| content |
HEADER HYDROLASE 20-FEB-17 5X61
TITLE CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE CATALYTIC SUBUNIT OF THE
TITLE 2 MALARIA VECTOR ANOPHELES GAMBIAE, 3.4 A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: B, A;
COMPND 4 FRAGMENT: CATALYTIC SUBUNIT, UNP RESIDUES 162-714;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7;
COMPND 7 ENGINEERED: 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: KOMAGATAELLA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPICZ* A
KEYWDS ALPHA/BETA HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.HAN,H.ROBINSON,H.DING,D.M.WONG,P.C.H.LAM,M.M.TOTROV,P.R.CARLIER,
AUTHOR 2 J.LI
REVDAT 1 15-MAR-17 5X61 0
JRNL AUTH Q.HAN,D.M.WONG,H.ROBINSON,H.DING,P.C.H.LAM,M.M.TOTROV,
JRNL AUTH 2 P.R.CARLIER,J.LI
JRNL TITL CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE CATALYTIC SUBUNITS
JRNL TITL 2 OF THE MALARIA VECTOR ANOPHELES GAMBIAE
JRNL REF INSECT SCI. 2017
JRNL REFN ISSN 1744-7917
JRNL PMID 28247978
JRNL DOI 10.1111/1744-7917.12450
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 36750
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1940
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) : 3.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2683
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.2810
REMARK 3 BIN FREE R VALUE SET COUNT : 145
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8498
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 168
REMARK 3 SOLVENT ATOMS : 6
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -0.01000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.377
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.372
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.258
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.367
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.923
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.898
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8906 ; 0.004 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12170 ; 0.929 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1072 ; 4.811 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 424 ;33.251 ;23.302
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1324 ;15.303 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 70 ;12.220 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1308 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6948 ; 0.003 ; 0.021
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5X61 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1300002990.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38760
