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HEADER HYDROLASE 14-SEP-11 4A16
TITLE STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEX WITH HUPRINE
TITLE 2 DERIVATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RESIDUES 35-574;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: CHO-K1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGS
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.CARLETTI,J.P.COLLETIER,F.NACHON,M.WEIK,C.RONCO,L.JEAN,P.Y.RENARD
REVDAT 1 28-MAR-12 4A16 0
JRNL AUTH C.RONCO,E.CARLETTI,J.P.COLLETIER,M.WEIK,F.NACHON,L.JEAN,
JRNL AUTH 2 P.Y.RENARD
JRNL TITL NEW HUPRINES DERIVATIVES AS SUBNANOMOLAR HUMAN
JRNL TITL 2 ACETYLCHOLINESTERASE INHIBITORS : FROM A RATIONAL DESIGN TO
JRNL TITL 3 VALIDATION BY X-RAY CRYSTALLOGRAPHY
JRNL REF CHEMMEDCHEM V. 7 400 2012
JRNL REFN ISSN 1860-7179
JRNL DOI 10.1002/CMDC.201100438
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.00
REMARK 3 NUMBER OF REFLECTIONS : 150577
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.15667
REMARK 3 R VALUE (WORKING SET) : 0.15517
REMARK 3 FREE R VALUE : 0.20563
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.0
REMARK 3 FREE R VALUE TEST SET COUNT : 4658
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.650
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.719
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10974
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.278
REMARK 3 BIN FREE R VALUE SET COUNT : 340
REMARK 3 BIN FREE R VALUE : 0.344
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16868
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 209
REMARK 3 SOLVENT ATOMS : 2323
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.829
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05
REMARK 3 B22 (A**2) : -0.06
REMARK 3 B33 (A**2) : 0.01
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.214
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.198
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.149
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.445
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 17603 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 24108 ; 2.138 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2182 ; 7.498 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 797 ;34.234 ;22.848
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2537 ;19.283 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 147 ;21.193 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2565 ; 0.144 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 10819 ; 1.068 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17442 ; 2.074 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6784 ; 3.140 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6653 ; 5.226 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 543
REMARK 3 ORIGIN FOR THE GROUP (A): 5.7405 -28.5189 86.4020
REMARK 3 T TENSOR
REMARK 3 T11: 0.0172 T22: 0.0546
REMARK 3 T33: 0.0625 T12: -0.0243
REMARK 3 T13: 0.0088 T23: -0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 0.1962 L22: 0.6953
REMARK 3 L33: 0.2017 L12: 0.0973
REMARK 3 L13: -0.0503 L23: -0.0818
REMARK 3 S TENSOR
REMARK 3 S11: -0.0056 S12: 0.0308 S13: -0.0160
REMARK 3 S21: 0.0628 S22: -0.0039 S23: 0.0119
REMARK 3 S31: -0.0092 S32: -0.0224 S33: 0.0096
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 4 B 543
REMARK 3 ORIGIN FOR THE GROUP (A): -7.4964 27.4349 66.1349
REMARK 3 T TENSOR
REMARK 3 T11: 0.1189 T22: 0.0765
REMARK 3 T33: 0.0488 T12: 0.0910
REMARK 3 T13: 0.0464 T23: 0.0321
REMARK 3 L TENSOR
REMARK 3 L11: 0.1555 L22: 0.7145
REMARK 3 L33: 0.5608 L12: -0.0712
REMARK 3 L13: 0.0883 L23: -0.3935
REMARK 3 S TENSOR
REMARK 3 S11: -0.0084 S12: -0.0082 S13: -0.0513
REMARK 3 S21: 0.1320 S22: 0.0875 S23: 0.1079
REMARK 3 S31: -0.1848 S32: -0.1115 S33: -0.0791
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 4 C 543
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6372 12.3774 25.0398
REMARK 3 T TENSOR
REMARK 3 T11: 0.0300 T22: 0.0675
REMARK 3 T33: 0.0513 T12: 0.0185
REMARK 3 T13: 0.0309 T23: 0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 0.1510 L22: 0.1910
REMARK 3 L33: 0.6552 L12: -0.0258
REMARK 3 L13: 0.0899 L23: -0.0655
REMARK 3 S TENSOR
REMARK 3 S11: -0.0416 S12: 0.0131 S13: -0.0277
REMARK 3 S21: -0.0006 S22: -0.0104 S23: -0.0041
REMARK 3 S31: -0.0136 S32: 0.0779 S33: 0.0520
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 4 D 543
REMARK 3 ORIGIN FOR THE GROUP (A): 47.7352 5.6872 81.3389
REMARK 3 T TENSOR
REMARK 3 T11: 0.0169 T22: 0.0900
REMARK 3 T33: 0.0713 T12: -0.0230
REMARK 3 T13: -0.0294 T23: 0.0524
REMARK 3 L TENSOR
REMARK 3 L11: 0.1824 L22: 0.2365
REMARK 3 L33: 0.8716 L12: -0.0867
REMARK 3 L13: 0.2157 L23: -0.1135
REMARK 3 S TENSOR
REMARK 3 S11: 0.0030 S12: 0.0635 S13: 0.0348
REMARK 3 S21: 0.0296 S22: -0.0650 S23: -0.0309
REMARK 3 S31: -0.0085 S32: 0.1445 S33: 0.0620
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 4A16 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-SEP-11.
