SEQRES 21 A 542 LEU SER ASP ALA VAL GLU CYS LEU ARG GLY LYS ASP PRO
SEQRES 22 A 542 HIS VAL LEU VAL ASN ASN GLU TRP GLY THR LEU GLY ILE
SEQRES 23 A 542 CYS GLU PHE PRO PHE VAL PRO VAL VAL ASP GLY ALA PHE
SEQRES 24 A 542 LEU ASP GLU THR PRO GLN ARG SER LEU ALA SER GLY ARG
SEQRES 25 A 542 PHE LYS LYS THR GLU ILE LEU THR GLY SER ASN THR GLU
SEQRES 26 A 542 GLU GLY TYR TYR PHE ILE ILE TYR TYR LEU THR GLU LEU
SEQRES 27 A 542 LEU ARG LYS GLU GLU GLY VAL THR VAL THR ARG GLU GLU
SEQRES 28 A 542 PHE LEU GLN ALA VAL ARG GLU LEU ASN PRO TYR VAL ASN
SEQRES 29 A 542 GLY ALA ALA ARG GLN ALA ILE VAL PHE GLU TYR THR ASP
SEQRES 30 A 542 TRP THR GLU PRO ASP ASN PRO ASN SER ASN ARG ASP ALA
SEQRES 31 A 542 LEU ASP LYS MET VAL GLY ASP TYR HIS PHE THR CYS ASN
SEQRES 32 A 542 VAL ASN GLU PHE ALA GLN ARG TYR ALA GLU GLU GLY ASN
SEQRES 33 A 542 ASN VAL TYR MET TYR LEU TYR THR HIS ARG SER LYS GLY
SEQRES 34 A 542 ASN PRO TRP PRO ARG TRP THR GLY VAL MET HIS GLY ASP
SEQRES 35 A 542 GLU ILE ASN TYR VAL PHE GLY GLU PRO LEU ASN PRO THR
SEQRES 36 A 542 LEU GLY TYR THR GLU ASP GLU LYS ASP PHE SER ARG LYS
SEQRES 37 A 542 ILE MET ARG TYR TRP SER ASN PHE ALA LYS THR GLY ASN
SEQRES 38 A 542 PRO ASN PRO ASN THR ALA SER SER GLU PHE PRO GLU TRP
SEQRES 39 A 542 PRO LYS HIS THR ALA HIS GLY ARG HIS TYR LEU GLU LEU
SEQRES 40 A 542 GLY LEU ASN THR SER PHE VAL GLY ARG GLY PRO ARG LEU
SEQRES 41 A 542 ARG GLN CYS ALA PHE TRP LYS LYS TYR LEU PRO GLN LEU
SEQRES 42 A 542 VAL ALA ALA THR SER ASN LEU PRO GLY
SEQRES 1 B 542 SER ASP ASN ASP PRO LEU VAL VAL ASN THR ASP LYS GLY
SEQRES 2 B 542 ARG ILE ARG GLY ILE THR VAL ASP ALA PRO SER GLY LYS
SEQRES 3 B 542 LYS VAL ASP VAL TRP LEU GLY ILE PRO TYR ALA GLN PRO
SEQRES 4 B 542 PRO VAL GLY PRO LEU ARG PHE ARG HIS PRO ARG PRO ALA
SEQRES 5 B 542 GLU LYS TRP THR GLY VAL LEU ASN THR THR THR PRO PRO
SEQRES 6 B 542 ASN SER CYS VAL GLN ILE VAL ASP THR VAL PHE GLY ASP
SEQRES 7 B 542 PHE PRO GLY ALA THR MET TRP ASN PRO ASN THR PRO LEU
SEQRES 8 B 542 SER GLU ASP CYS LEU TYR ILE ASN VAL VAL ALA PRO ARG
SEQRES 9 B 542 PRO ARG PRO LYS ASN ALA ALA VAL MET LEU TRP ILE PHE
SEQRES 10 B 542 GLY GLY SER PHE TYR SER GLY THR ALA THR LEU ASP VAL
SEQRES 11 B 542 TYR ASP HIS ARG ALA LEU ALA SER GLU GLU ASN VAL ILE
SEQRES 12 B 542 VAL VAL SER LEU GLN TYR ARG VAL ALA SER LEU GLY PHE
SEQRES 13 B 542 LEU PHE LEU GLY THR PRO GLU ALA PRO GLY ASN ALA GLY
SEQRES 14 B 542 LEU PHE ASP GLN ASN LEU ALA LEU ARG TRP VAL ARG ASP
SEQRES 15 B 542 ASN ILE HIS ARG PHE GLY GLY ASP PRO SER ARG VAL THR