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 64.0
REMARK 200 DATA REDUNDANCY : 20.30
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.52
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHASES
REMARK 200 STARTING MODEL: 2HA2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 78.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES BUFFER, 1.6M AMMONIUM
REMARK 280 SULFATE, 0.1M SODIUM CHLORIDE, PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, 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 75.26533
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 150.53067
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 112.89800
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 188.16333
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 37.63267
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: 7500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -173.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 ASN B 699
REMARK 465 LEU B 700
REMARK 465 PRO B 701
REMARK 465 GLY B 702
REMARK 465 PRO B 703
REMARK 465 ALA B 704
REMARK 465 PRO B 705
REMARK 465 PRO B 706
REMARK 465 SER B 707
REMARK 465 GLU B 708
REMARK 465 PRO B 709
REMARK 465 CYS B 710
REMARK 465 GLU B 711
REMARK 465 SER B 712
REMARK 465 SER B 713
REMARK 465 ALA B 714
REMARK 465 ASN A 699
REMARK 465 LEU A 700
REMARK 465 PRO A 701
REMARK 465 GLY A 702
REMARK 465 PRO A 703
REMARK 465 ALA A 704
REMARK 465 PRO A 705
REMARK 465 PRO A 706
REMARK 465 SER A 707
REMARK 465 GLU A 708
REMARK 465 PRO A 709
REMARK 465 CYS A 710
REMARK 465 GLU A 711
REMARK 465 SER A 712
REMARK 465 SER A 713
REMARK 465 ALA A 714
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 ND2 ASN A 220 O5 NAG A 809 1.86
REMARK 500 ND2 ASN B 220 O5 NAG B 809 1.91
REMARK 500 O4 NAG B 809 O5 NAG B 810 1.93
REMARK 500 C3 NAG B 809 C1 NAG B 810 2.01
REMARK 500 OD1 ASN B 220 C1 NAG B 809 2.01
REMARK 500 O3 NAG B 809 O5 NAG B 810 2.11
REMARK 500 O7 NAG B 809 N2 NAG B 810 2.12
REMARK 500 O3 NAG B 809 C2 NAG B 810 2.17
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 B 206 -15.40 73.12
REMARK 500 ASN B 220 98.59 -67.31
REMARK 500 ASP B 238 50.03 -92.99
REMARK 500 CYS B 255 -6.08 -141.96
REMARK 500 ALA B 312 -157.12 58.48
REMARK 500 PHE B 316 16.61 -142.39
REMARK 500 ARG B 353 58.49 -117.11
REMARK 500 SER B 360 -117.49 60.26
REMARK 500 GLN B 380 -65.43 -103.32
REMARK 500 PRO B 418 5.41 -68.52
REMARK 500 TYR B 494 -70.68 -76.42
REMARK 500 LYS B 501 42.89 -75.85
REMARK 500 PHE B 560 -78.38 -134.31
REMARK 500 ALA B 647 77.75 60.88