REMARK 100 THE PDBE ID CODE IS EBI-49648.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9765
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 210)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 155235
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.65
REMARK 200 RESOLUTION RANGE LOW (A) : 50.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.7
REMARK 200 R MERGE (I) : 0.01
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.5
REMARK 200 R MERGE FOR SHELL (I) : 0.07
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: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1MAA
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BICINE BUFFER PH 9, 1.6 M
REMARK 280 AMMONIUM SULFATE.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 68.97000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 112.66000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 85.96500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 112.66000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 68.97000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 85.96500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 3680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -125.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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
REMARK 350 BIOMOLECULE: 2
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: 3370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -115.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 THR A 545
REMARK 465 GLU A 546
REMARK 465 ALA A 547
REMARK 465 PRO A 548
REMARK 465 THR B 545
REMARK 465 GLU B 546
REMARK 465 ALA B 547
REMARK 465 PRO B 548
REMARK 465 THR C 545
REMARK 465 GLU C 546
REMARK 465 ALA C 547
REMARK 465 PRO C 548
REMARK 465 THR D 545
REMARK 465 GLU D 546
REMARK 465 ALA D 547
REMARK 465 PRO D 548
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 493 CG CD NE CZ NH1 NH2
REMARK 470 ALA A 544 CA C O CB
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
REMARK 470 ALA B 544 CA C O CB
REMARK 470 ARG C 493 CG CD NE CZ NH1 NH2
REMARK 470 ALA C 544 CA C O CB
REMARK 470 ARG D 493 CG CD NE CZ NH1 NH2
REMARK 470 ALA D 544 CA C O CB
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 OD2 ASP A 5 OH TYR A 105 2.13
REMARK 500 O THR A 63 O HOH A 2113 2.07
REMARK 500 O VAL A 73 O HOH A 2142 2.19
REMARK 500 OH TYR A 77 O HOH A 2151 1.94
REMARK 500 NE ARG A 219 O HOH A 2342 2.15
REMARK 500 NH2 ARG A 219 O HOH A 2342 1.93
REMARK 500 O PHE A 346 O HOH A 2465 2.18
REMARK 500 N LYS A 348 O HOH A 2151 2.19
REMARK 500 CB LEU A 540 O HOH A 2502 2.18
REMARK 500 NH1 ARG B 245 O HOH B 2254 1.96
REMARK 500 C GLY B 256 O HOH B 2270 2.14
REMARK 500 N CYS B 257 O HOH B 2270 1.80
REMARK 500 O PRO B 259 O HOH B 2274 1.98
REMARK 500 CA ALA B 262 O HOH B 2277 1.96
REMARK 500 ND2 ASN B 464 O HOH B 2436 2.00
REMARK 500 O ASP B 494 O HOH B 2452 1.96
REMARK 500 CB GLU C 4 O HOH C 2001 1.60
REMARK 500 NE ARG C 13 O HOH C 2027 2.08
REMARK 500 NH1 ARG C 107 O HOH C 2195 2.05
REMARK 500 O PRO C 108 O HOH C 2194 2.11
REMARK 500 OD1 ASN C 265 O HOH C 2355 2.12
REMARK 500 CD1 LEU C 339 O HOH C 2439 2.10
REMARK 500 NH2 ARG C 485 O HOH C 2243 2.10
REMARK 500 NH1 ARG D 11 O HOH D 2016 2.08
REMARK 500 NH2 ARG D 54 O HOH D 2077 2.20
REMARK 500 O PRO D 108 O HOH D 2169 2.00
REMARK 500 N MET D 211 O HOH D 2261 2.11
REMARK 500 CD PRO D 258 O HOH D 2303 1.81
REMARK 500 CA GLY D 261 O HOH A 2659 2.07
REMARK 500 OD2 ASP D 304 O HOH D 2227 2.17
REMARK 500 O ALA D 419 O HOH D 2437 2.19
REMARK 500 O HOH A 2001 O HOH A 2006 2.14
REMARK 500 O HOH A 2025 O HOH A 2047 2.18
REMARK 500 O HOH A 2186 O HOH A 2394 2.08
REMARK 500 O HOH A 2193 O HOH D 2338 2.12
REMARK 500 O HOH A 2319 O HOH A 2639 1.83
REMARK 500 O HOH A 2356 O HOH A 2376 2.05
REMARK 500 O HOH A 2361 O HOH A 2362 2.00
REMARK 500 O HOH A 2390 O HOH A 2392 2.18
REMARK 500 O HOH A 2460 O HOH A 2573 2.18
REMARK 500 O HOH A 2567 O HOH A 2575 2.11
REMARK 500 O HOH B 2043 O HOH B 2130 2.03
REMARK 500 O HOH B 2107 O HOH B 2245 2.16
REMARK 500 O HOH B 2281 O HOH B 2285 2.19
REMARK 500 O HOH C 2115 O HOH C 2176 2.20
REMARK 500 O HOH C 2293 O HOH C 2600 1.81
REMARK 500 O HOH C 2325 O HOH C 2329 2.05
REMARK 500 O HOH C 2458 O HOH C 2459 1.80
REMARK 500 O HOH C 2566 O HOH C 2567 2.18
REMARK 500 O HOH C 2581 O HOH C 2582 2.06
REMARK 500
REMARK 500 THIS ENTRY HAS 57 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH C 2024 O HOH D 2077 2554 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 VAL A 340 CB VAL A 340 CG2 -0.138
REMARK 500 CYS B 96 CB CYS B 96 SG 0.119
REMARK 500 GLU B 268 CG GLU B 268 CD 0.154
REMARK 500 GLU C 4 CD GLU C 4 OE2 0.107
REMARK 500 GLU C 268 CG GLU C 268 CD 0.107
REMARK 500 ASP C 304 CB ASP C 304 CG 0.131
REMARK 500 TYR C 428 CB TYR C 428 CG 0.092
REMARK 500 GLU D 81 CB GLU D 81 CG 0.143
REMARK 500 GLU D 81 CG GLU D 81 CD 0.114
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 LEU A 17 CA - CB - CG ANGL. DEV. = 17.9 DEGREES
REMARK 500 ARG A 219 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 475 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 522 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 LEU A 540 CA - CB - CG ANGL. DEV. = 27.5 DEGREES
REMARK 500 MET B 211 CG - SD - CE ANGL. DEV. = 10.5 DEGREES
REMARK 500 LEU B 251 CA - CB - CG ANGL. DEV. = -14.5 DEGREES
REMARK 500 ARG B 253 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 253 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 CYS B 257 N - CA - C ANGL. DEV. = 20.6 DEGREES
REMARK 500 GLY B 263 N - CA - C ANGL. DEV. = 18.3 DEGREES
REMARK 500 ARG B 475 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 CYS B 529 CA - CB - SG ANGL. DEV. = -8.5 DEGREES