SEQRES 16 B 542 LEU PHE GLY GLU SER ALA GLY ALA VAL SER VAL SER LEU
SEQRES 17 B 542 HIS LEU LEU SER ALA LEU SER ARG ASP LEU PHE GLN ARG
SEQRES 18 B 542 ALA ILE LEU GLN SER GLY SER PRO THR ALA PRO TRP ALA
SEQRES 19 B 542 LEU VAL SER ARG GLU GLU ALA THR LEU ARG ALA LEU ARG
SEQRES 20 B 542 LEU ALA GLU ALA VAL GLY CYS PRO HIS GLU PRO SER LYS
SEQRES 21 B 542 LEU SER ASP ALA VAL GLU CYS LEU ARG GLY LYS ASP PRO
SEQRES 22 B 542 HIS VAL LEU VAL ASN ASN GLU TRP GLY THR LEU GLY ILE
SEQRES 23 B 542 CYS GLU PHE PRO PHE VAL PRO VAL VAL ASP GLY ALA PHE
SEQRES 24 B 542 LEU ASP GLU THR PRO GLN ARG SER LEU ALA SER GLY ARG
SEQRES 25 B 542 PHE LYS LYS THR GLU ILE LEU THR GLY SER ASN THR GLU
SEQRES 26 B 542 GLU GLY TYR TYR PHE ILE ILE TYR TYR LEU THR GLU LEU
SEQRES 27 B 542 LEU ARG LYS GLU GLU GLY VAL THR VAL THR ARG GLU GLU
SEQRES 28 B 542 PHE LEU GLN ALA VAL ARG GLU LEU ASN PRO TYR VAL ASN
SEQRES 29 B 542 GLY ALA ALA ARG GLN ALA ILE VAL PHE GLU TYR THR ASP
SEQRES 30 B 542 TRP THR GLU PRO ASP ASN PRO ASN SER ASN ARG ASP ALA
SEQRES 31 B 542 LEU ASP LYS MET VAL GLY ASP TYR HIS PHE THR CYS ASN
SEQRES 32 B 542 VAL ASN GLU PHE ALA GLN ARG TYR ALA GLU GLU GLY ASN
SEQRES 33 B 542 ASN VAL TYR MET TYR LEU TYR THR HIS ARG SER LYS GLY
SEQRES 34 B 542 ASN PRO TRP PRO ARG TRP THR GLY VAL MET HIS GLY ASP
SEQRES 35 B 542 GLU ILE ASN TYR VAL PHE GLY GLU PRO LEU ASN PRO THR
SEQRES 36 B 542 LEU GLY TYR THR GLU ASP GLU LYS ASP PHE SER ARG LYS
SEQRES 37 B 542 ILE MET ARG TYR TRP SER ASN PHE ALA LYS THR GLY ASN
SEQRES 38 B 542 PRO ASN PRO ASN THR ALA SER SER GLU PHE PRO GLU TRP
SEQRES 39 B 542 PRO LYS HIS THR ALA HIS GLY ARG HIS TYR LEU GLU LEU
SEQRES 40 B 542 GLY LEU ASN THR SER PHE VAL GLY ARG GLY PRO ARG LEU
SEQRES 41 B 542 ARG GLN CYS ALA PHE TRP LYS LYS TYR LEU PRO GLN LEU
SEQRES 42 B 542 VAL ALA ALA THR SER ASN LEU PRO GLY
HET BT7 A 801 15
HET NAG A 802 14
HET NAG A 803 14
HET FLC A 804 13
HET FLC A 805 13
HET CL A 806 1
HET BT7 B 801 15
HET NAG B 802 14
HET FLC B 803 13
HET FLC B 804 13
HETNAM BT7 (1S)-2,2-DIFLUORO-1-[1-(PENTAN-3-YL)-1H-PYRAZOL-4-
HETNAM 2 BT7 YL]ETHAN-1-OL
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FLC CITRATE ANION
HETNAM CL CHLORIDE ION
FORMUL 3 BT7 2(C10 H16 F2 N2 O)
FORMUL 4 NAG 3(C8 H15 N O6)
FORMUL 6 FLC 4(C6 H5 O7 3-)
FORMUL 8 CL CL 1-
FORMUL 13 HOH *388(H2 O)
HELIX 1 AA1 VAL A 201 ARG A 205 5 5
HELIX 2 AA2 PHE A 239 MET A 244 1 6
HELIX 3 AA3 LEU A 288 ASP A 292 5 5
HELIX 4 AA4 HIS A 293 ASN A 301 1 9
HELIX 5 AA5 VAL A 311 LEU A 317 1 7