REMARK 500 SER B 672 16.60 -154.78
REMARK 500 LYS B 688 -60.98 -108.17
REMARK 500 PHE A 206 -21.28 75.59
REMARK 500 CYS A 255 -1.35 -142.62
REMARK 500 ASN A 269 106.61 -162.70
REMARK 500 ALA A 312 -150.41 61.08
REMARK 500 PHE A 316 21.56 -144.19
REMARK 500 PRO A 351 -8.23 -58.69
REMARK 500 SER A 360 -116.03 57.90
REMARK 500 GLN A 380 -63.42 -94.93
REMARK 500 ALA A 458 -65.01 -91.79
REMARK 500 TYR A 535 49.67 -106.07
REMARK 500 GLU A 540 80.79 -155.48
REMARK 500 PHE A 560 -79.97 -133.83
REMARK 500 ALA A 647 83.62 52.20
REMARK 500 ASN A 670 56.11 -111.75
REMARK 500 LYS A 688 -60.75 -101.20
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 SO4 B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE B 812
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NH4 A 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 812
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 809 through NAG A 810 bound to ASN A 220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 809 through NAG B 810
DBREF 5X61 B 162 714 UNP Q869C3 ACES_ANOGA 162 714
DBREF 5X61 A 162 714 UNP Q869C3 ACES_ANOGA 162 714
SEQRES 1 B 553 ASP ASN ASP PRO LEU VAL VAL ASN THR ASP LYS GLY ARG
SEQRES 2 B 553 ILE ARG GLY ILE THR VAL ASP ALA PRO SER GLY LYS LYS
SEQRES 3 B 553 VAL ASP VAL TRP LEU GLY ILE PRO TYR ALA GLN PRO PRO
SEQRES 4 B 553 VAL GLY PRO LEU ARG PHE ARG HIS PRO ARG PRO ALA GLU
SEQRES 5 B 553 LYS TRP THR GLY VAL LEU ASN THR THR THR PRO PRO ASN
SEQRES 6 B 553 SER CYS VAL GLN ILE VAL ASP THR VAL PHE GLY ASP PHE
SEQRES 7 B 553 PRO GLY ALA THR MET TRP ASN PRO ASN THR PRO LEU SER
SEQRES 8 B 553 GLU ASP CYS LEU TYR ILE ASN VAL VAL ALA PRO ARG PRO
SEQRES 9 B 553 ARG PRO LYS ASN ALA ALA VAL MET LEU TRP ILE PHE GLY
SEQRES 10 B 553 GLY GLY PHE TYR SER GLY THR ALA THR LEU ASP VAL TYR
SEQRES 11 B 553 ASP HIS ARG ALA LEU ALA SER GLU GLU ASN VAL ILE VAL
SEQRES 12 B 553 VAL SER LEU GLN TYR ARG VAL ALA SER LEU GLY PHE LEU
SEQRES 13 B 553 PHE LEU GLY THR PRO GLU ALA PRO GLY ASN ALA GLY LEU
SEQRES 14 B 553 PHE ASP GLN ASN LEU ALA LEU ARG TRP VAL ARG ASP ASN
SEQRES 15 B 553 ILE HIS ARG PHE GLY GLY ASP PRO SER ARG VAL THR LEU
SEQRES 16 B 553 PHE GLY GLU SER ALA GLY ALA VAL SER VAL SER LEU HIS
SEQRES 17 B 553 LEU LEU SER ALA LEU SER ARG ASP LEU PHE GLN ARG ALA
SEQRES 18 B 553 ILE LEU GLN SER GLY SER PRO THR ALA PRO TRP ALA LEU
SEQRES 19 B 553 VAL SER ARG GLU GLU ALA THR LEU ARG ALA LEU ARG LEU
SEQRES 20 B 553 ALA GLU ALA VAL GLY CYS PRO HIS GLU PRO SER LYS LEU
SEQRES 21 B 553 SER ASP ALA VAL GLU CYS LEU ARG GLY LYS ASP PRO HIS
SEQRES 22 B 553 VAL LEU VAL ASN ASN GLU TRP GLY THR LEU GLY ILE CYS