REMARK 500 GLU C 4 OE1 - CD - OE2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ARG C 13 NE - CZ - NH1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ARG C 18 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 PRO C 111 C - N - CA ANGL. DEV. = 10.9 DEGREES
REMARK 500 ARG C 246 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 PRO C 258 C - N - CA ANGL. DEV. = -14.1 DEGREES
REMARK 500 LEU C 269 CA - CB - CG ANGL. DEV. = 15.4 DEGREES
REMARK 500 ILE C 294 CB - CA - C ANGL. DEV. = -12.3 DEGREES
REMARK 500 ASP C 310 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG D 245 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG D 245 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 CYS D 257 CA - CB - SG ANGL. DEV. = -15.7 DEGREES
REMARK 500 CYS D 257 CB - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 PRO D 258 C - N - CA ANGL. DEV. = -16.5 DEGREES
REMARK 500 ASP D 266 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG D 274 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 LEU D 380 CA - CB - CG ANGL. DEV. = 14.1 DEGREES
REMARK 500 ASP D 404 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG D 475 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG D 475 NE - CZ - NH2 ANGL. DEV. = -3.8 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 47 -9.80 79.51
REMARK 500 ALA A 62 50.92 -109.93
REMARK 500 PRO A 104 150.04 -47.25
REMARK 500 ALA A 167 74.24 -166.46
REMARK 500 SER A 203 -125.32 57.78
REMARK 500 ALA A 262 -120.16 -114.15
REMARK 500 ASP A 306 -78.49 -109.07
REMARK 500 GLU A 351 -7.27 -59.18
REMARK 500 VAL A 407 -58.71 -130.83
REMARK 500 ASP A 494 165.83 173.99
REMARK 500 LYS A 496 75.71 75.97
REMARK 500 PRO A 498 -165.78 -71.87
REMARK 500 LEU B 8 25.17 -74.19
REMARK 500 PHE B 47 -6.14 71.86
REMARK 500 ALA B 62 52.72 -101.54
REMARK 500 CYS B 96 -6.99 -153.46
REMARK 500 LEU B 97 80.41 -68.16
REMARK 500 ARG B 107 137.43 -34.26
REMARK 500 ALA B 109 -97.40 -12.03
REMARK 500 PRO B 111 103.67 -37.74
REMARK 500 ALA B 189 -18.26 -45.53
REMARK 500 PRO B 194 2.21 -58.32
REMARK 500 SER B 203 -124.78 53.61
REMARK 500 PRO B 217 -7.57 -59.38
REMARK 500 VAL B 255 -148.29 -93.48
REMARK 500 CYS B 257 94.10 81.43
REMARK 500 ALA B 262 -22.32 -141.28
REMARK 500 ASP B 306 -84.04 -119.23
REMARK 500 ASP B 323 31.83 -96.25
REMARK 500 ASN B 350 -157.96 -91.02
REMARK 500 SER B 352 63.73 62.04
REMARK 500 ASP B 390 106.42 -59.42
REMARK 500 VAL B 407 -65.00 -127.11
REMARK 500 PRO B 440 162.69 -49.73
REMARK 500 LEU B 459 -116.53 -48.48
REMARK 500 ASP B 460 92.15 6.25
REMARK 500 ASN B 464 34.70 79.56
REMARK 500 THR B 466 163.86 -41.96
REMARK 500 ASP B 488 117.11 -171.61
REMARK 500 LYS B 496 126.17 71.30
REMARK 500 SER B 497 -53.15 -148.95
REMARK 500 PRO B 498 -154.20 -88.94
REMARK 500 LEU B 518 116.52 -39.87
REMARK 500 ALA B 542 71.13 61.61
REMARK 500 PHE C 47 -10.10 75.79
REMARK 500 ALA C 62 51.96 -116.60
REMARK 500 SER C 110 118.22 70.74
REMARK 500 PRO C 111 114.60 -32.55
REMARK 500 ALA C 167 78.20 -150.61
REMARK 500 PRO C 194 -9.61 -58.32
REMARK 500
REMARK 500 THIS ENTRY HAS 78 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 CYS A 257 PRO A 258 132.25
REMARK 500 GLY B 256 CYS B 257 126.43
REMARK 500 CYS C 257 PRO C 258 139.04
REMARK 500 SER C 495 LYS C 496 -148.41
REMARK 500 ALA C 542 THR C 543 133.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLU A 166 22.5 L L OUTSIDE RANGE
REMARK 500 VAL A 340 24.8 L L OUTSIDE RANGE
REMARK 500 TYR A 449 24.7 L L OUTSIDE RANGE
REMARK 500 SER A 497 24.0 L L OUTSIDE RANGE
REMARK 500 LEU A 540 22.6 L L OUTSIDE RANGE
REMARK 500 CYS B 257 12.8 L L OUTSIDE RANGE
REMARK 500 LYS C 23 23.9 L L OUTSIDE RANGE
REMARK 500 ALA C 262 23.6 L L OUTSIDE RANGE
REMARK 500 GLU D 4 25.0 L L OUTSIDE RANGE
REMARK 500 CYS D 257 11.6 L L OUTSIDE RANGE
REMARK 500 ARG D 493 23.0 L L OUTSIDE RANGE
REMARK 500 ASP D 494 23.4 L L OUTSIDE RANGE
REMARK 500 SER D 497 24.6 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG B 1546
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H34 A1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H34 B1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H34 C1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H34 D1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1549
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WHQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY
REMARK 900 SARIN (AGED) IN COMPLEX WITH HI-6
REMARK 900 RELATED ID: 2JGH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED VX
REMARK 900 RELATED ID: 1MAH RELATED DB: PDB
REMARK 900 FASCICULIN2 - MOUSE ACETYLCHOLINESTERASE COMPLEX
REMARK 900 RELATED ID: 1MAA RELATED DB: PDB
REMARK 900 MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN,
REMARK 900 GLYCOSYLATEDPROTEIN
REMARK 900 RELATED ID: 2HA6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 MOUSEACETYLCHOLINESTERASE COMPLEXED WITH SUCCINYLCHOLINE
REMARK 900 RELATED ID: 2JGG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED SARIN
REMARK 900 RELATED ID: 2C0Q RELATED DB: PDB
REMARK 900 NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN
REMARK 900 RELATED ID: 2JGL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED VX AND SARIN
REMARK 900 RELATED ID: 2XUG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (
REMARK 900 1 WK)
REMARK 900 RELATED ID: 1Q84 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 TZ2PA6ANTI COMPLEX
REMARK 900 RELATED ID: 2XUD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE Y337A MUTANT OF MOUSE
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2JGM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)
REMARK 900 RELATED ID: 2XUJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1
REMARK 900 MTH)
REMARK 900 RELATED ID: 1Q83 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 TZ2PA6SYN COMPLEX
REMARK 900 RELATED ID: 2JGE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED METHAMIDOPHOS
