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HEADER HYDROLASE/HYDROLASE INHIBITOR 23-AUG-17 6ARX
TITLE CRYSTAL STRUCTURE OF AN INSECTICIDE-RESISTANT ACETYLCHOLINESTERASE
TITLE 2 MUTANT FROM THE MALARIA VECTOR ANOPHELES GAMBIAE IN THE LIGAND-FREE
TITLE 3 STATE
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, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.CHEUNG,A.MAHMOOD,R.KALATHUR,L.LIXUAN,P.R.CARLIER
REVDAT 1 10-JAN-18 6ARX 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. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.10
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 125762
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 6259
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 49.1146 - 7.1461 0.99 4035 189 0.1498 0.1634
REMARK 3 2 7.1461 - 5.6748 1.00 4043 190 0.1391 0.1615
REMARK 3 3 5.6748 - 4.9582 1.00 3977 223 0.1279 0.1455
REMARK 3 4 4.9582 - 4.5052 1.00 3997 225 0.1080 0.1243
REMARK 3 5 4.5052 - 4.1825 1.00 3989 229 0.1120 0.1300
REMARK 3 6 4.1825 - 3.9360 1.00 4004 212 0.1290 0.1542
REMARK 3 7 3.9360 - 3.7390 1.00 4009 186 0.1408 0.1778
REMARK 3 8 3.7390 - 3.5763 1.00 3991 221 0.1607 0.1691
REMARK 3 9 3.5763 - 3.4386 1.00 3965 246 0.1720 0.2306
REMARK 3 10 3.4386 - 3.3200 1.00 3994 192 0.1903 0.2302
REMARK 3 11 3.3200 - 3.2162 1.00 3980 243 0.2100 0.2428
REMARK 3 12 3.2162 - 3.1243 1.00 3940 213 0.2128 0.2411
REMARK 3 13 3.1243 - 3.0421 1.00 3995 227 0.2081 0.2490
REMARK 3 14 3.0421 - 2.9678 1.00 4027 220 0.2111 0.2408
REMARK 3 15 2.9678 - 2.9004 1.00 3988 197 0.2255 0.2654
REMARK 3 16 2.9004 - 2.8387 1.00 4015 173 0.2315 0.2709
REMARK 3 17 2.8387 - 2.7819 1.00 3982 197 0.2341 0.2849
REMARK 3 18 2.7819 - 2.7294 1.00 3945 229 0.2359 0.2602
REMARK 3 19 2.7294 - 2.6807 1.00 3994 196 0.2472 0.2580
REMARK 3 20 2.6807 - 2.6352 1.00 4027 182 0.2530 0.2838
REMARK 3 21 2.6352 - 2.5927 1.00 4009 191 0.2611 0.2847
REMARK 3 22 2.5927 - 2.5528 1.00 3999 216 0.2792 0.2993
REMARK 3 23 2.5528 - 2.5153 1.00 3907 250 0.2724 0.3314
REMARK 3 24 2.5153 - 2.4799 1.00 3995 223 0.2869 0.3207
REMARK 3 25 2.4799 - 2.4463 1.00 3962 224 0.2894 0.3183
REMARK 3 26 2.4463 - 2.4146 1.00 3975 183 0.2962 0.2779
REMARK 3 27 2.4146 - 2.3844 1.00 4014 185 0.2944 0.3214
REMARK 3 28 2.3844 - 2.3557 1.00 3971 200 0.3050 0.3198
REMARK 3 29 2.3557 - 2.3283 1.00 3989 226 0.3186 0.3409
REMARK 3 30 2.3283 - 2.3021 0.94 3785 171 0.3437 0.3738
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.210
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 46.63
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.22
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 : 0.012 8935
REMARK 3 ANGLE : 1.165 12214
REMARK 3 CHIRALITY : 0.063 1297
REMARK 3 PLANARITY : 0.008 1616
REMARK 3 DIHEDRAL : 11.879 5268
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 : 5176
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6ARX 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_1000229275.
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 : 125913
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.200
REMARK 200 R MERGE (I) : 0.21000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 3.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 2.63400
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 (1.11.1_2575: ???)