SEQRES 23 B 553 GLU PHE PRO PHE VAL PRO VAL VAL ASP GLY ALA PHE LEU
SEQRES 24 B 553 ASP GLU THR PRO GLN ARG SER LEU ALA SER GLY ARG PHE
SEQRES 25 B 553 LYS LYS THR GLU ILE LEU THR GLY SER ASN THR GLU GLU
SEQRES 26 B 553 GLY TYR TYR PHE ILE ILE TYR TYR LEU THR GLU LEU LEU
SEQRES 27 B 553 ARG LYS GLU GLU GLY VAL THR VAL THR ARG GLU GLU PHE
SEQRES 28 B 553 LEU GLN ALA VAL ARG GLU LEU ASN PRO TYR VAL ASN GLY
SEQRES 29 B 553 ALA ALA ARG GLN ALA ILE VAL PHE GLU TYR THR ASP TRP
SEQRES 30 B 553 THR GLU PRO ASP ASN PRO ASN SER ASN ARG ASP ALA LEU
SEQRES 31 B 553 ASP LYS MET VAL GLY ASP TYR HIS PHE THR CYS ASN VAL
SEQRES 32 B 553 ASN GLU PHE ALA GLN ARG TYR ALA GLU GLU GLY ASN ASN
SEQRES 33 B 553 VAL TYR MET TYR LEU TYR THR HIS ARG SER LYS GLY ASN
SEQRES 34 B 553 PRO TRP PRO ARG TRP THR GLY VAL MET HIS GLY ASP GLU
SEQRES 35 B 553 ILE ASN TYR VAL PHE GLY GLU PRO LEU ASN PRO THR LEU
SEQRES 36 B 553 GLY TYR THR GLU ASP GLU LYS ASP PHE SER ARG LYS ILE
SEQRES 37 B 553 MET ARG TYR TRP SER ASN PHE ALA LYS THR GLY ASN PRO
SEQRES 38 B 553 ASN PRO ASN THR ALA SER SER GLU PHE PRO GLU TRP PRO
SEQRES 39 B 553 LYS HIS THR ALA HIS GLY ARG HIS TYR LEU GLU LEU GLY
SEQRES 40 B 553 LEU ASN THR SER PHE VAL GLY ARG GLY PRO ARG LEU ARG
SEQRES 41 B 553 GLN CYS ALA PHE TRP LYS LYS TYR LEU PRO GLN LEU VAL
SEQRES 42 B 553 ALA ALA THR SER ASN LEU PRO GLY PRO ALA PRO PRO SER
SEQRES 43 B 553 GLU PRO CYS GLU SER SER ALA
SEQRES 1 A 553 ASP ASN ASP PRO LEU VAL VAL ASN THR ASP LYS GLY ARG
SEQRES 2 A 553 ILE ARG GLY ILE THR VAL ASP ALA PRO SER GLY LYS LYS
SEQRES 3 A 553 VAL ASP VAL TRP LEU GLY ILE PRO TYR ALA GLN PRO PRO
SEQRES 4 A 553 VAL GLY PRO LEU ARG PHE ARG HIS PRO ARG PRO ALA GLU
SEQRES 5 A 553 LYS TRP THR GLY VAL LEU ASN THR THR THR PRO PRO ASN
SEQRES 6 A 553 SER CYS VAL GLN ILE VAL ASP THR VAL PHE GLY ASP PHE
SEQRES 7 A 553 PRO GLY ALA THR MET TRP ASN PRO ASN THR PRO LEU SER
SEQRES 8 A 553 GLU ASP CYS LEU TYR ILE ASN VAL VAL ALA PRO ARG PRO
SEQRES 9 A 553 ARG PRO LYS ASN ALA ALA VAL MET LEU TRP ILE PHE GLY
SEQRES 10 A 553 GLY GLY PHE TYR SER GLY THR ALA THR LEU ASP VAL TYR
SEQRES 11 A 553 ASP HIS ARG ALA LEU ALA SER GLU GLU ASN VAL ILE VAL
SEQRES 12 A 553 VAL SER LEU GLN TYR ARG VAL ALA SER LEU GLY PHE LEU
SEQRES 13 A 553 PHE LEU GLY THR PRO GLU ALA PRO GLY ASN ALA GLY LEU
SEQRES 14 A 553 PHE ASP GLN ASN LEU ALA LEU ARG TRP VAL ARG ASP ASN
SEQRES 15 A 553 ILE HIS ARG PHE GLY GLY ASP PRO SER ARG VAL THR LEU
SEQRES 16 A 553 PHE GLY GLU SER ALA GLY ALA VAL SER VAL SER LEU HIS
SEQRES 17 A 553 LEU LEU SER ALA LEU SER ARG ASP LEU PHE GLN ARG ALA