REMARK 900 RELATED ID: 2WLS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUS MUSCULUS ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH AMTS13
REMARK 900 RELATED ID: 2XUP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX
REMARK 900 WITH SOAKED TZ2PA6 SYN INHIBITOR
REMARK 900 RELATED ID: 2XUK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (
REMARK 900 10 MTH)
REMARK 900 RELATED ID: 2HA3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH CHOLINE
REMARK 900 RELATED ID: 2Y2U RELATED DB: PDB
REMARK 900 NONAGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY
REMARK 900 VX-UPDATE
REMARK 900 RELATED ID: 1C2B RELATED DB: PDB
REMARK 900 ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2HA0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH 4-KETOAMYLTRIMETHYLAMMONIUM
REMARK 900 RELATED ID: 2XUF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (
REMARK 900 1 MTH)
REMARK 900 RELATED ID: 2WU3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH FENAMIPHOS AND HI-6
REMARK 900 RELATED ID: 2JEY RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH HLO-7
REMARK 900 RELATED ID: 2JGI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)
REMARK 900 RELATED ID: 1N5R RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 PROPIDIUM COMPLEX
REMARK 900 RELATED ID: 2XUH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (
REMARK 900 10 MTH)
REMARK 900 RELATED ID: 2JGJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED METHAMIDOPHOS
REMARK 900 RELATED ID: 1J06 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN THE
REMARK 900 APOFORM
REMARK 900 RELATED ID: 2C0P RELATED DB: PDB
REMARK 900 AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN
REMARK 900 RELATED ID: 2JF0 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN
REMARK 900 AND ORTHO-7
REMARK 900 RELATED ID: 2XUO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A MUTANT IN COMPLEX
REMARK 900 WITH SOAKED TZ2PA6 ANTI INHIBITOR
REMARK 900 RELATED ID: 2XUI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1
REMARK 900 WK)
REMARK 900 RELATED ID: 2H9Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH M-(N,N,N-TRIMETHYLAMMONIO)
REMARK 900 TRIFLUOROACETOPHENONE
REMARK 900 RELATED ID: 2WHR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 K027
REMARK 900 RELATED ID: 1N5M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 GALLAMINE COMPLEX
REMARK 900 RELATED ID: 2HA5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 ACETYLCHOLINESTERASECOMPLEXED WITH ACETYLTHIOCHOLINE
REMARK 900 RELATED ID: 2XUQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX
REMARK 900 WITH SOAKED TZ2PA6 ANTI-SYN INHIBITORS
REMARK 900 RELATED ID: 2HA2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH SUCCINYLCHOLINE
REMARK 900 RELATED ID: 2WHP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY
REMARK 900 SARIN AND IN COMPLEX WITH HI-6
REMARK 900 RELATED ID: 2JEZ RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN
REMARK 900 AND HLO-7
REMARK 900 RELATED ID: 2JGK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED FENAMIPHOS
REMARK 900 RELATED ID: 1KU6 RELATED DB: PDB
REMARK 900 FASCICULIN 2-MOUSE ACETYLCHOLINESTERASE COMPLEX
REMARK 900 RELATED ID: 2HA4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 MOUSEACETYLCHOLINESTERASE COMPLEXED WITH ACETYLCHOLINE
REMARK 900 RELATED ID: 1J07 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 DECIDIUM COMPLEX
REMARK 900 RELATED ID: 2HA7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 MOUSEACETYLCHOLINESTERASE COMPLEXED WITH BUTYRYLTHIOCHOLINE
REMARK 900 RELATED ID: 2JGF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED FENAMIPHOS
REMARK 900 RELATED ID: 2WU4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH FENAMIPHOS AND ORTHO-7
REMARK 900 RELATED ID: 2Y2V RELATED DB: PDB
REMARK 900 NONAGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY
REMARK 900 SARIN-UPDATE
REMARK 900 RELATED ID: 1C2O RELATED DB: PDB
REMARK 900 ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CONTAINS MUTATION L544STOP TO PRODUCE TRUNCATION
DBREF 4A16 A 4 543 UNP P21836 ACES_MOUSE 35 574
DBREF 4A16 B 4 543 UNP P21836 ACES_MOUSE 35 574
DBREF 4A16 C 4 543 UNP P21836 ACES_MOUSE 35 574
DBREF 4A16 D 4 543 UNP P21836 ACES_MOUSE 35 574
SEQADV 4A16 ALA A 544 UNP P21836 EXPRESSION TAG
SEQADV 4A16 THR A 545 UNP P21836 EXPRESSION TAG
SEQADV 4A16 GLU A 546 UNP P21836 EXPRESSION TAG
SEQADV 4A16 ALA A 547 UNP P21836 EXPRESSION TAG
SEQADV 4A16 PRO A 548 UNP P21836 EXPRESSION TAG
SEQADV 4A16 ALA B 544 UNP P21836 EXPRESSION TAG
SEQADV 4A16 THR B 545 UNP P21836 EXPRESSION TAG
SEQADV 4A16 GLU B 546 UNP P21836 EXPRESSION TAG
SEQADV 4A16 ALA B 547 UNP P21836 EXPRESSION TAG
SEQADV 4A16 PRO B 548 UNP P21836 EXPRESSION TAG
SEQADV 4A16 ALA C 544 UNP P21836 EXPRESSION TAG
SEQADV 4A16 THR C 545 UNP P21836 EXPRESSION TAG
SEQADV 4A16 GLU C 546 UNP P21836 EXPRESSION TAG
SEQADV 4A16 ALA C 547 UNP P21836 EXPRESSION TAG
SEQADV 4A16 PRO C 548 UNP P21836 EXPRESSION TAG
SEQADV 4A16 ALA D 544 UNP P21836 EXPRESSION TAG
SEQADV 4A16 THR D 545 UNP P21836 EXPRESSION TAG
SEQADV 4A16 GLU D 546 UNP P21836 EXPRESSION TAG
SEQADV 4A16 ALA D 547 UNP P21836 EXPRESSION TAG
SEQADV 4A16 PRO D 548 UNP P21836 EXPRESSION TAG
SEQRES 1 A 545 GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG GLY GLY GLN
SEQRES 2 A 545 LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY GLY PRO VAL
SEQRES 3 A 545 SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL
SEQRES 4 A 545 GLY SER ARG ARG PHE MET PRO PRO GLU PRO LYS ARG PRO
SEQRES 5 A 545 TRP SER GLY VAL LEU ASP ALA THR THR PHE GLN ASN VAL
SEQRES 6 A 545 CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU
SEQRES 7 A 545 GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU
SEQRES 8 A 545 ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG
SEQRES 9 A 545 PRO ALA SER PRO THR PRO VAL LEU ILE TRP ILE TYR GLY