HELIX 6 AA6 ASN A 327 ILE A 344 1 18
HELIX 7 AA7 HIS A 345 PHE A 347 5 3
HELIX 8 AA8 SER A 360 SER A 372 1 13
HELIX 9 AA9 SER A 397 VAL A 412 1 16
HELIX 10 AB1 LYS A 420 ARG A 429 1 10
HELIX 11 AB2 ASP A 432 ASN A 439 1 8
HELIX 12 AB3 THR A 463 GLY A 471 1 9
HELIX 13 AB4 GLY A 487 LEU A 495 1 9
HELIX 14 AB5 THR A 508 ASN A 520 1 13
HELIX 15 AB6 ASN A 524 TYR A 535 1 12
HELIX 16 AB7 ASN A 543 PHE A 560 1 18
HELIX 17 AB8 PHE A 560 GLU A 574 1 15
HELIX 18 AB9 PRO A 593 GLY A 597 5 5
HELIX 19 AC1 GLU A 603 PHE A 608 1 6
HELIX 20 AC2 GLY A 609 ASN A 613 5 5
HELIX 21 AC3 THR A 619 GLY A 640 1 22
HELIX 22 AC4 ARG A 679 LYS A 688 1 10
HELIX 23 AC5 LYS A 688 THR A 697 1 10
HELIX 24 AC6 VAL B 201 ARG B 205 5 5
HELIX 25 AC7 PHE B 239 MET B 244 1 6
HELIX 26 AC8 LEU B 288 ASP B 292 5 5
HELIX 27 AC9 HIS B 293 ASN B 301 1 9
HELIX 28 AD1 VAL B 311 LEU B 317 1 7
HELIX 29 AD2 ASN B 327 ILE B 344 1 18
HELIX 30 AD3 HIS B 345 PHE B 347 5 3
HELIX 31 AD4 SER B 360 LEU B 370 1 11
HELIX 32 AD5 SER B 397 VAL B 412 1 16
HELIX 33 AD6 LYS B 420 LYS B 431 1 12
HELIX 34 AD7 ASP B 432 ASN B 439 1 8
HELIX 35 AD8 THR B 463 GLY B 471 1 9
HELIX 36 AD9 GLY B 487 LEU B 495 1 9
HELIX 37 AE1 THR B 508 ASN B 520 1 13
HELIX 38 AE2 ASN B 524 TYR B 535 1 12
HELIX 39 AE3 ASN B 543 PHE B 560 1 18
HELIX 40 AE4 PHE B 560 GLU B 574 1 15
HELIX 41 AE5 PRO B 593 GLY B 597 5 5
HELIX 42 AE6 GLU B 603 PHE B 608 1 6
HELIX 43 AE7 GLY B 609 ASN B 613 5 5
HELIX 44 AE8 THR B 619 GLY B 640 1 22
HELIX 45 AE9 ARG B 679 LYS B 688 1 10
HELIX 46 AF1 LYS B 688 THR B 697 1 10
SHEET 1 AA1 3 VAL A 167 THR A 170 0
SHEET 2 AA1 3 GLY A 173 ARG A 176 -1 O GLY A 173 N THR A 170
SHEET 3 AA1 3 VAL A 218 ASN A 220 1 O LEU A 219 N ARG A 176
SHEET 1 AA211 ILE A 178 ASP A 181 0
SHEET 2 AA211 LYS A 187 PRO A 195 -1 O VAL A 188 N VAL A 180
SHEET 3 AA211 TYR A 257 PRO A 263 -1 O VAL A 260 N TRP A 191
SHEET 4 AA211 ILE A 303 LEU A 307 -1 O SER A 306 N ASN A 259
SHEET 5 AA211 ALA A 270 ILE A 276 1 N TRP A 275 O VAL A 305
SHEET 6 AA211 GLY A 349 GLU A 359 1 O ASP A 350 N ALA A 270
SHEET 7 AA211 ARG A 381 GLN A 385 1 O GLN A 385 N GLY A 358
SHEET 8 AA211 ILE A 478 ASN A 483 1 O LEU A 479 N LEU A 384
SHEET 9 AA211 VAL A 578 TYR A 583 1 O TYR A 583 N SER A 482
SHEET 10 AA211 HIS A 663 LEU A 667 1 O LEU A 667 N LEU A 582
SHEET 11 AA211 VAL A 674 ARG A 676 -1 O GLY A 675 N TYR A 664
SHEET 1 AA3 3 VAL B 167 THR B 170 0
SHEET 2 AA3 3 GLY B 173 ARG B 176 -1 O GLY B 173 N THR B 170
SHEET 3 AA3 3 VAL B 218 ASN B 220 1 O LEU B 219 N ARG B 176