SEQRES 18 A 553 ILE LEU GLN SER GLY SER PRO THR ALA PRO TRP ALA LEU
SEQRES 19 A 553 VAL SER ARG GLU GLU ALA THR LEU ARG ALA LEU ARG LEU
SEQRES 20 A 553 ALA GLU ALA VAL GLY CYS PRO HIS GLU PRO SER LYS LEU
SEQRES 21 A 553 SER ASP ALA VAL GLU CYS LEU ARG GLY LYS ASP PRO HIS
SEQRES 22 A 553 VAL LEU VAL ASN ASN GLU TRP GLY THR LEU GLY ILE CYS
SEQRES 23 A 553 GLU PHE PRO PHE VAL PRO VAL VAL ASP GLY ALA PHE LEU
SEQRES 24 A 553 ASP GLU THR PRO GLN ARG SER LEU ALA SER GLY ARG PHE
SEQRES 25 A 553 LYS LYS THR GLU ILE LEU THR GLY SER ASN THR GLU GLU
SEQRES 26 A 553 GLY TYR TYR PHE ILE ILE TYR TYR LEU THR GLU LEU LEU
SEQRES 27 A 553 ARG LYS GLU GLU GLY VAL THR VAL THR ARG GLU GLU PHE
SEQRES 28 A 553 LEU GLN ALA VAL ARG GLU LEU ASN PRO TYR VAL ASN GLY
SEQRES 29 A 553 ALA ALA ARG GLN ALA ILE VAL PHE GLU TYR THR ASP TRP
SEQRES 30 A 553 THR GLU PRO ASP ASN PRO ASN SER ASN ARG ASP ALA LEU
SEQRES 31 A 553 ASP LYS MET VAL GLY ASP TYR HIS PHE THR CYS ASN VAL
SEQRES 32 A 553 ASN GLU PHE ALA GLN ARG TYR ALA GLU GLU GLY ASN ASN
SEQRES 33 A 553 VAL TYR MET TYR LEU TYR THR HIS ARG SER LYS GLY ASN
SEQRES 34 A 553 PRO TRP PRO ARG TRP THR GLY VAL MET HIS GLY ASP GLU
SEQRES 35 A 553 ILE ASN TYR VAL PHE GLY GLU PRO LEU ASN PRO THR LEU
SEQRES 36 A 553 GLY TYR THR GLU ASP GLU LYS ASP PHE SER ARG LYS ILE
SEQRES 37 A 553 MET ARG TYR TRP SER ASN PHE ALA LYS THR GLY ASN PRO
SEQRES 38 A 553 ASN PRO ASN THR ALA SER SER GLU PHE PRO GLU TRP PRO
SEQRES 39 A 553 LYS HIS THR ALA HIS GLY ARG HIS TYR LEU GLU LEU GLY
SEQRES 40 A 553 LEU ASN THR SER PHE VAL GLY ARG GLY PRO ARG LEU ARG
SEQRES 41 A 553 GLN CYS ALA PHE TRP LYS LYS TYR LEU PRO GLN LEU VAL
SEQRES 42 A 553 ALA ALA THR SER ASN LEU PRO GLY PRO ALA PRO PRO SER
SEQRES 43 A 553 GLU PRO CYS GLU SER SER ALA
MODRES 5X61 ASN A 220 ASN GLYCOSYLATION SITE
MODRES 5X61 ASN B 220 ASN GLYCOSYLATION SITE
HET SO4 B 801 5
HET SO4 B 802 5
HET SO4 B 803 5
HET SO4 B 804 5
HET SO4 B 805 5
HET SO4 B 806 5
HET SO4 B 807 5
HET SO4 B 808 5
HET NAG B 809 14
HET NAG B 810 14
HET NH4 B 811 1
HET EPE B 812 15
HET SO4 A 801 5
HET SO4 A 802 5
HET SO4 A 803 5
HET SO4 A 804 5
HET SO4 A 805 5
HET SO4 A 806 5
HET SO4 A 807 5
HET SO4 A 808 5
HET NAG A 809 14
HET NAG A 810 14
HET NH4 A 811 1
HET EPE A 812 15
HETNAM SO4 SULFATE ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM NH4 AMMONIUM ION
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN EPE HEPES
FORMUL 3 SO4 16(O4 S 2-)
FORMUL 11 NAG 4(C8 H15 N O6)
FORMUL 12 NH4 2(H4 N 1+)
FORMUL 13 EPE 2(C8 H18 N2 O4 S)
FORMUL 25 HOH *6(H2 O)
HELIX 1 AA1 VAL B 201 ARG B 205 5 5
HELIX 2 AA2 PHE B 239 MET B 244 1 6