SEQRES 10 A 545 GLY GLY PHE TYR SER GLY ALA ALA SER LEU ASP VAL TYR
SEQRES 11 A 545 ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY ALA VAL LEU
SEQRES 12 A 545 VAL SER MET ASN TYR ARG VAL GLY THR PHE GLY PHE LEU
SEQRES 13 A 545 ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 A 545 LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU
SEQRES 15 A 545 ASN ILE ALA ALA PHE GLY GLY ASP PRO MET SER VAL THR
SEQRES 16 A 545 LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET
SEQRES 17 A 545 HIS ILE LEU SER LEU PRO SER ARG SER LEU PHE HIS ARG
SEQRES 18 A 545 ALA VAL LEU GLN SER GLY THR PRO ASN GLY PRO TRP ALA
SEQRES 19 A 545 THR VAL SER ALA GLY GLU ALA ARG ARG ARG ALA THR LEU
SEQRES 20 A 545 LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY GLY ALA GLY
SEQRES 21 A 545 GLY ASN ASP THR GLU LEU ILE ALA CYS LEU ARG THR ARG
SEQRES 22 A 545 PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP HIS VAL LEU
SEQRES 23 A 545 PRO GLN GLU SER ILE PHE ARG PHE SER PHE VAL PRO VAL
SEQRES 24 A 545 VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU
SEQRES 25 A 545 ILE ASN THR GLY ASP PHE GLN ASP LEU GLN VAL LEU VAL
SEQRES 26 A 545 GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR
SEQRES 27 A 545 GLY VAL PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE
SEQRES 28 A 545 SER ARG ALA GLN PHE LEU ALA GLY VAL ARG ILE GLY VAL
SEQRES 29 A 545 PRO GLN ALA SER ASP LEU ALA ALA GLU ALA VAL VAL LEU
SEQRES 30 A 545 HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO THR HIS
SEQRES 31 A 545 LEU ARG ASP ALA MET SER ALA VAL VAL GLY ASP HIS ASN
SEQRES 32 A 545 VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA
SEQRES 33 A 545 ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE PHE GLU HIS
SEQRES 34 A 545 ARG ALA SER THR LEU THR TRP PRO LEU TRP MET GLY VAL
SEQRES 35 A 545 PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY LEU PRO
SEQRES 36 A 545 LEU ASP PRO SER LEU ASN TYR THR THR GLU GLU ARG ILE
SEQRES 37 A 545 PHE ALA GLN ARG LEU MET LYS TYR TRP THR ASN PHE ALA
SEQRES 38 A 545 ARG THR GLY ASP PRO ASN ASP PRO ARG ASP SER LYS SER
SEQRES 39 A 545 PRO GLN TRP PRO PRO TYR THR THR ALA ALA GLN GLN TYR
SEQRES 40 A 545 VAL SER LEU ASN LEU LYS PRO LEU GLU VAL ARG ARG GLY
SEQRES 41 A 545 LEU ARG ALA GLN THR CYS ALA PHE TRP ASN ARG PHE LEU
SEQRES 42 A 545 PRO LYS LEU LEU SER ALA THR ALA THR GLU ALA PRO
SEQRES 1 B 545 GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG GLY GLY GLN
SEQRES 2 B 545 LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY GLY PRO VAL
SEQRES 3 B 545 SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL
SEQRES 4 B 545 GLY SER ARG ARG PHE MET PRO PRO GLU PRO LYS ARG PRO
SEQRES 5 B 545 TRP SER GLY VAL LEU ASP ALA THR THR PHE GLN ASN VAL
SEQRES 6 B 545 CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU
SEQRES 7 B 545 GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU
SEQRES 8 B 545 ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG
SEQRES 9 B 545 PRO ALA SER PRO THR PRO VAL LEU ILE TRP ILE TYR GLY
SEQRES 10 B 545 GLY GLY PHE TYR SER GLY ALA ALA SER LEU ASP VAL TYR
SEQRES 11 B 545 ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY ALA VAL LEU
SEQRES 12 B 545 VAL SER MET ASN TYR ARG VAL GLY THR PHE GLY PHE LEU
SEQRES 13 B 545 ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 B 545 LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU
SEQRES 15 B 545 ASN ILE ALA ALA PHE GLY GLY ASP PRO MET SER VAL THR
SEQRES 16 B 545 LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET
SEQRES 17 B 545 HIS ILE LEU SER LEU PRO SER ARG SER LEU PHE HIS ARG
SEQRES 18 B 545 ALA VAL LEU GLN SER GLY THR PRO ASN GLY PRO TRP ALA
SEQRES 19 B 545 THR VAL SER ALA GLY GLU ALA ARG ARG ARG ALA THR LEU
SEQRES 20 B 545 LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY GLY ALA GLY
SEQRES 21 B 545 GLY ASN ASP THR GLU LEU ILE ALA CYS LEU ARG THR ARG
SEQRES 22 B 545 PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP HIS VAL LEU
SEQRES 23 B 545 PRO GLN GLU SER ILE PHE ARG PHE SER PHE VAL PRO VAL
SEQRES 24 B 545 VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU
SEQRES 25 B 545 ILE ASN THR GLY ASP PHE GLN ASP LEU GLN VAL LEU VAL
SEQRES 26 B 545 GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR
SEQRES 27 B 545 GLY VAL PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE
SEQRES 28 B 545 SER ARG ALA GLN PHE LEU ALA GLY VAL ARG ILE GLY VAL
SEQRES 29 B 545 PRO GLN ALA SER ASP LEU ALA ALA GLU ALA VAL VAL LEU
SEQRES 30 B 545 HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO THR HIS
SEQRES 31 B 545 LEU ARG ASP ALA MET SER ALA VAL VAL GLY ASP HIS ASN
SEQRES 32 B 545 VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA
SEQRES 33 B 545 ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE PHE GLU HIS
SEQRES 34 B 545 ARG ALA SER THR LEU THR TRP PRO LEU TRP MET GLY VAL
SEQRES 35 B 545 PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY LEU PRO
SEQRES 36 B 545 LEU ASP PRO SER LEU ASN TYR THR THR GLU GLU ARG ILE
SEQRES 37 B 545 PHE ALA GLN ARG LEU MET LYS TYR TRP THR ASN PHE ALA
SEQRES 38 B 545 ARG THR GLY ASP PRO ASN ASP PRO ARG ASP SER LYS SER
SEQRES 39 B 545 PRO GLN TRP PRO PRO TYR THR THR ALA ALA GLN GLN TYR
SEQRES 40 B 545 VAL SER LEU ASN LEU LYS PRO LEU GLU VAL ARG ARG GLY
SEQRES 41 B 545 LEU ARG ALA GLN THR CYS ALA PHE TRP ASN ARG PHE LEU
SEQRES 42 B 545 PRO LYS LEU LEU SER ALA THR ALA THR GLU ALA PRO
SEQRES 1 C 545 GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG GLY GLY GLN
SEQRES 2 C 545 LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY GLY PRO VAL
SEQRES 3 C 545 SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL
SEQRES 4 C 545 GLY SER ARG ARG PHE MET PRO PRO GLU PRO LYS ARG PRO
SEQRES 5 C 545 TRP SER GLY VAL LEU ASP ALA THR THR PHE GLN ASN VAL
