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HEADER HYDROLASE 29-OCT-15 5EIE
TITLE MACHE-TZ2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7;
COMPND 6 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 GENE: ACHE;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293
KEYWDS ACETYLCHOLINESTERASE, INHIBITOR, CLICK CHEMISTRY, TACRINE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.BOURNE,P.MARCHOT
REVDAT 1 20-JAN-16 5EIE 0
JRNL AUTH Y.BOURNE,K.B.SHARPLESS,P.TAYLOR,P.MARCHOT
JRNL TITL STERIC AND DYNAMIC PARAMETERS INFLUENCING IN SITU
JRNL TITL 2 CYCLOADDITIONS TO FORM TRIAZOLE INHIBITORS WITH CRYSTALLINE
JRNL TITL 3 ACETYLCHOLINESTERASE.
JRNL REF J.AM.CHEM.SOC. 2016
JRNL REFN ESSN 1520-5126
JRNL PMID 26731630
JRNL DOI 10.1021/JACS.5B11384
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 115553
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.990
REMARK 3 FREE R VALUE TEST SET COUNT : 2294
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.15
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.86
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 6624
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2114
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6493
REMARK 3 BIN R VALUE (WORKING SET) : 0.2115
REMARK 3 BIN FREE R VALUE : 0.2067
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.98
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 131
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8357
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 177
REMARK 3 SOLVENT ATOMS : 669
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.08
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -9.16200
REMARK 3 B22 (A**2) : -6.85420
REMARK 3 B33 (A**2) : 16.01620
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.250
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.132
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.118
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.129
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.117
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 8939 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 12234 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2997 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 197 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1339 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 8939 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1111 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 10904 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.05
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.71
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.52
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 27.7447 12.5218 16.6451
REMARK 3 T TENSOR
REMARK 3 T11: -0.0509 T22: -0.0598
REMARK 3 T33: -0.1249 T12: 0.0042
REMARK 3 T13: 0.0047 T23: 0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 0.7278 L22: 0.7031
REMARK 3 L33: 1.7955 L12: -0.0907
REMARK 3 L13: 0.0741 L23: -0.3723
REMARK 3 S TENSOR
REMARK 3 S11: -0.0799 S12: 0.0035 S13: -0.0643
REMARK 3 S21: -0.0400 S22: 0.0016 S23: -0.0008
REMARK 3 S31: 0.1923 S32: -0.0588 S33: 0.0783
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7847 4.7572 -40.1465
REMARK 3 T TENSOR
REMARK 3 T11: -0.0849 T22: -0.0777
REMARK 3 T33: -0.1707 T12: -0.0173
REMARK 3 T13: -0.0082 T23: -0.0766
REMARK 3 L TENSOR
REMARK 3 L11: 0.6447 L22: 1.1154
REMARK 3 L33: 2.4612 L12: -0.0545
REMARK 3 L13: 0.1552 L23: 0.8016
REMARK 3 S TENSOR
REMARK 3 S11: 0.1193 S12: 0.0752 S13: -0.0568
REMARK 3 S21: 0.1234 S22: -0.1668 S23: 0.1079
REMARK 3 S31: 0.2284 S32: -0.0473 S33: 0.0475
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5EIE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214959.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5-8.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.931
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 115553
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 46.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05500
REMARK 200 FOR THE DATA SET : 22.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : 0.59700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 1J06
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25-30% PEG 550 MME OR PEG 600, 60-100
REMARK 280 MM HEPES OR SODIUM ACETATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
