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HEADER HYDROLASE 13-SEP-17 5YDI
TITLE CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE CATALYTIC SUBUNITS OF THE
TITLE 2 MALARIA VECTOR ANOPHELES GAMBIAE, NEW CRYSTAL PACKING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B, C;
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_COMMON: PICHIA PASTORIS;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPICZ*A
KEYWDS ALPHA/BATA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.HAN,H.GUAN,H.DING,C.LIAO,H.ROBINSON,J.LI
REVDAT 1 07-MAR-18 5YDI 0
JRNL AUTH Q.HAN,H.GUAN,H.DING,C.LIAO,H.ROBINSON,J.LI
JRNL TITL CRYSTAL STRUCTURES OF ACETYLCHOLINESTERASE OF THE MALARIA
JRNL TITL 2 VECTOR ANOPHELES GAMBIAE REVEAL A POLYMERIZATION INTERFACE,
JRNL TITL 3 LIGAND BINDING RESIDUES AND POST TRANSLATIONAL MODIFICATIONS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.45 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) : 3.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 31768
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1697
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) : 3.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2324
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.2790
REMARK 3 BIN FREE R VALUE SET COUNT : 105
REMARK 3 BIN FREE R VALUE : 0.2950
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12747
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 220
REMARK 3 SOLVENT ATOMS : 10
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.543
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.404
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.984
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.906
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.854
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13367 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18258 ; 1.042 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1608 ; 5.040 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 636 ;34.171 ;23.302
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1986 ;15.305 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 105 ;13.756 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1983 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10428 ; 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 5YDI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1300005088.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAY-13
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31768
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.450
REMARK 200 RESOLUTION RANGE LOW (A) : 63.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 76.0
REMARK 200 DATA REDUNDANCY : 13.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.64
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: 5YDH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES BUFFER, 20% PEG 4000, 22%
REMARK 280 GLYCEROL, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.63500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.63500