SEQRES 6 C 545 CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU
SEQRES 7 C 545 GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU
SEQRES 8 C 545 ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG
SEQRES 9 C 545 PRO ALA SER PRO THR PRO VAL LEU ILE TRP ILE TYR GLY
SEQRES 10 C 545 GLY GLY PHE TYR SER GLY ALA ALA SER LEU ASP VAL TYR
SEQRES 11 C 545 ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY ALA VAL LEU
SEQRES 12 C 545 VAL SER MET ASN TYR ARG VAL GLY THR PHE GLY PHE LEU
SEQRES 13 C 545 ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 C 545 LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU
SEQRES 15 C 545 ASN ILE ALA ALA PHE GLY GLY ASP PRO MET SER VAL THR
SEQRES 16 C 545 LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET
SEQRES 17 C 545 HIS ILE LEU SER LEU PRO SER ARG SER LEU PHE HIS ARG
SEQRES 18 C 545 ALA VAL LEU GLN SER GLY THR PRO ASN GLY PRO TRP ALA
SEQRES 19 C 545 THR VAL SER ALA GLY GLU ALA ARG ARG ARG ALA THR LEU
SEQRES 20 C 545 LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY GLY ALA GLY
SEQRES 21 C 545 GLY ASN ASP THR GLU LEU ILE ALA CYS LEU ARG THR ARG
SEQRES 22 C 545 PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP HIS VAL LEU
SEQRES 23 C 545 PRO GLN GLU SER ILE PHE ARG PHE SER PHE VAL PRO VAL
SEQRES 24 C 545 VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU
SEQRES 25 C 545 ILE ASN THR GLY ASP PHE GLN ASP LEU GLN VAL LEU VAL
SEQRES 26 C 545 GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR
SEQRES 27 C 545 GLY VAL PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE
SEQRES 28 C 545 SER ARG ALA GLN PHE LEU ALA GLY VAL ARG ILE GLY VAL
SEQRES 29 C 545 PRO GLN ALA SER ASP LEU ALA ALA GLU ALA VAL VAL LEU
SEQRES 30 C 545 HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO THR HIS
SEQRES 31 C 545 LEU ARG ASP ALA MET SER ALA VAL VAL GLY ASP HIS ASN
SEQRES 32 C 545 VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA
SEQRES 33 C 545 ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE PHE GLU HIS
SEQRES 34 C 545 ARG ALA SER THR LEU THR TRP PRO LEU TRP MET GLY VAL
SEQRES 35 C 545 PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY LEU PRO
SEQRES 36 C 545 LEU ASP PRO SER LEU ASN TYR THR THR GLU GLU ARG ILE
SEQRES 37 C 545 PHE ALA GLN ARG LEU MET LYS TYR TRP THR ASN PHE ALA
SEQRES 38 C 545 ARG THR GLY ASP PRO ASN ASP PRO ARG ASP SER LYS SER
SEQRES 39 C 545 PRO GLN TRP PRO PRO TYR THR THR ALA ALA GLN GLN TYR
SEQRES 40 C 545 VAL SER LEU ASN LEU LYS PRO LEU GLU VAL ARG ARG GLY
SEQRES 41 C 545 LEU ARG ALA GLN THR CYS ALA PHE TRP ASN ARG PHE LEU
SEQRES 42 C 545 PRO LYS LEU LEU SER ALA THR ALA THR GLU ALA PRO
SEQRES 1 D 545 GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG GLY GLY GLN
SEQRES 2 D 545 LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY GLY PRO VAL
SEQRES 3 D 545 SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL
SEQRES 4 D 545 GLY SER ARG ARG PHE MET PRO PRO GLU PRO LYS ARG PRO
SEQRES 5 D 545 TRP SER GLY VAL LEU ASP ALA THR THR PHE GLN ASN VAL
SEQRES 6 D 545 CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU
SEQRES 7 D 545 GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU
SEQRES 8 D 545 ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG
SEQRES 9 D 545 PRO ALA SER PRO THR PRO VAL LEU ILE TRP ILE TYR GLY
SEQRES 10 D 545 GLY GLY PHE TYR SER GLY ALA ALA SER LEU ASP VAL TYR
SEQRES 11 D 545 ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY ALA VAL LEU
SEQRES 12 D 545 VAL SER MET ASN TYR ARG VAL GLY THR PHE GLY PHE LEU
SEQRES 13 D 545 ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 D 545 LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU
SEQRES 15 D 545 ASN ILE ALA ALA PHE GLY GLY ASP PRO MET SER VAL THR
SEQRES 16 D 545 LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET
SEQRES 17 D 545 HIS ILE LEU SER LEU PRO SER ARG SER LEU PHE HIS ARG
SEQRES 18 D 545 ALA VAL LEU GLN SER GLY THR PRO ASN GLY PRO TRP ALA
SEQRES 19 D 545 THR VAL SER ALA GLY GLU ALA ARG ARG ARG ALA THR LEU
SEQRES 20 D 545 LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY GLY ALA GLY
SEQRES 21 D 545 GLY ASN ASP THR GLU LEU ILE ALA CYS LEU ARG THR ARG
SEQRES 22 D 545 PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP HIS VAL LEU
SEQRES 23 D 545 PRO GLN GLU SER ILE PHE ARG PHE SER PHE VAL PRO VAL
SEQRES 24 D 545 VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU
SEQRES 25 D 545 ILE ASN THR GLY ASP PHE GLN ASP LEU GLN VAL LEU VAL
SEQRES 26 D 545 GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR
SEQRES 27 D 545 GLY VAL PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE
SEQRES 28 D 545 SER ARG ALA GLN PHE LEU ALA GLY VAL ARG ILE GLY VAL
SEQRES 29 D 545 PRO GLN ALA SER ASP LEU ALA ALA GLU ALA VAL VAL LEU
SEQRES 30 D 545 HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO THR HIS
SEQRES 31 D 545 LEU ARG ASP ALA MET SER ALA VAL VAL GLY ASP HIS ASN
SEQRES 32 D 545 VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA
SEQRES 33 D 545 ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE PHE GLU HIS
SEQRES 34 D 545 ARG ALA SER THR LEU THR TRP PRO LEU TRP MET GLY VAL
SEQRES 35 D 545 PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY LEU PRO
SEQRES 36 D 545 LEU ASP PRO SER LEU ASN TYR THR THR GLU GLU ARG ILE
SEQRES 37 D 545 PHE ALA GLN ARG LEU MET LYS TYR TRP THR ASN PHE ALA
SEQRES 38 D 545 ARG THR GLY ASP PRO ASN ASP PRO ARG ASP SER LYS SER
SEQRES 39 D 545 PRO GLN TRP PRO PRO TYR THR THR ALA ALA GLN GLN TYR
SEQRES 40 D 545 VAL SER LEU ASN LEU LYS PRO LEU GLU VAL ARG ARG GLY
SEQRES 41 D 545 LEU ARG ALA GLN THR CYS ALA PHE TRP ASN ARG PHE LEU
SEQRES 42 D 545 PRO LYS LEU LEU SER ALA THR ALA THR GLU ALA PRO
HET H34 A1545 30
HET SO4 A1546 5
HET SO4 A1547 5
HET SO4 A1548 5
HET CL A1549 1
HET CL A1550 1
HET H34 B1545 30
HET NAG B1546 14
HET SO4 B1547 5
HET SO4 B1548 5
HET SO4 B1549 5
