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HEADER HYDROLASE 13-SEP-17 5YDH
TITLE CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE CATALYTIC SUBUNITS OF THE
TITLE 2 MALARIA VECTOR ANOPHELES GAMBIAE, 3.2 A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 162-737;
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/BETA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.HAN,H.GUAN,H.ROBINSON,H.DING,C.LIAO,J.LI
REVDAT 1 07-MAR-18 5YDH 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. 3.21 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 : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 43806
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) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2338
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) : 3.21
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.29
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3246
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3160
REMARK 3 BIN FREE R VALUE SET COUNT : 171
REMARK 3 BIN FREE R VALUE : 0.3370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8514
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 334
REMARK 3 SOLVENT ATOMS : 12
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 84.29
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) : -0.02000
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): 0.697
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.340
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.262
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.015
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9090 ; 0.004 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12435 ; 1.020 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1074 ; 4.926 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 424 ;33.602 ;23.349
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1324 ;14.919 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 70 ;14.047 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1357 ; 0.069 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6994 ; 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 : MASK
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 5YDH 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_1300005085.
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 : 43806
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.210
REMARK 200 RESOLUTION RANGE LOW (A) : 56.510
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 63.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.21
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.38
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: MOLREP
REMARK 200 STARTING MODEL: 4NQH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 78.93
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, PH 7.5, VAPOR DIFFUSION, HANGING 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 75.34033
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 150.68067
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 113.01050
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 188.35083
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 37.67017
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: 10800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -285.0 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 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 PHE A 715
REMARK 465 PHE A 716
REMARK 465 TYR A 717
REMARK 465 ARG A 718
REMARK 465 PRO A 719
REMARK 465 ASP A 720
REMARK 465 LEU A 721
REMARK 465 ILE A 722
REMARK 465 VAL A 723
REMARK 465 LEU A 724
REMARK 465 LEU A 725
REMARK 465 VAL A 726
REMARK 465 SER A 727
REMARK 465 LEU A 728
REMARK 465 LEU A 729
REMARK 465 THR A 730
REMARK 465 ALA A 731
REMARK 465 THR A 732
REMARK 465 VAL A 733
REMARK 465 ARG A 734
REMARK 465 PHE A 735
REMARK 465 ILE A 736
REMARK 465 GLN A 737
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 PHE B 715
REMARK 465 PHE B 716
REMARK 465 TYR B 717
REMARK 465 ARG B 718
REMARK 465 PRO B 719
REMARK 465 ASP B 720
REMARK 465 LEU B 721
REMARK 465 ILE B 722
REMARK 465 VAL B 723
REMARK 465 LEU B 724
REMARK 465 LEU B 725
REMARK 465 VAL B 726
REMARK 465 SER B 727
REMARK 465 LEU B 728
REMARK 465 LEU B 729
REMARK 465 THR B 730
REMARK 465 ALA B 731
REMARK 465 THR B 732
REMARK 465 VAL B 733
REMARK 465 ARG B 734
REMARK 465 PHE B 735
REMARK 465 ILE B 736
REMARK 465 GLN B 737
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 670 O5 NAG A 811 1.78
REMARK 500 ND2 ASN B 670 C2 NAG B 817 2.12
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 ASP A 171 -9.89 -57.53
REMARK 500 PHE A 206 -26.47 74.99
REMARK 500 ASP A 238 34.90 -95.22