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 63.72000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 117.95500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 63.72000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 117.95500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 83.63500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 63.72000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 117.95500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 83.63500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 63.72000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 117.95500
REMARK 290 SMTRY3 8 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: 4260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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: 5110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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 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 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 C 699
REMARK 465 LEU C 700
REMARK 465 PRO C 701
REMARK 465 GLY C 702
REMARK 465 PRO C 703
REMARK 465 ALA C 704
REMARK 465 PRO C 705
REMARK 465 PRO C 706
REMARK 465 SER C 707
REMARK 465 GLU C 708
REMARK 465 PRO C 709
REMARK 465 CYS C 710
REMARK 465 GLU C 711
REMARK 465 SER C 712
REMARK 465 SER C 713
REMARK 465 ALA C 714
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 206 -11.82 70.94
REMARK 500 VAL A 235 -14.72 -49.32
REMARK 500 ALA A 312 -151.22 61.95
REMARK 500 SER A 360 -119.71 55.16
REMARK 500 GLN A 380 -67.88 -105.16
REMARK 500 ALA A 458 -60.74 -104.34
REMARK 500 GLU A 497 -71.21 -56.12
REMARK 500 GLU A 540 78.95 -152.97
REMARK 500 PHE A 560 -74.38 -132.19
REMARK 500 PHE A 651 72.86 38.73
REMARK 500 LYS A 688 -62.73 -109.42
REMARK 500 PHE B 206 -8.51 68.18
REMARK 500 PHE B 281 16.03 59.66
REMARK 500 ALA B 312 -151.28 61.30
REMARK 500 SER B 360 -114.85 58.51
REMARK 500 GLN B 380 -61.79 -100.31
REMARK 500 GLU B 485 79.06 -116.80
REMARK 500 PHE B 560 -77.79 -130.36
REMARK 500 SER B 649 -137.13 43.51
REMARK 500 PHE B 651 70.60 38.46
REMARK 500 LYS B 688 -61.68 -105.34
REMARK 500 PHE C 206 -4.72 71.91
REMARK 500 PHE C 281 18.35 58.26
REMARK 500 ALA C 312 -151.51 62.71
REMARK 500 SER C 360 -116.49 55.54
REMARK 500 GLN C 380 -70.30 -98.58
REMARK 500 GLU C 540 79.34 -154.06
REMARK 500 PHE C 560 -73.99 -130.93
REMARK 500 SER C 649 -9.18 60.73
REMARK 500 LYS C 688 -66.35 -100.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 805 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 360 OG
REMARK 620 2 GOL A 804 O1 120.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 811 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 360 OG
REMARK 620 2 HOH B 901 O 70.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 806 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER C 360 OG
REMARK 620 2 HOH C 901 O 64.7
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 812
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 801 bound