HELIX 3 AA3 LEU B 288 ASP B 292 5 5
HELIX 4 AA4 HIS B 293 ASN B 301 1 9
HELIX 5 AA5 ALA B 312 LEU B 317 1 6
HELIX 6 AA6 ASN B 327 ILE B 344 1 18
HELIX 7 AA7 HIS B 345 PHE B 347 5 3
HELIX 8 AA8 SER B 360 SER B 372 1 13
HELIX 9 AA9 SER B 397 GLY B 413 1 17
HELIX 10 AB1 LYS B 420 ARG B 429 1 10
HELIX 11 AB2 ASP B 432 ASN B 438 1 7
HELIX 12 AB3 THR B 463 SER B 470 1 8
HELIX 13 AB4 GLY B 487 LEU B 495 1 9
HELIX 14 AB5 THR B 508 ASN B 520 1 13
HELIX 15 AB6 GLY B 525 TYR B 535 1 11
HELIX 16 AB7 ASN B 543 PHE B 560 1 18
HELIX 17 AB8 PHE B 560 GLU B 574 1 15
HELIX 18 AB9 PRO B 593 GLY B 597 5 5
HELIX 19 AC1 GLU B 603 PHE B 608 1 6
HELIX 20 AC2 ASN B 613 GLY B 617 5 5
HELIX 21 AC3 THR B 619 GLY B 640 1 22
HELIX 22 AC4 ARG B 679 LYS B 688 1 10
HELIX 23 AC5 LYS B 688 SER B 698 1 11
HELIX 24 AC6 VAL A 201 ARG A 205 5 5
HELIX 25 AC7 PHE A 239 MET A 244 1 6
HELIX 26 AC8 ASP A 292 ASN A 301 1 10
HELIX 27 AC9 ALA A 312 LEU A 317 1 6
HELIX 28 AD1 ASN A 327 ILE A 344 1 18
HELIX 29 AD2 HIS A 345 PHE A 347 5 3
HELIX 30 AD3 SER A 360 SER A 372 1 13
HELIX 31 AD4 SER A 375 PHE A 379 5 5
HELIX 32 AD5 SER A 397 VAL A 412 1 16
HELIX 33 AD6 LYS A 420 LYS A 431 1 12
HELIX 34 AD7 ASP A 432 ASN A 439 1 8
HELIX 35 AD8 THR A 463 SER A 470 1 8
HELIX 36 AD9 GLY A 487 TYR A 494 1 8
HELIX 37 AE1 THR A 508 ASN A 520 1 13
HELIX 38 AE2 GLY A 525 TYR A 535 1 11
HELIX 39 AE3 ASN A 543 PHE A 560 1 18
HELIX 40 AE4 PHE A 560 GLU A 573 1 14
HELIX 41 AE5 PRO A 593 GLY A 597 5 5
HELIX 42 AE6 GLU A 603 PHE A 608 1 6
HELIX 43 AE7 THR A 619 GLY A 640 1 22
HELIX 44 AE8 ARG A 679 LYS A 688 1 10
HELIX 45 AE9 LYS A 688 THR A 697 1 10
SHEET 1 AA1 3 VAL B 167 VAL B 168 0
SHEET 2 AA1 3 ARG B 174 ARG B 176 -1 O ILE B 175 N VAL B 168
SHEET 3 AA1 3 VAL B 218 ASN B 220 1 O LEU B 219 N ARG B 176
SHEET 1 AA211 ILE B 178 ASP B 181 0
SHEET 2 AA211 LYS B 187 PRO B 195 -1 O VAL B 188 N VAL B 180
SHEET 3 AA211 TYR B 257 PRO B 263 -1 O ALA B 262 N ASP B 189
SHEET 4 AA211 ILE B 303 LEU B 307 -1 O SER B 306 N ASN B 259
SHEET 5 AA211 ALA B 270 ILE B 276 1 N TRP B 275 O VAL B 305
SHEET 6 AA211 GLY B 349 GLU B 359 1 O THR B 355 N VAL B 272
SHEET 7 AA211 ARG B 381 GLN B 385 1 O ILE B 383 N LEU B 356
SHEET 8 AA211 ILE B 478 ASN B 483 1 O LEU B 479 N LEU B 384
SHEET 9 AA211 VAL B 578 TYR B 583 1 O TYR B 583 N SER B 482
SHEET 10 AA211 HIS B 663 LEU B 667 1 O LEU B 667 N LEU B 582
SHEET 11 AA211 VAL B 674 ARG B 676 -1 O GLY B 675 N TYR B 664
SHEET 1 AA3 2 ALA B 197 GLN B 198 0
SHEET 2 AA3 2 ARG B 210 PRO B 211 -1 O ARG B 210 N GLN B 198
SHEET 1 AA4 2 SER B 227 CYS B 228 0