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 39.83000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.19500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.56000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.19500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.83000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.56000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 12.0 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 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 260
REMARK 465 GLY A 261
REMARK 465 ALA A 262
REMARK 465 GLY A 263
REMARK 465 GLY A 264
REMARK 465 GLU B 1
REMARK 465 GLY B 2
REMARK 465 PRO B 259
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 ALA B 262
REMARK 465 GLY B 263
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 TYR A 341 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 THR A 543 OG1 CG2
REMARK 470 ARG B 3 CG CD NE CZ NH1 NH2
REMARK 470 TYR B 341 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
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 B 493 CB - CA - C ANGL. DEV. = -25.4 DEGREES
REMARK 500 ARG B 493 N - CA - C ANGL. DEV. = 39.6 DEGREES
REMARK 500 ASP B 494 C - N - CA ANGL. DEV. = 26.1 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 -2.61 76.40
REMARK 500 TYR A 77 79.76 -118.29
REMARK 500 SER A 203 -116.94 59.55
REMARK 500 ASP A 306 -85.54 -123.74
REMARK 500 VAL A 407 -60.66 -126.61
REMARK 500 PHE B 47 -2.06 76.62
REMARK 500 ALA B 62 50.21 -115.49
REMARK 500 SER B 203 -116.98 59.70
REMARK 500 ASP B 306 -86.09 -123.57
REMARK 500 VAL B 407 -61.68 -126.97
REMARK 500 PRO B 492 25.33 -68.64
REMARK 500 ARG B 493 -35.08 -138.17
REMARK 500 ASP B 494 81.36 -62.23
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 ARG B 493 ASP B 494 147.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1061 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH A1062 DISTANCE = 6.13 ANGSTROMS
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 7PG B 606
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TZ2 A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TZ2 B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7PG B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 601 through NAG A 603 bound to ASN A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 604 bound
REMARK 800 to ASN A 464
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 601 bound
REMARK 800 to ASN B 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 602 bound
REMARK 800 to ASN B 464
DBREF 5EIE A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 5EIE B 1 543 UNP P21836 ACES_MOUSE 32 574
SEQRES 1 A 543 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 A 543 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 A 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 A 543 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 A 543 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 A 543 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 A 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 A 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 A 543 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 A 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 A 543 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 A 543 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 A 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 A 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 A 543 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 A 543 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 A 543 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 A 543 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 A 543 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 A 543 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 A 543 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 A 543 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 A 543 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 A 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 A 543 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 A 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 A 543 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 A 543 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 A 543 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 A 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 A 543 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 A 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 A 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 A 543 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 A 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 A 543 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 A 543 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 A 543 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 A 543 