REMARK 800 to ASN A 220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 802 bound
REMARK 800 to ASN A 670
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 801 through BMA B 803 bound to ASN B 220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 804 through MAN B 809 bound to ASN B 670
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 804 bound
REMARK 800 to ASN C 220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C
REMARK 800 801 through BMA C 803 bound to ASN C 670
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5X61 RELATED DB: PDB
DBREF 5YDI A 162 714 UNP Q869C3 ACES_ANOGA 162 714
DBREF 5YDI B 162 714 UNP Q869C3 ACES_ANOGA 162 714
DBREF 5YDI C 162 714 UNP Q869C3 ACES_ANOGA 162 714
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
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 C 553 ASP ASN ASP PRO LEU VAL VAL ASN THR ASP LYS GLY ARG
SEQRES 2 C 553 ILE ARG GLY ILE THR VAL ASP ALA PRO SER GLY LYS LYS
SEQRES 3 C 553 VAL ASP VAL TRP LEU GLY ILE PRO TYR ALA GLN PRO PRO
SEQRES 4 C 553 VAL GLY PRO LEU ARG PHE ARG HIS PRO ARG PRO ALA GLU
SEQRES 5 C 553 LYS TRP THR GLY VAL LEU ASN THR THR THR PRO PRO ASN
SEQRES 6 C 553 SER CYS VAL GLN ILE VAL ASP THR VAL PHE GLY ASP PHE
SEQRES 7 C 553 PRO GLY ALA THR MET TRP ASN PRO ASN THR PRO LEU SER
SEQRES 8 C 553 GLU ASP CYS LEU TYR ILE ASN VAL VAL ALA PRO ARG PRO
SEQRES 9 C 553 ARG PRO LYS ASN ALA ALA VAL MET LEU TRP ILE PHE GLY
SEQRES 10 C 553 GLY GLY PHE TYR SER GLY THR ALA THR LEU ASP VAL TYR
SEQRES 11 C 553 ASP HIS ARG ALA LEU ALA SER GLU GLU ASN VAL ILE VAL
SEQRES 12 C 553 VAL SER LEU GLN TYR ARG VAL ALA SER LEU GLY PHE LEU
SEQRES 13 C 553 PHE LEU GLY THR PRO GLU ALA PRO GLY ASN ALA GLY LEU
SEQRES 14 C 553 PHE ASP GLN ASN LEU ALA LEU ARG TRP VAL ARG ASP ASN
SEQRES 15 C 553 ILE HIS ARG PHE GLY GLY ASP PRO SER ARG VAL THR LEU
SEQRES 16 C 553 PHE GLY GLU SER ALA GLY ALA VAL SER VAL SER LEU HIS
SEQRES 17 C 553 LEU LEU SER ALA LEU SER ARG ASP LEU PHE GLN ARG ALA
SEQRES 18 C 553 ILE LEU GLN SER GLY SER PRO THR ALA PRO TRP ALA LEU
SEQRES 19 C 553 VAL SER ARG GLU GLU ALA THR LEU ARG ALA LEU ARG LEU
SEQRES 20 C 553 ALA GLU ALA VAL GLY CYS PRO HIS GLU PRO SER LYS LEU
SEQRES 21 C 553 SER ASP ALA VAL GLU CYS LEU ARG GLY LYS ASP PRO HIS
SEQRES 22 C 553 VAL LEU VAL ASN ASN GLU TRP GLY THR LEU GLY ILE CYS
SEQRES 23 C 553 GLU PHE PRO PHE VAL PRO VAL VAL ASP GLY ALA PHE LEU
SEQRES 24 C 553 ASP GLU THR PRO GLN ARG SER LEU ALA SER GLY ARG PHE
SEQRES 25 C 553 LYS LYS THR GLU ILE LEU THR GLY SER ASN THR GLU GLU
SEQRES 26 C 553 GLY TYR TYR PHE ILE ILE TYR TYR LEU THR GLU LEU LEU
SEQRES 27 C 553 ARG LYS GLU GLU GLY VAL THR VAL THR ARG GLU GLU PHE
SEQRES 28 C 553 LEU GLN ALA VAL ARG GLU LEU ASN PRO TYR VAL ASN GLY
SEQRES 29 C 553 ALA ALA ARG GLN ALA ILE VAL PHE GLU TYR THR ASP TRP
SEQRES 30 C 553 THR GLU PRO ASP ASN PRO ASN SER ASN ARG ASP ALA LEU
SEQRES 31 C 553 ASP LYS MET VAL GLY ASP TYR HIS PHE THR CYS ASN VAL
SEQRES 32 C 553 ASN GLU PHE ALA GLN ARG TYR ALA GLU GLU GLY ASN ASN
SEQRES 33 C 553 VAL TYR MET TYR LEU TYR THR HIS ARG SER LYS GLY ASN