SHEET 2 AA4 2 LEU B 251 SER B 252 1 O SER B 252 N SER B 227
SHEET 1 AA5 3 VAL A 167 THR A 170 0
SHEET 2 AA5 3 GLY A 173 ARG A 176 -1 O ILE A 175 N VAL A 168
SHEET 3 AA5 3 VAL A 218 ASN A 220 1 O LEU A 219 N ARG A 176
SHEET 1 AA611 ILE A 178 ASP A 181 0
SHEET 2 AA611 LYS A 187 PRO A 195 -1 O VAL A 188 N VAL A 180
SHEET 3 AA611 TYR A 257 PRO A 263 -1 O ALA A 262 N ASP A 189
SHEET 4 AA611 ILE A 303 LEU A 307 -1 O SER A 306 N ASN A 259
SHEET 5 AA611 ALA A 270 ILE A 276 1 N TRP A 275 O VAL A 305
SHEET 6 AA611 GLY A 349 GLU A 359 1 O THR A 355 N VAL A 272
SHEET 7 AA611 ARG A 381 GLN A 385 1 O ILE A 383 N LEU A 356
SHEET 8 AA611 ILE A 478 ASN A 483 1 O LEU A 479 N LEU A 384
SHEET 9 AA611 VAL A 578 TYR A 583 1 O TYR A 583 N SER A 482
SHEET 10 AA611 HIS A 663 LEU A 667 1 O LEU A 667 N LEU A 582
SHEET 11 AA611 VAL A 674 ARG A 676 -1 O GLY A 675 N TYR A 664
SSBOND 1 CYS B 228 CYS B 255 1555 1555 2.04
SSBOND 2 CYS B 414 CYS B 427 1555 1555 2.04
SSBOND 3 CYS B 562 CYS B 683 1555 1555 2.05
SSBOND 4 CYS A 228 CYS A 255 1555 1555 2.04
SSBOND 5 CYS A 414 CYS A 427 1555 1555 2.04
SSBOND 6 CYS A 562 CYS A 683 1555 1555 2.04
LINK ND2 ASN A 220 C1 NAG A 809 1555 1555 1.57
LINK O3 NAG B 809 C1 NAG B 810 1555 1555 1.18
LINK O3 NAG A 809 C1 NAG A 810 1555 1555 1.39
LINK ND2 ASN B 220 C1 NAG B 809 1555 1555 1.97
CISPEP 1 ARG B 264 PRO B 265 0 2.08
CISPEP 2 GLY B 677 PRO B 678 0 2.54
CISPEP 3 ARG A 264 PRO A 265 0 3.02
CISPEP 4 GLY A 677 PRO A 678 0 -0.60
SITE 1 AC1 3 ARG B 376 LYS B 474 LYS B 475
SITE 1 AC2 2 ARG B 353 LYS B 638
SITE 1 AC3 3 PRO A 203 SER B 470 ARG B 472
SITE 1 AC4 4 SER B 397 ARG B 398 GLU B 399 HOH B 904
SITE 1 AC5 2 LYS B 187 ARG B 264
SITE 1 AC6 2 LEU B 582 ARG B 679
SITE 1 AC7 3 ARG B 174 THR B 216 GLY B 217
SITE 1 AC8 4 TRP B 441 GLY B 442 LEU B 444 EPE B 812
SITE 1 AC9 3 TYR B 282 TRP B 441 SO4 B 808
SITE 1 AD1 3 SER A 470 ARG A 472 PRO B 203
SITE 1 AD2 2 ARG A 353 LYS A 638
SITE 1 AD3 2 GLY A 504 ARG A 594
SITE 1 AD4 2 ASN A 524 ARG A 528
SITE 1 AD5 3 SER A 397 ARG A 398 GLU A 399
SITE 1 AD6 5 THR A 536 ASP A 537 TRP A 538 THR A 539
SITE 2 AD6 5 ARG B 681
SITE 1 AD7 2 GLY A 525 ARG A 528
SITE 1 AD8 4 THR A 658 HIS A 660 GLY A 661 HIS A 663
SITE 1 AD9 1 TRP A 245
SITE 1 AE1 2 TYR A 282 TRP A 441
SITE 1 AE2 2 ARG A 176 ASN A 220
SITE 1 AE3 2 ARG B 176 ASN B 220
CRYST1 148.723 148.723 225.796 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 0.006724 0.003882 0.000000 0.00000
SCALE2 0.000000 0.007764 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004429 0.00000
TER 4250 SER B 698
TER 8500 SER A 698
MASTER 437 0 24 45 32 0 22 6 8672 2 180 86
END |