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 A 543 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 A 543 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 A 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 1 B 543 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 B 543 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 B 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 B 543 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 B 543 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 B 543 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 B 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 B 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 B 543 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 B 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 B 543 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 B 543 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 B 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 B 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 B 543 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 B 543 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 B 543 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 B 543 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 B 543 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 B 543 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 B 543 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 B 543 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 B 543 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 B 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 B 543 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 B 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 B 543 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 B 543 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 B 543 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 B 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 B 543 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 B 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 B 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 B 543 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 B 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 B 543 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 B 543 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 B 543 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 B 543 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 B 543 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 B 543 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 B 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR
HET NAG A 601 14
HET FUC A 602 10
HET NAG A 603 14
HET NAG A 604 14
HET TZ2 A 605 20
HET ACT A 606 4
HET PG4 A 607 13
HET NAG B 601 14
HET NAG B 602 14
HET CL B 603 1
HET TZ2 B 604 20
HET ACT B 605 4
HET 7PG B 606 22
HET PG4 B 607 13
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM TZ2 ~{N}-(2-AZIDOETHYL)-1,2,3,4-TETRAHYDROACRIDIN-9-AMINE
HETNAM ACT ACETATE ION
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM CL CHLORIDE ION
HETNAM 7PG 2,5,8,11,14,17,20,23-OCTAOXAPENTACOSAN-25-OL
FORMUL 3 NAG 5(C8 H15 N O6)
FORMUL 3 FUC C6 H12 O5
FORMUL 5 TZ2 2(C15 H17 N5)
FORMUL 6 ACT 2(C2 H3 O2 1-)
FORMUL 7 PG4 2(C8 H18 O5)
FORMUL 10 CL CL 1-
FORMUL 13 7PG C17 H36 O9
FORMUL 15 HOH *669(H2 O)
HELIX 1 AA1 ASP A 5 GLN A 7 5 3
HELIX 2 AA2 VAL A 42 ARG A 46 5 5
HELIX 3 AA3 PHE A 80 MET A 85 1 6
HELIX 4 AA4 LEU A 130 ASP A 134 5 5
HELIX 5 AA5 GLY A 135 GLY A 143 1 9
HELIX 6 AA6 VAL A 153 LEU A 159 1 7
HELIX 7 AA7 ASN A 170 ILE A 187 1 18
HELIX 8 AA8 ALA A 188 PHE A 190 5 3
HELIX 9 AA9 SER A 203 SER A 215 1 13
HELIX 10 AB1 SER A 215 SER A 220 1 6
HELIX 11 AB2 SER A 240 VAL A 255 1 16
HELIX 12 AB3 ASP A 266 THR A 275 1 10
HELIX 13 AB4 PRO A 277 GLU A 285 1 9
HELIX 14 AB5 TRP A 286 LEU A 289 5 4
HELIX 15 AB6 THR A 311 GLY A 319 1 9
HELIX 16 AB7 GLY A 335 VAL A 343 1 9
HELIX 17 AB8 SER A 355 VAL A 367 1 13
HELIX 18 AB9 SER A 371 THR A 383 1 13
HELIX 19 AC1 ASP A 390 VAL A 407 1 18
HELIX 20 AC2 VAL A 407 GLN A 421 1 15
HELIX 21 AC3 PRO A 440 GLY A 444 5 5
HELIX 22 AC4 GLU A 450 PHE A 455 1 6
HELIX 23 AC5 GLY A 456 ASN A 464 5 9
HELIX 24 AC6 THR A 466 GLY A 487 1 22
HELIX 25 AC7 ARG A 525 ARG A 534 1 10
HELIX 26 AC8 ARG A 534 THR A 543 1 10
HELIX 27 AC9 ASP B 5 GLN B 7 5 3
HELIX 28 AD1 VAL B 42 ARG B 46 5 5
HELIX 29 AD2 PHE B 80 MET B 85 1 6
HELIX 30 AD3 LEU B 130 ASP B 134 5 5
HELIX 31 AD4 GLY B 135 GLY B 143 1 9
HELIX 32 AD5 VAL B 153 LEU B 159 1 7
HELIX 33 AD6 ASN B 170 ILE B 187 1 18