SEQRES 34 C 553 PRO TRP PRO ARG TRP THR GLY VAL MET HIS GLY ASP GLU
SEQRES 35 C 553 ILE ASN TYR VAL PHE GLY GLU PRO LEU ASN PRO THR LEU
SEQRES 36 C 553 GLY TYR THR GLU ASP GLU LYS ASP PHE SER ARG LYS ILE
SEQRES 37 C 553 MET ARG TYR TRP SER ASN PHE ALA LYS THR GLY ASN PRO
SEQRES 38 C 553 ASN PRO ASN THR ALA SER SER GLU PHE PRO GLU TRP PRO
SEQRES 39 C 553 LYS HIS THR ALA HIS GLY ARG HIS TYR LEU GLU LEU GLY
SEQRES 40 C 553 LEU ASN THR SER PHE VAL GLY ARG GLY PRO ARG LEU ARG
SEQRES 41 C 553 GLN CYS ALA PHE TRP LYS LYS TYR LEU PRO GLN LEU VAL
SEQRES 42 C 553 ALA ALA THR SER ASN LEU PRO GLY PRO ALA PRO PRO SER
SEQRES 43 C 553 GLU PRO CYS GLU SER SER ALA
MODRES 5YDI ASN B 220 ASN GLYCOSYLATION SITE
MODRES 5YDI ASN A 220 ASN GLYCOSYLATION SITE
MODRES 5YDI ASN B 670 ASN GLYCOSYLATION SITE
MODRES 5YDI ASN C 670 ASN GLYCOSYLATION SITE
MODRES 5YDI ASN A 670 ASN GLYCOSYLATION SITE
MODRES 5YDI ASN C 220 ASN GLYCOSYLATION SITE
HET NAG A 801 14
HET NAG A 802 14
HET GOL A 803 6
HET GOL A 804 6
HET NA A 805 1
HET NAG B 801 14
HET NAG B 802 14
HET BMA B 803 11
HET NAG B 804 14
HET NAG B 805 14
HET BMA B 806 11
HET MAN B 807 11
HET MAN B 808 11
HET MAN B 809 11
HET GOL B 810 6
HET NA B 811 1
HET NA B 812 1
HET NAG C 801 14
HET NAG C 802 14
HET BMA C 803 11
HET NAG C 804 14
HET GOL C 805 6
HET NA C 806 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM GOL GLYCEROL
HETNAM NA SODIUM ION
HETNAM BMA BETA-D-MANNOSE
HETNAM MAN ALPHA-D-MANNOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 NAG 9(C8 H15 N O6)
FORMUL 6 GOL 4(C3 H8 O3)
FORMUL 8 NA 4(NA 1+)
FORMUL 9 BMA 3(C6 H12 O6)
FORMUL 10 MAN 3(C6 H12 O6)
FORMUL 18 HOH *10(H2 O)
HELIX 1 AA1 VAL A 201 ARG A 205 5 5
HELIX 2 AA2 PHE A 239 MET A 244 1 6
HELIX 3 AA3 ASP A 292 ASN A 301 1 10
HELIX 4 AA4 VAL A 311 LEU A 317 1 7
HELIX 5 AA5 ASN A 327 ILE A 344 1 18
HELIX 6 AA6 HIS A 345 PHE A 347 5 3
HELIX 7 AA7 SER A 360 SER A 372 1 13
HELIX 8 AA8 SER A 375 PHE A 379 5 5
HELIX 9 AA9 SER A 397 GLY A 413 1 17
HELIX 10 AB1 LYS A 420 LYS A 431 1 12
HELIX 11 AB2 ASP A 432 ASN A 439 1 8
HELIX 12 AB3 THR A 463 GLY A 471 1 9
HELIX 13 AB4 GLY A 487 TYR A 494 1 8
HELIX 14 AB5 THR A 508 ASN A 520 1 13
HELIX 15 AB6 ALA A 527 TYR A 535 1 9
HELIX 16 AB7 ASN A 543 PHE A 560 1 18
HELIX 17 AB8 PHE A 560 GLU A 573 1 14
HELIX 18 AB9 PRO A 593 GLY A 597 5 5
HELIX 19 AC1 GLU A 603 PHE A 608 1 6
HELIX 20 AC2 GLY A 609 ASN A 613 5 5
HELIX 21 AC3 THR A 619 GLY A 640 1 22
HELIX 22 AC4 ARG A 679 LYS A 688 1 10
HELIX 23 AC5 LYS A 688 THR A 697 1 10
HELIX 24 AC6 VAL B 201 ARG B 205 5 5
HELIX 25 AC7 ASP B 292 ASN B 301 1 10
HELIX 26 AC8 VAL B 311 LEU B 317 1 7
HELIX 27 AC9 ASN B 327 ILE B 344 1 18
HELIX 28 AD1 HIS B 345 PHE B 347 5 3
HELIX 29 AD2 SER B 360 SER B 372 1 13
HELIX 30 AD3 SER B 397 GLY B 413 1 17
HELIX 31 AD4 LEU B 421 LYS B 431 1 11
HELIX 32 AD5 ASP B 432 ASN B 439 1 8
HELIX 33 AD6 THR B 463 GLY B 471 1 9
HELIX 34 AD7 GLY B 487 TYR B 494 1 8
HELIX 35 AD8 THR B 508 ASN B 520 1 13
HELIX 36 AD9 GLY B 525 TYR B 535 1 11
HELIX 37 AE1 ASN B 543 PHE B 560 1 18
HELIX 38 AE2 PHE B 560 GLU B 574 1 15