REMARK 200 STARTING MODEL: 4EY4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 79.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.02
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 75.28567
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 150.57133
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 112.92850
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 188.21417
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 37.64283
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: 3400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 -74.79950
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 129.55653
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 75.28567
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 GLY A 161
REMARK 465 ASP A 162
REMARK 465 LEU A 700
REMARK 465 PRO A 701
REMARK 465 GLY A 702
REMARK 465 GLY 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 NH2 ARG A 517 OG1 FLC A 1004 2.15
REMARK 500 NH2 ARG B 676 OB2 FLC B 1002 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 376 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 GLY A 617 C - N - CA ANGL. DEV. = -13.3 DEGREES
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 -7.28 74.43
REMARK 500 THR A 221 79.13 -115.13
REMARK 500 ALA A 312 -159.87 61.28
REMARK 500 PHE A 316 12.89 -144.03
REMARK 500 SER A 360 -119.50 59.81
REMARK 500 HIS A 416 41.87 -153.17
REMARK 500 LYS A 420 70.59 -117.93
REMARK 500 GLU A 485 73.44 -119.51
REMARK 500 LEU A 495 72.93 -106.68
REMARK 500 LEU A 499 72.75 -102.62
REMARK 500 GLU A 540 73.95 -155.30
REMARK 500 PHE A 560 -77.11 -129.39
REMARK 500 ASN A 670 69.42 -108.74
REMARK 500 PHE B 206 -6.84 74.86
REMARK 500 THR B 221 77.90 -112.81
REMARK 500 ASP B 238 30.99 -91.53
REMARK 500 ALA B 312 -156.22 59.15
REMARK 500 PHE B 316 13.71 -142.29
REMARK 500 SER B 360 -119.41 61.23
REMARK 500 HIS B 416 40.98 -151.27
REMARK 500 LEU B 495 70.84 -106.13
REMARK 500 LEU B 499 73.85 -105.71
REMARK 500 GLU B 540 75.80 -155.21
REMARK 500 PHE B 560 -75.34 -129.52
REMARK 500 ASN B 670 72.65 -111.44
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 FLC A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC B 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1001
REMARK 800 bound to ASN A 220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1002
REMARK 800 bound to ASN A 670
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1001
REMARK 800 bound to ASN B 220
DBREF 6ARX A 162 702 UNP Q869C3 ACES_ANOGA 162 702
DBREF 6ARX B 162 702 UNP Q869C3 ACES_ANOGA 162 702
SEQADV 6ARX GLY A 161 UNP Q869C3 EXPRESSION TAG
SEQADV 6ARX SER A 280 UNP Q869C3 GLY 280 ENGINEERED MUTATION
SEQADV 6ARX GLY B 161 UNP Q869C3 EXPRESSION TAG
SEQADV 6ARX SER B 280 UNP Q869C3 GLY 280 ENGINEERED MUTATION
SEQRES 1 A 542 GLY 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 GLY 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 NAG A1001 14
HET NAG A1002 14
HET FLC A1003 13
HET FLC A1004 13
HET CL A1005 1
HET NAG B1001 14
HET FLC B1002 13
HET FLC B1003 13
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FLC CITRATE ANION
HETNAM CL CHLORIDE ION
FORMUL 3 NAG 3(C8 H15 N O6)
FORMUL 5 FLC 4(C6 H5 O7 3-)
FORMUL 7 CL CL 1-
FORMUL 11 HOH *360(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 LYS A 431 1 12
HELIX 11 AB2 ASP A 432 ASN A 438 1 7
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 438 1 7
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 ASP B 602 PHE B 608 1 7
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 ILE B 175 N VAL B 168
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 VAL B 260 N TRP B 191
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 GLN B 385 N GLY B 358
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 2.06
SSBOND 2 CYS A 414 CYS A 427 1555 1555 2.10
SSBOND 3 CYS A 562 CYS A 683 1555 1555 2.05
SSBOND 4 CYS B 228 CYS B 255 1555 1555 2.05
SSBOND 5 CYS B 414 CYS B 427 1555 1555 2.12
SSBOND 6 CYS B 562 CYS B 683 1555 1555 2.06
LINK ND2 ASN A 220 C1 NAG A1001 1555 1555 1.47
LINK ND2 ASN A 670 C1 NAG A1002 1555 1555 1.45
LINK ND2 ASN B 220 C1 NAG B1001 1555 1555 1.46
CISPEP 1 ARG A 264 PRO A 265 0 0.98
CISPEP 2 GLY A 677 PRO A 678 0 10.43
CISPEP 3 ARG B 264 PRO B 265 0 1.06
CISPEP 4 GLY B 677 PRO B 678 0 9.78
SITE 1 AC1 4 THR A 658 HIS A 660 HIS A 663 ARG A 676
SITE 1 AC2 4 ARG A 517 ASN A 524 GLY A 525 ARG A 528
SITE 1 AC3 3 ARG A 376 ARG A 472 GLN B 198
SITE 1 AC4 4 THR B 658 HIS B 660 HIS B 663 ARG B 676
SITE 1 AC5 4 ARG B 517 ASN B 524 GLY B 525 ARG B 528
SITE 1 AC6 2 ARG A 176 ASN A 220
SITE 1 AC7 1 ASN A 670
SITE 1 AC8 2 VAL B 218 ASN B 220
CRYST1 149.599 149.599 225.857 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 0.006685 0.003859 0.000000 0.00000
SCALE2 0.000000 0.007719 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004428 0.00000
TER 4290 ASN A 699
TER 8580 ASN B 699
MASTER 372 0 8 46 28 0 8 6 8957 2 109 84
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