HET SO4 B1550 5
HET CL B1551 1
HET H34 C1545 30
HET SO4 C1546 5
HET SO4 C1547 5
HET SO4 C1548 5
HET CL C1549 1
HET CL C1550 1
HET H34 D1545 30
HET SO4 D1546 5
HET SO4 D1547 5
HET SO4 D1548 5
HET SO4 D1549 5
HETNAM H34 (1-{4-[(7S,11S)-12-AMINO-3-CHLORO-6,7,10,11-
HETNAM 2 H34 TETRAHYDRO-7,11-METHANOCYCLOOCTA[B]QUINOLIN-9-
HETNAM 3 H34 YL]BUTYL}-1H-1,2,3-TRIAZOL-4-YL)METHANOL
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 5 H34 4(C23 H26 CL N5 O)
FORMUL 6 SO4 14(O4 S 2-)
FORMUL 7 CL 5(CL 1-)
FORMUL 8 NAG C8 H15 N O6
FORMUL 9 HOH *2323(H2 O)
HELIX 1 1 VAL A 42 ARG A 46 5 5
HELIX 2 2 PHE A 80 MET A 85 1 6
HELIX 3 3 LEU A 130 ASP A 134 5 5
HELIX 4 4 GLY A 135 GLY A 143 1 9
HELIX 5 5 VAL A 153 LEU A 159 1 7
HELIX 6 6 ASN A 170 ILE A 187 1 18
HELIX 7 7 ALA A 188 PHE A 190 5 3
HELIX 8 8 SER A 203 LEU A 214 1 12
HELIX 9 9 SER A 215 SER A 220 1 6
HELIX 10 10 SER A 240 VAL A 255 1 16
HELIX 11 11 ASN A 265 THR A 275 1 11
HELIX 12 12 PRO A 277 GLU A 285 1 9
HELIX 13 13 TRP A 286 LEU A 289 5 4
HELIX 14 14 THR A 311 GLY A 319 1 9
HELIX 15 15 GLY A 335 VAL A 343 1 9
HELIX 16 16 SER A 355 VAL A 367 1 13
HELIX 17 17 SER A 371 THR A 383 1 13
HELIX 18 18 ASP A 390 VAL A 407 1 18
HELIX 19 19 VAL A 407 GLN A 421 1 15
HELIX 20 20 PRO A 440 GLY A 444 5 5
HELIX 21 21 GLU A 450 PHE A 455 1 6
HELIX 22 22 GLY A 456 ASP A 460 5 5
HELIX 23 23 ASP A 460 ASN A 464 5 5
HELIX 24 24 THR A 466 GLY A 487 1 22
HELIX 25 25 ARG A 525 ARG A 534 1 10
HELIX 26 26 ARG A 534 ALA A 542 1 9
HELIX 27 27 ASP B 5 GLN B 7 5 3
HELIX 28 28 VAL B 42 ARG B 46 5 5
HELIX 29 29 PHE B 80 MET B 85 1 6
HELIX 30 30 LEU B 130 ASP B 134 5 5
HELIX 31 31 GLY B 135 VAL B 141 1 7
HELIX 32 32 VAL B 153 LEU B 159 1 7
HELIX 33 33 ASN B 170 ILE B 187 1 18
HELIX 34 34 ALA B 188 PHE B 190 5 3
HELIX 35 35 SER B 203 SER B 215 1 13
HELIX 36 36 LEU B 216 PHE B 222 5 7
HELIX 37 37 ALA B 241 VAL B 255 1 15
HELIX 38 38 ASN B 265 THR B 275 1 11
HELIX 39 39 PRO B 277 ASP B 283 1 7
HELIX 40 40 HIS B 284 LEU B 289 5 6
HELIX 41 41 THR B 311 GLY B 319 1 9
HELIX 42 42 GLY B 335 VAL B 343 1 9
HELIX 43 43 SER B 355 VAL B 367 1 13
HELIX 44 44 SER B 371 THR B 383 1 13
HELIX 45 45 ASP B 390 VAL B 407 1 18
HELIX 46 46 VAL B 407 GLN B 421 1 15
HELIX 47 47 PRO B 440 GLY B 444 5 5
HELIX 48 48 GLU B 450 GLY B 456 1 7
HELIX 49 49 ASP B 460 ASN B 464 5 5
HELIX 50 50 THR B 466 GLY B 487 1 22
HELIX 51 51 ARG B 525 ARG B 534 1 10
HELIX 52 52 ARG B 534 SER B 541 1 8
HELIX 53 53 VAL C 42 ARG C 46 5 5
HELIX 54 54 PHE C 80 MET C 85 1 6
HELIX 55 55 LEU C 130 ASP C 134 5 5
HELIX 56 56 GLY C 135 GLY C 143 1 9
HELIX 57 57 VAL C 153 LEU C 159 1 7
HELIX 58 58 ASN C 170 ILE C 187 1 18
HELIX 59 59 ALA C 188 PHE C 190 5 3
HELIX 60 60 SER C 203 LEU C 214 1 12
HELIX 61 61 SER C 215 SER C 220 1 6
HELIX 62 62 ALA C 241 VAL C 255 1 15
HELIX 63 63 ASN C 265 ARG C 274 1 10
HELIX 64 64 PRO C 277 ASP C 283 1 7
HELIX 65 65 HIS C 284 LEU C 289 5 6
HELIX 66 66 THR C 311 THR C 318 1 8
HELIX 67 67 GLY C 335 VAL C 343 1 9
HELIX 68 68 SER C 355 VAL C 367 1 13
HELIX 69 69 SER C 371 THR C 383 1 13
HELIX 70 70 ASP C 390 VAL C 407 1 18
HELIX 71 71 VAL C 407 GLN C 421 1 15
HELIX 72 72 PRO C 440 GLY C 444 5 5
HELIX 73 73 GLU C 450 PHE C 455 1 6
HELIX 74 74 GLY C 456 ASP C 460 5 5
HELIX 75 75 ASP C 460 ASN C 464 5 5
HELIX 76 76 THR C 466 GLY C 487 1 22
HELIX 77 77 ARG C 525 ARG C 534 1 10
HELIX 78 78 ARG C 534 SER C 541 1 8
HELIX 79 79 ASP D 5 GLN D 7 5 3
HELIX 80 80 VAL D 42 ARG D 46 5 5
HELIX 81 81 PHE D 80 MET D 85 1 6
HELIX 82 82 LEU D 130 ASP D 134 5 5
HELIX 83 83 GLY D 135 GLY D 143 1 9
HELIX 84 84 VAL D 153 LEU D 159 1 7
HELIX 85 85 ASN D 170 ILE D 187 1 18
HELIX 86 86 ALA D 188 PHE D 190 5 3
HELIX 87 87 SER D 203 SER D 215 1 13
HELIX 88 88 SER D 215 SER D 220 1 6
HELIX 89 89 ALA D 241 VAL D 255 1 15
HELIX 90 90 ASN D 265 ARG D 274 1 10
HELIX 91 91 PRO D 277 ASP D 283 1 7
HELIX 92 92 HIS D 284 LEU D 289 5 6
HELIX 93 93 THR D 311 GLY D 319 1 9
HELIX 94 94 GLY D 335 VAL D 343 1 9
HELIX 95 95 SER D 355 VAL D 367 1 13
HELIX 96 96 SER D 371 THR D 383 1 13
HELIX 97 97 ASP D 390 VAL D 407 1 18
HELIX 98 98 VAL D 407 GLN D 421 1 15
HELIX 99 99 PRO D 440 GLY D 444 5 5
HELIX 100 100 GLU D 450 GLY D 456 1 7
HELIX 101 101 LEU D 457 ASN D 464 5 8
HELIX 102 102 THR D 466 GLY D 487 1 22
HELIX 103 103 ARG D 525 PHE D 535 1 11
HELIX 104 104 PHE D 535 THR D 543 1 9
SHEET 1 AA 3 LEU A 9 VAL A 12 0
SHEET 2 AA 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 AA 3 VAL A 59 ASP A 61 1 O LEU A 60 N ARG A 18
SHEET 1 AB11 ILE A 20 ALA A 24 0
SHEET 2 AB11 GLY A 27 PRO A 36 -1 O GLY A 27 N ALA A 24
SHEET 3 AB11 TYR A 98 PRO A 104 -1 O LEU A 99 N ILE A 35
SHEET 4 AB11 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 5 AB11 THR A 112 ILE A 118 1 O PRO A 113 N VAL A 145
SHEET 6 AB11 GLY A 192 GLU A 202 1 N ASP A 193 O THR A 112
SHEET 7 AB11 ARG A 224 GLN A 228 1 O ARG A 224 N LEU A 199
SHEET 8 AB11 GLN A 325 VAL A 331 1 O GLN A 325 N ALA A 225
SHEET 9 AB11 ARG A 424 PHE A 430 1 O ARG A 424 N VAL A 326
SHEET 10 AB11 GLN A 509 LEU A 513 1 O VAL A 511 N ILE A 429
SHEET 11 AB11 GLU A 519 ARG A 522 -1 O GLU A 519 N SER A 512
SHEET 1 AC 2 VAL A 68 CYS A 69 0
SHEET 2 AC 2 LEU A 92 SER A 93 1 N SER A 93 O VAL A 68
SHEET 1 BA 3 LEU B 9 VAL B 12 0
SHEET 2 BA 3 GLY B 15 ARG B 18 -1 O GLY B 15 N VAL B 12
SHEET 3 BA 3 VAL B 59 ASP B 61 1 O LEU B 60 N ARG B 18
SHEET 1 BB11 ILE B 20 ALA B 24 0
SHEET 2 BB11 GLY B 27 PRO B 36 -1 O GLY B 27 N ALA B 24
SHEET 3 BB11 TYR B 98 PRO B 104 -1 O LEU B 99 N ILE B 35
SHEET 4 BB11 VAL B 145 MET B 149 -1 O LEU B 146 N TRP B 102
SHEET 5 BB11 THR B 112 ILE B 118 1 O PRO B 113 N VAL B 145
SHEET 6 BB11 GLY B 192 GLU B 202 1 N ASP B 193 O THR B 112
SHEET 7 BB11 ARG B 224 GLN B 228 1 O ARG B 224 N LEU B 199
SHEET 8 BB11 GLN B 325 VAL B 331 1 O GLN B 325 N ALA B 225
SHEET 9 BB11 ARG B 424 PHE B 430 1 O ARG B 424 N VAL B 326