HELIX 39 AE3 PRO B 593 GLY B 597 5 5
HELIX 40 AE4 GLU B 603 PHE B 608 1 6
HELIX 41 AE5 GLY B 609 ASN B 613 5 5
HELIX 42 AE6 THR B 619 GLY B 640 1 22
HELIX 43 AE7 ARG B 679 LYS B 688 1 10
HELIX 44 AE8 LYS B 688 SER B 698 1 11
HELIX 45 AE9 VAL C 201 ARG C 205 5 5
HELIX 46 AF1 PHE C 239 MET C 244 1 6
HELIX 47 AF2 ASP C 292 ASN C 301 1 10
HELIX 48 AF3 VAL C 311 LEU C 317 1 7
HELIX 49 AF4 ASN C 327 ILE C 344 1 18
HELIX 50 AF5 HIS C 345 PHE C 347 5 3
HELIX 51 AF6 SER C 360 SER C 372 1 13
HELIX 52 AF7 SER C 375 PHE C 379 5 5
HELIX 53 AF8 SER C 397 GLY C 413 1 17
HELIX 54 AF9 LYS C 420 LYS C 431 1 12
HELIX 55 AG1 ASP C 432 ASN C 438 1 7
HELIX 56 AG2 THR C 463 GLY C 471 1 9
HELIX 57 AG3 GLY C 487 TYR C 494 1 8
HELIX 58 AG4 THR C 508 ASN C 520 1 13
HELIX 59 AG5 GLY C 525 TYR C 535 1 11
HELIX 60 AG6 ASN C 543 PHE C 560 1 18
HELIX 61 AG7 PHE C 560 GLU C 573 1 14
HELIX 62 AG8 PRO C 593 GLY C 597 5 5
HELIX 63 AG9 GLU C 603 PHE C 608 1 6
HELIX 64 AH1 GLY C 609 ASN C 613 5 5
HELIX 65 AH2 THR C 619 GLY C 640 1 22
HELIX 66 AH3 PRO C 644 SER C 648 5 5
HELIX 67 AH4 ARG C 679 LYS C 688 1 10
HELIX 68 AH5 LYS C 688 THR C 697 1 10
SHEET 1 AA1 3 VAL A 167 THR A 170 0
SHEET 2 AA1 3 GLY A 173 ARG A 176 -1 O ILE A 175 N VAL A 168
SHEET 3 AA1 3 VAL A 218 ASN A 220 1 O LEU A 219 N ARG A 176
SHEET 1 AA211 ILE A 178 ASP A 181 0
SHEET 2 AA211 LYS A 187 PRO A 195 -1 O VAL A 190 N ILE A 178
SHEET 3 AA211 TYR A 257 PRO A 263 -1 O ALA A 262 N ASP A 189
SHEET 4 AA211 ILE A 303 LEU A 307 -1 O SER A 306 N ASN A 259
SHEET 5 AA211 ALA A 270 ILE A 276 1 N TRP A 275 O VAL A 305
SHEET 6 AA211 GLY A 349 GLU A 359 1 O THR A 355 N VAL A 272
SHEET 7 AA211 ARG A 381 GLN A 385 1 O ILE A 383 N LEU A 356
SHEET 8 AA211 ILE A 478 ASN A 483 1 O LEU A 479 N LEU A 384
SHEET 9 AA211 VAL A 578 TYR A 583 1 O TYR A 579 N ILE A 478
SHEET 10 AA211 HIS A 663 LEU A 667 1 O LEU A 665 N LEU A 582
SHEET 11 AA211 VAL A 674 ARG A 676 -1 O GLY A 675 N TYR A 664
SHEET 1 AA3 2 SER A 227 CYS A 228 0
SHEET 2 AA3 2 LEU A 251 SER A 252 1 O SER A 252 N SER A 227
SHEET 1 AA4 3 VAL B 167 THR B 170 0
SHEET 2 AA4 3 GLY B 173 ARG B 176 -1 O GLY B 173 N THR B 170
SHEET 3 AA4 3 VAL B 218 ASN B 220 1 O LEU B 219 N ARG B 176
SHEET 1 AA511 ILE B 178 ASP B 181 0
SHEET 2 AA511 LYS B 187 PRO B 195 -1 O VAL B 188 N VAL B 180
SHEET 3 AA511 TYR B 257 PRO B 263 -1 O ILE B 258 N ILE B 194
SHEET 4 AA511 ILE B 303 LEU B 307 -1 O SER B 306 N ASN B 259
SHEET 5 AA511 ALA B 270 ILE B 276 1 N TRP B 275 O VAL B 305
SHEET 6 AA511 GLY B 349 GLU B 359 1 O THR B 355 N VAL B 272
SHEET 7 AA511 ARG B 381 GLN B 385 1 O ILE B 383 N LEU B 356
SHEET 8 AA511 ILE B 478 ASN B 483 1 O LEU B 479 N LEU B 384
SHEET 9 AA511 VAL B 578 TYR B 583 1 O TYR B 579 N ILE B 478
SHEET 10 AA511 HIS B 663 LEU B 667 1 O LEU B 667 N LEU B 582
SHEET 11 AA511 VAL B 674 ARG B 676 -1 O GLY B 675 N TYR B 664
SHEET 1 AA6 3 VAL C 167 THR C 170 0
SHEET 2 AA6 3 GLY C 173 ARG C 176 -1 O ILE C 175 N VAL C 168
SHEET 3 AA6 3 VAL C 218 ASN C 220 1 O LEU C 219 N ARG C 174
SHEET 1 AA711 ILE C 178 ASP C 181 0