SHEET 1 AA411 ILE B 178 ASP B 181 0
SHEET 2 AA411 LYS B 187 PRO B 195 -1 O VAL B 188 N VAL B 180
SHEET 3 AA411 TYR B 257 PRO B 263 -1 O ILE B 258 N ILE B 194
SHEET 4 AA411 ILE B 303 LEU B 307 -1 O SER B 306 N ASN B 259
SHEET 5 AA411 ALA B 270 ILE B 276 1 N TRP B 275 O VAL B 305
SHEET 6 AA411 GLY B 349 GLU B 359 1 O ASP B 350 N ALA B 270
SHEET 7 AA411 ARG B 381 GLN B 385 1 O ILE B 383 N LEU B 356
SHEET 8 AA411 ILE B 478 ASN B 483 1 O LEU B 479 N LEU B 384
SHEET 9 AA411 VAL B 578 TYR B 583 1 O TYR B 583 N SER B 482
SHEET 10 AA411 HIS B 663 LEU B 667 1 O LEU B 667 N LEU B 582
SHEET 11 AA411 VAL B 674 ARG B 676 -1 O GLY B 675 N TYR B 664
SSBOND 1 CYS A 228 CYS A 255 1555 1555 2.07
SSBOND 2 CYS A 414 CYS A 427 1555 1555 2.09
SSBOND 3 CYS A 562 CYS A 683 1555 1555 2.08
SSBOND 4 CYS B 228 CYS B 255 1555 1555 2.06
SSBOND 5 CYS B 414 CYS B 427 1555 1555 2.09
SSBOND 6 CYS B 562 CYS B 683 1555 1555 2.07
LINK ND2 ASN A 220 C1 NAG A 802 1555 1555 1.47
LINK OG SER A 360 C11 BT7 A 801 1555 1555 1.43
LINK ND2 ASN A 670 C1 NAG A 803 1555 1555 1.45
LINK ND2 ASN B 220 C1 NAG B 802 1555 1555 1.47
LINK OG SER B 360 C11 BT7 B 801 1555 1555 1.42
CISPEP 1 ARG A 264 PRO A 265 0 0.61
CISPEP 2 GLY A 677 PRO A 678 0 7.76
CISPEP 3 ARG B 264 PRO B 265 0 0.50
CISPEP 4 GLY B 677 PRO B 678 0 9.12
SITE 1 AC1 14 TRP A 245 GLY A 278 GLY A 279 SER A 280
SITE 2 AC1 14 GLU A 359 SER A 360 ALA A 361 TRP A 393
SITE 3 AC1 14 PHE A 449 TYR A 489 PHE A 490 PHE A 560
SITE 4 AC1 14 HIS A 600 HOH A1007
SITE 1 AC2 5 THR A 658 HIS A 660 HIS A 663 ARG A 676
SITE 2 AC2 5 HOH A 966
SITE 1 AC3 4 ARG A 517 ASN A 524 GLY A 525 ARG A 528
SITE 1 AC4 3 ARG A 376 ARG A 472 GLN B 198
SITE 1 AC5 4 THR B 658 HIS B 660 HIS B 663 ARG B 676
SITE 1 AC6 4 ARG B 517 ASN B 524 GLY B 525 ARG B 528
SITE 1 AC7 1 ASN A 220
SITE 1 AC8 1 ASN A 670
SITE 1 AC9 1 ASN B 220
SITE 1 AD1 18 TRP B 245 GLY B 278 GLY B 279 SER B 280
SITE 2 AD1 18 GLU B 359 ALA B 361 GLY B 362 ALA B 363
SITE 3 AD1 18 VAL B 364 GLN B 385 SER B 386 TRP B 393
SITE 4 AD1 18 PHE B 449 TYR B 489 PHE B 490 PHE B 560
SITE 5 AD1 18 HIS B 600 HOH B 976
CRYST1 150.333 150.333 226.478 90.00 90.00 120.00 P 61 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 0.006652 0.003840 0.000000 0.00000
SCALE2 0.000000 0.007681 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004415 0.00000
TER 4290 ASN A 699
TER 8580 ASN B 699
MASTER 363 0 10 46 28 0 18 6 9015 2 141 84
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