SHEET 10 BB11 GLN B 509 LEU B 513 1 O VAL B 511 N ILE B 429
SHEET 11 BB11 GLU B 519 ARG B 522 -1 O GLU B 519 N SER B 512
SHEET 1 BC 2 VAL B 68 CYS B 69 0
SHEET 2 BC 2 LEU B 92 SER B 93 1 N SER B 93 O VAL B 68
SHEET 1 BD 2 VAL B 239 SER B 240 0
SHEET 2 BD 2 VAL B 302 VAL B 303 1 N VAL B 303 O VAL B 239
SHEET 1 CA 3 LEU C 9 VAL C 12 0
SHEET 2 CA 3 GLY C 15 ARG C 18 -1 O GLY C 15 N VAL C 12
SHEET 3 CA 3 VAL C 59 ASP C 61 1 O LEU C 60 N ARG C 18
SHEET 1 CB11 ILE C 20 ALA C 24 0
SHEET 2 CB11 GLY C 27 PRO C 36 -1 O GLY C 27 N ALA C 24
SHEET 3 CB11 TYR C 98 PRO C 104 -1 O LEU C 99 N ILE C 35
SHEET 4 CB11 VAL C 145 MET C 149 -1 O LEU C 146 N TRP C 102
SHEET 5 CB11 THR C 112 ILE C 118 1 O PRO C 113 N VAL C 145
SHEET 6 CB11 GLY C 192 GLU C 202 1 N ASP C 193 O THR C 112
SHEET 7 CB11 ARG C 224 GLN C 228 1 O ARG C 224 N LEU C 199
SHEET 8 CB11 GLN C 325 VAL C 331 1 O GLN C 325 N ALA C 225
SHEET 9 CB11 ARG C 424 PHE C 430 1 O ARG C 424 N VAL C 326
SHEET 10 CB11 GLN C 509 LEU C 513 1 O VAL C 511 N ILE C 429
SHEET 11 CB11 GLU C 519 ARG C 522 -1 O GLU C 519 N SER C 512
SHEET 1 CC 2 VAL C 68 CYS C 69 0
SHEET 2 CC 2 LEU C 92 SER C 93 1 N SER C 93 O VAL C 68
SHEET 1 CD 2 VAL C 239 SER C 240 0
SHEET 2 CD 2 VAL C 302 VAL C 303 1 N VAL C 303 O VAL C 239
SHEET 1 DA 3 LEU D 9 VAL D 12 0
SHEET 2 DA 3 GLY D 15 ARG D 18 -1 O GLY D 15 N VAL D 12
SHEET 3 DA 3 VAL D 59 ASP D 61 1 O LEU D 60 N ARG D 18
SHEET 1 DB11 ILE D 20 ALA D 24 0
SHEET 2 DB11 GLY D 27 PRO D 36 -1 O GLY D 27 N ALA D 24
SHEET 3 DB11 TYR D 98 PRO D 104 -1 O LEU D 99 N ILE D 35
SHEET 4 DB11 VAL D 145 MET D 149 -1 O LEU D 146 N TRP D 102
SHEET 5 DB11 THR D 112 ILE D 118 1 O PRO D 113 N VAL D 145
SHEET 6 DB11 GLY D 192 GLU D 202 1 N ASP D 193 O THR D 112
SHEET 7 DB11 ARG D 224 GLN D 228 1 O ARG D 224 N LEU D 199
SHEET 8 DB11 GLN D 325 VAL D 331 1 O GLN D 325 N ALA D 225
SHEET 9 DB11 ARG D 424 PHE D 430 1 O ARG D 424 N VAL D 326
SHEET 10 DB11 GLN D 509 LEU D 513 1 O VAL D 511 N ILE D 429
SHEET 11 DB11 GLU D 519 ARG D 522 -1 O GLU D 519 N SER D 512
SHEET 1 DC 2 VAL D 68 CYS D 69 0
SHEET 2 DC 2 LEU D 92 SER D 93 1 N SER D 93 O VAL D 68
SHEET 1 DD 2 VAL D 239 SER D 240 0
SHEET 2 DD 2 VAL D 302 VAL D 303 1 N VAL D 303 O VAL D 239
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.16
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.20
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.12
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.10
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.27
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.14
SSBOND 7 CYS C 69 CYS C 96 1555 1555 2.12
SSBOND 8 CYS C 257 CYS C 272 1555 1555 2.19
SSBOND 9 CYS C 409 CYS C 529 1555 1555 2.16
SSBOND 10 CYS D 69 CYS D 96 1555 1555 2.09
SSBOND 11 CYS D 257 CYS D 272 1555 1555 2.27
SSBOND 12 CYS D 409 CYS D 529 1555 1555 2.10
CISPEP 1 TYR A 105 PRO A 106 0 -5.69
CISPEP 2 PRO A 258 PRO A 259 0 25.99
CISPEP 3 SER A 497 PRO A 498 0 -11.09
CISPEP 4 TYR B 105 PRO B 106 0 3.33
CISPEP 5 CYS B 257 PRO B 258 0 -11.13
CISPEP 6 SER B 497 PRO B 498 0 -10.09
CISPEP 7 TYR C 105 PRO C 106 0 -1.22
CISPEP 8 PRO C 258 PRO C 259 0 9.22
CISPEP 9 SER C 497 PRO C 498 0 -4.37
CISPEP 10 TYR D 105 PRO D 106 0 1.91
CISPEP 11 SER D 497 PRO D 498 0 3.17
SITE 1 AC1 16 TRP A 86 GLY A 121 TYR A 124 GLU A 202
SITE 2 AC1 16 SER A 203 TRP A 286 PHE A 295 TYR A 337
SITE 3 AC1 16 PHE A 338 TYR A 341 TRP A 439 HIS A 447
SITE 4 AC1 16 TYR A 449 HOH A2148 HOH A2157 HOH A2428
SITE 1 AC2 5 ARG A 525 ALA A 526 GLN A 527 THR A 528
SITE 2 AC2 5 HOH A2660
SITE 1 AC3 3 GLN A 413 ARG A 417 ASN A 533
SITE 1 AC4 5 ARG A 356 LEU A 360 HOH A2661 HOH A2663
SITE 2 AC4 5 ARG B 534
SITE 1 AC5 3 ARG A 136 HOH A2057 HOH A2060
SITE 1 AC6 3 HOH A2174 HOH A2183 HOH A2250
SITE 1 AC7 19 TRP B 86 GLY B 120 GLY B 121 TYR B 124
SITE 2 AC7 19 GLU B 202 SER B 203 TRP B 286 PHE B 295
SITE 3 AC7 19 ARG B 296 PHE B 297 TYR B 337 PHE B 338
SITE 4 AC7 19 TYR B 341 TRP B 439 HIS B 447 TYR B 449
SITE 5 AC7 19 HOH B2095 HOH B2325 HOH B2496
SITE 1 AC8 9 ASN B 265 GLU B 268 HOH B2287 HOH B2294
SITE 2 AC8 9 HOH B2497 HOH B2498 HOH B2499 HOH B2501
SITE 3 AC8 9 HOH B2502
SITE 1 AC9 5 ARG B 525 ALA B 526 GLN B 527 THR B 528
SITE 2 AC9 5 HOH B2477
SITE 1 BC1 5 HIS B 387 PRO B 388 GLU B 389 ASP B 390
SITE 2 BC1 5 HOH B2403
SITE 1 BC2 3 ARG A 534 ARG B 356 HOH B2503
SITE 1 BC3 3 GLN B 413 ARG B 417 ASN B 533
SITE 1 BC4 2 HOH B2474 HOH B2475
SITE 1 BC5 20 HOH B2276 TRP C 86 GLY C 121 TYR C 124
SITE 2 BC5 20 GLU C 202 SER C 203 TRP C 286 SER C 293
SITE 3 BC5 20 ILE C 294 PHE C 295 ARG C 296 TYR C 337
SITE 4 BC5 20 PHE C 338 TYR C 341 TRP C 439 HIS C 447
SITE 5 BC5 20 TYR C 449 HOH C2133 HOH C2220 HOH C2396
SITE 1 BC6 5 ARG C 525 ALA C 526 GLN C 527 THR C 528
SITE 2 BC6 5 HOH C2604
SITE 1 BC7 5 VAL C 42 GLY C 43 SER C 44 HOH C2620
SITE 2 BC7 5 HOH C2621
SITE 1 BC8 3 GLN C 413 ARG C 417 HOH C2613
SITE 1 BC9 3 GLU C 452 HOH C2522 HOH C2523
SITE 1 CC1 2 ARG C 136 HOH C2044
SITE 1 CC2 17 TRP D 86 GLY D 121 TYR D 124 GLU D 202
SITE 2 CC2 17 TRP D 286 SER D 293 PHE D 295 ARG D 296
SITE 3 CC2 17 TYR D 337 PHE D 338 TYR D 341 TRP D 439
SITE 4 CC2 17 HIS D 447 TYR D 449 HOH D2114 HOH D2349
SITE 5 CC2 17 HOH D2529
SITE 1 CC3 6 ARG D 525 ALA D 526 GLN D 527 THR D 528
SITE 2 CC3 6 HOH D2511 HOH D2518
SITE 1 CC4 2 ARG D 356 HOH D2530
SITE 1 CC5 3 GLN D 413 ARG D 417 ASN D 533
SITE 1 CC6 5 GLU D 519 ARG D 521 ARG D 522 HOH D2505
SITE 2 CC6 5 HOH D2533
CRYST1 137.940 171.930 225.320 90.00 90.00 90.00 P 21 21 21 16
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 0.007250 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005816 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004438 0.00000
TER 4237 ALA A 544
TER 8454 ALA B 544
TER 12657 ALA C 544
TER 16872 ALA D 544
MASTER 885 0 24 104 70 0 49 619400 4 228 168
END |