SHEET 2 AA711 LYS C 187 PRO C 195 -1 O VAL C 188 N VAL C 180
SHEET 3 AA711 TYR C 257 PRO C 263 -1 O ALA C 262 N ASP C 189
SHEET 4 AA711 ILE C 303 LEU C 307 -1 O VAL C 304 N VAL C 261
SHEET 5 AA711 ALA C 270 ILE C 276 1 N TRP C 275 O VAL C 305
SHEET 6 AA711 GLY C 349 GLU C 359 1 O THR C 355 N VAL C 272
SHEET 7 AA711 ARG C 381 GLN C 385 1 O ILE C 383 N LEU C 356
SHEET 8 AA711 ILE C 478 ASN C 483 1 O LEU C 479 N LEU C 384
SHEET 9 AA711 VAL C 578 TYR C 583 1 O TYR C 579 N THR C 480
SHEET 10 AA711 HIS C 663 LEU C 667 1 O LEU C 665 N MET C 580
SHEET 11 AA711 VAL C 674 ARG C 676 -1 O GLY C 675 N TYR C 664
SSBOND 1 CYS A 228 CYS A 255 1555 1555 2.04
SSBOND 2 CYS A 414 CYS A 427 1555 1555 2.04
SSBOND 3 CYS A 562 CYS A 683 1555 1555 2.04
SSBOND 4 CYS B 228 CYS B 255 1555 1555 2.03
SSBOND 5 CYS B 414 CYS B 427 1555 1555 2.04
SSBOND 6 CYS B 562 CYS B 683 1555 1555 2.04
SSBOND 7 CYS C 228 CYS C 255 1555 1555 2.03
SSBOND 8 CYS C 414 CYS C 427 1555 1555 2.04
SSBOND 9 CYS C 562 CYS C 683 1555 1555 2.05
LINK ND2 ASN A 220 C1 NAG A 801 1555 1555 1.43
LINK OG SER A 360 NA NA A 805 1555 1555 2.08
LINK ND2 ASN A 670 C1 NAG A 802 1555 1555 1.45
LINK ND2 ASN B 220 C1 NAG B 801 1555 1555 1.44
LINK OG SER B 360 NA NA B 811 1555 1555 2.16
LINK ND2 ASN B 670 C1 NAG B 804 1555 1555 1.44
LINK ND2 ASN C 220 C1 NAG C 804 1555 1555 1.44
LINK OG SER C 360 NA NA C 806 1555 1555 2.19
LINK ND2 ASN C 670 C1 NAG C 801 1555 1555 1.45
LINK O1 GOL A 804 NA NA A 805 1555 1555 2.73
LINK O4 NAG B 801 C1 NAG B 802 1555 1555 1.45
LINK O4 NAG B 802 C1 BMA B 803 1555 1555 1.46
LINK O4 NAG B 804 C1 NAG B 805 1555 1555 1.46
LINK O4 NAG B 805 C1 BMA B 806 1555 1555 1.47
LINK O3 BMA B 806 C1 MAN B 808 1555 1555 1.46
LINK O6 BMA B 806 C1 MAN B 807 1555 1555 1.46
LINK O6 MAN B 808 C1 MAN B 809 1555 1555 1.44
LINK O3 GOL B 810 NA NA B 812 1555 1555 2.29
LINK NA NA B 811 O HOH B 901 1555 1555 2.15
LINK O4 NAG C 801 C1 NAG C 802 1555 1555 1.44
LINK O4 NAG C 802 C1 BMA C 803 1555 1555 1.44
LINK NA NA C 806 O HOH C 901 1555 1555 2.20
CISPEP 1 ARG A 264 PRO A 265 0 2.98
CISPEP 2 GLY A 677 PRO A 678 0 0.12
CISPEP 3 ARG B 264 PRO B 265 0 0.67
CISPEP 4 GLY B 677 PRO B 678 0 1.15
CISPEP 5 ARG C 264 PRO C 265 0 -0.06
CISPEP 6 GLY C 677 PRO C 678 0 -2.82
SITE 1 AC1 1 TYR A 282
SITE 1 AC2 2 TYR A 489 NA A 805
SITE 1 AC3 2 SER A 360 GOL A 804
SITE 1 AC4 2 TYR B 282 NA B 812
SITE 1 AC5 3 SER B 360 PHE B 490 HOH B 901
SITE 1 AC6 1 GOL B 810
SITE 1 AC7 2 TYR C 282 TYR C 489
SITE 1 AC8 3 SER C 360 PHE C 490 HOH C 901
SITE 1 AC9 2 ASN A 220 THR A 222
SITE 1 AD1 1 ASN A 670
SITE 1 AD2 2 ARG B 176 ASN B 220
SITE 1 AD3 3 ASN B 670 NAG C 802 BMA C 803
SITE 1 AD4 2 ASN C 220 THR C 222
SITE 1 AD5 2 MAN B 809 ASN C 670
CRYST1 127.440 235.910 167.270 90.00 90.00 90.00 C 2 2 21 24
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 0.007847 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004239 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005978 0.00000
TER 4250 SER A 698
TER 8500 SER B 698
TER 12750 SER C 698
MASTER 461 0 23 68 44 0 14 612977 3 249 129
END |