HELIX 34 AD7 ALA B 188 PHE B 190 5 3
HELIX 35 AD8 SER B 203 SER B 215 1 13
HELIX 36 AD9 SER B 215 SER B 220 1 6
HELIX 37 AE1 ALA B 241 VAL B 255 1 15
HELIX 38 AE2 ASN B 265 THR B 275 1 11
HELIX 39 AE3 PRO B 277 TRP B 286 1 10
HELIX 40 AE4 THR B 311 GLY B 319 1 9
HELIX 41 AE5 GLY B 335 VAL B 343 1 9
HELIX 42 AE6 SER B 355 VAL B 367 1 13
HELIX 43 AE7 SER B 371 THR B 383 1 13
HELIX 44 AE8 ASP B 390 VAL B 407 1 18
HELIX 45 AE9 VAL B 407 GLN B 421 1 15
HELIX 46 AF1 PRO B 440 GLY B 444 5 5
HELIX 47 AF2 GLU B 450 PHE B 455 1 6
HELIX 48 AF3 GLY B 456 ASN B 464 5 9
HELIX 49 AF4 THR B 466 GLY B 487 1 22
HELIX 50 AF5 ARG B 525 ARG B 534 1 10
HELIX 51 AF6 ARG B 534 ALA B 542 1 9
SHEET 1 AA1 3 LEU A 9 VAL A 12 0
SHEET 2 AA1 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 AA1 3 VAL A 59 ASP A 61 1 O LEU A 60 N GLN A 16
SHEET 1 AA211 ILE A 20 ALA A 24 0
SHEET 2 AA211 GLY A 27 PRO A 36 -1 O ALA A 31 N ILE A 20
SHEET 3 AA211 TYR A 98 PRO A 104 -1 O VAL A 101 N PHE A 32
SHEET 4 AA211 VAL A 145 MET A 149 -1 O SER A 148 N ASN A 100
SHEET 5 AA211 THR A 112 ILE A 118 1 N TRP A 117 O VAL A 147
SHEET 6 AA211 GLY A 192 GLU A 202 1 O ASP A 193 N THR A 112
SHEET 7 AA211 ARG A 224 GLN A 228 1 O GLN A 228 N GLY A 201
SHEET 8 AA211 GLN A 325 VAL A 331 1 O LEU A 327 N LEU A 227
SHEET 9 AA211 ARG A 424 PHE A 430 1 O ARG A 424 N VAL A 326
SHEET 10 AA211 GLN A 509 LEU A 513 1 O LEU A 513 N ILE A 429
SHEET 11 AA211 GLU A 519 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 AA3 2 VAL A 68 CYS A 69 0
SHEET 2 AA3 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68
SHEET 1 AA4 3 LEU B 9 VAL B 12 0
SHEET 2 AA4 3 GLY B 15 ARG B 18 -1 O GLY B 15 N VAL B 12
SHEET 3 AA4 3 VAL B 59 ASP B 61 1 O LEU B 60 N GLN B 16
SHEET 1 AA511 ILE B 20 ALA B 24 0
SHEET 2 AA511 GLY B 27 PRO B 36 -1 O VAL B 29 N LEU B 22
SHEET 3 AA511 TYR B 98 PRO B 104 -1 O LEU B 99 N ILE B 35
SHEET 4 AA511 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 AA511 THR B 112 ILE B 118 1 N TRP B 117 O VAL B 147
SHEET 6 AA511 GLY B 192 GLU B 202 1 O ASP B 193 N THR B 112
SHEET 7 AA511 ARG B 224 GLN B 228 1 O GLN B 228 N GLY B 201
SHEET 8 AA511 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 AA511 ARG B 424 PHE B 430 1 O ARG B 424 N VAL B 326
SHEET 10 AA511 GLN B 509 LEU B 513 1 O LEU B 513 N ILE B 429
SHEET 11 AA511 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 AA6 2 VAL B 68 CYS B 69 0
SHEET 2 AA6 2 LEU B 92 SER B 93 1 O SER B 93 N VAL B 68
SHEET 1 AA7 2 VAL B 239 SER B 240 0
SHEET 2 AA7 2 VAL B 302 VAL B 303 1 O VAL B 303 N VAL B 239
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.06
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.11
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.06
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.05
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.07
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.06
LINK ND2 ASN A 350 C1 NAG A 601 1555 1555 1.44
LINK ND2 ASN A 464 C1 NAG A 604 1555 1555 1.43
LINK ND2 ASN B 350 C1 NAG B 601 1555 1555 1.43
LINK ND2 ASN B 464 C1 NAG B 602 1555 1555 1.44
LINK O4 NAG A 601 C1 NAG A 603 1555 1555 1.43
LINK O6 NAG A 601 C1 FUC A 602 1555 1555 1.40
CISPEP 1 TYR A 105 PRO A 106 0 -2.21
CISPEP 2 TYR B 105 PRO B 106 0 -0.02
CISPEP 3 CYS B 257 PRO B 258 0 1.47
SITE 1 AC1 10 TRP A 86 TYR A 124 GLU A 202 PHE A 297
SITE 2 AC1 10 TYR A 337 PHE A 338 TRP A 439 HIS A 447
SITE 3 AC1 10 TYR A 449 ACT A 606
SITE 1 AC2 7 GLY A 121 GLY A 122 SER A 203 ALA A 204
SITE 2 AC2 7 PHE A 297 HIS A 447 TZ2 A 605
SITE 1 AC3 6 HIS A 381 ASP A 384 HIS A 393 ARG A 525
SITE 2 AC3 6 THR A 528 HOH A 710
SITE 1 AC4 3 ARG B 296 PRO B 368 GLN B 369
SITE 1 AC5 11 TRP B 86 GLY B 121 TYR B 124 GLU B 202
SITE 2 AC5 11 PHE B 297 TYR B 337 PHE B 338 TRP B 439
SITE 3 AC5 11 HIS B 447 TYR B 449 ACT B 605
SITE 1 AC6 7 GLY B 121 GLY B 122 SER B 203 ALA B 204
SITE 2 AC6 7 PHE B 297 HIS B 447 TZ2 B 604
SITE 1 AC7 12 LEU A 380 HIS A 381 GLN A 527 PHE A 535
SITE 2 AC7 12 ALA B 377 LEU B 380 HIS B 381 GLN B 527
SITE 3 AC7 12 PHE B 531 PHE B 535 PG4 B 607 HOH B 755
SITE 1 AC8 4 GLN A 527 HIS B 381 TYR B 382 7PG B 606
SITE 1 AC9 8 PRO A 344 GLY A 345 PHE A 346 SER A 347
SITE 2 AC9 8 ASN A 350 GLN A 358 HOH A 712 HOH A 780
SITE 1 AD1 1 ASN A 464
SITE 1 AD2 2 SER B 347 ASN B 350
SITE 1 AD3 2 SER B 462 ASN B 464
CRYST1 79.660 113.120 226.390 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012553 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008840 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004417 0.00000
TER 4240 THR A 543
TER 8486 THR B 543
MASTER 417 0 14 51 34 0 22 6 9203 2 192 84
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