REMARK 500 ALA A 312 -154.75 62.51
REMARK 500 SER A 360 -116.69 57.77
REMARK 500 GLN A 380 -66.21 -105.22
REMARK 500 GLU A 485 71.80 -119.99
REMARK 500 GLU A 540 79.90 -155.77
REMARK 500 PHE A 560 -70.99 -134.22
REMARK 500 ALA A 647 71.89 57.51
REMARK 500 LYS A 688 -60.31 -108.59
REMARK 500 PHE B 206 -21.07 68.72
REMARK 500 CYS B 255 -3.36 -145.90
REMARK 500 ASN B 269 74.27 46.34
REMARK 500 PHE B 281 11.13 59.44
REMARK 500 ALA B 312 -155.04 61.63
REMARK 500 PHE B 316 11.19 -143.25
REMARK 500 ASN B 327 17.73 59.80
REMARK 500 ARG B 353 36.46 -95.50
REMARK 500 SER B 360 -114.34 53.22
REMARK 500 GLN B 380 -81.85 -95.60
REMARK 500 LEU B 395 156.60 175.84
REMARK 500 HIS B 416 58.71 -110.66
REMARK 500 ALA B 458 -60.95 -91.45
REMARK 500 GLU B 485 77.37 -116.75
REMARK 500 TYR B 535 63.98 -111.78
REMARK 500 PHE B 560 -78.29 -137.28
REMARK 500 ALA B 647 70.46 56.09
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 A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 816
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 817
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 818
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 819
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CO A 820
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 812
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 813
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 814
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 815
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 816
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE B 823
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 824
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CO B 825
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 812 through MAN A 815 bound to ASN A 220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 811 bound
REMARK 800 to ASN A 670
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 818 through MAN B 822 bound to ASN B 220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 817 bound
REMARK 800 to ASN B 670
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5X61 RELATED DB: PDB
DBREF 5YDH A 162 737 UNP Q869C3 ACES_ANOGA 162 737
DBREF 5YDH B 162 737 UNP Q869C3 ACES_ANOGA 162 737
SEQRES 1 A 576 ASP ASN ASP PRO LEU VAL VAL ASN THR ASP LYS GLY ARG
SEQRES 2 A 576 ILE ARG GLY ILE THR VAL ASP ALA PRO SER GLY LYS LYS
SEQRES 3 A 576 VAL ASP VAL TRP LEU GLY ILE PRO TYR ALA GLN PRO PRO
SEQRES 4 A 576 VAL GLY PRO LEU ARG PHE ARG HIS PRO ARG PRO ALA GLU
SEQRES 5 A 576 LYS TRP THR GLY VAL LEU ASN THR THR THR PRO PRO ASN
SEQRES 6 A 576 SER CYS VAL GLN ILE VAL ASP THR VAL PHE GLY ASP PHE
SEQRES 7 A 576 PRO GLY ALA THR MET TRP ASN PRO ASN THR PRO LEU SER
SEQRES 8 A 576 GLU ASP CYS LEU TYR ILE ASN VAL VAL ALA PRO ARG PRO
SEQRES 9 A 576 ARG PRO LYS ASN ALA ALA VAL MET LEU TRP ILE PHE GLY
SEQRES 10 A 576 GLY GLY PHE TYR SER GLY THR ALA THR LEU ASP VAL TYR
SEQRES 11 A 576 ASP HIS ARG ALA LEU ALA SER GLU GLU ASN VAL ILE VAL
SEQRES 12 A 576 VAL SER LEU GLN TYR ARG VAL ALA SER LEU GLY PHE LEU
SEQRES 13 A 576 PHE LEU GLY THR PRO GLU ALA PRO GLY ASN ALA GLY LEU
SEQRES 14 A 576 PHE ASP GLN ASN LEU ALA LEU ARG TRP VAL ARG ASP ASN
SEQRES 15 A 576 ILE HIS ARG PHE GLY GLY ASP PRO SER ARG VAL THR LEU
SEQRES 16 A 576 PHE GLY GLU SER ALA GLY ALA VAL SER VAL SER LEU HIS
SEQRES 17 A 576 LEU LEU SER ALA LEU SER ARG ASP LEU PHE GLN ARG ALA
SEQRES 18 A 576 ILE LEU GLN SER GLY SER PRO THR ALA PRO TRP ALA LEU
SEQRES 19 A 576 VAL SER ARG GLU GLU ALA THR LEU ARG ALA LEU ARG LEU
SEQRES 20 A 576 ALA GLU ALA VAL GLY CYS PRO HIS GLU PRO SER LYS LEU
SEQRES 21 A 576 SER ASP ALA VAL GLU CYS LEU ARG GLY LYS ASP PRO HIS
SEQRES 22 A 576 VAL LEU VAL ASN ASN GLU TRP GLY THR LEU GLY ILE CYS
SEQRES 23 A 576 GLU PHE PRO PHE VAL PRO VAL VAL ASP GLY ALA PHE LEU
SEQRES 24 A 576 ASP GLU THR PRO GLN ARG SER LEU ALA SER GLY ARG PHE
SEQRES 25 A 576 LYS LYS THR GLU ILE LEU THR GLY SER ASN THR GLU GLU
SEQRES 26 A 576 GLY TYR TYR PHE ILE ILE TYR TYR LEU THR GLU LEU LEU
SEQRES 27 A 576 ARG LYS GLU GLU GLY VAL THR VAL THR ARG GLU GLU PHE
SEQRES 28 A 576 LEU GLN ALA VAL ARG GLU LEU ASN PRO TYR VAL ASN GLY
SEQRES 29 A 576 ALA ALA ARG GLN ALA ILE VAL PHE GLU TYR THR ASP TRP
SEQRES 30 A 576 THR GLU PRO ASP ASN PRO ASN SER ASN ARG ASP ALA LEU
SEQRES 31 A 576 ASP LYS MET VAL GLY ASP TYR HIS PHE THR CYS ASN VAL
SEQRES 32 A 576 ASN GLU PHE ALA GLN ARG TYR ALA GLU GLU GLY ASN ASN
SEQRES 33 A 576 VAL TYR MET TYR LEU TYR THR HIS ARG SER LYS GLY ASN
SEQRES 34 A 576 PRO TRP PRO ARG TRP THR GLY VAL MET HIS GLY ASP GLU
SEQRES 35 A 576 ILE ASN TYR VAL PHE GLY GLU PRO LEU ASN PRO THR LEU
SEQRES 36 A 576 GLY TYR THR GLU ASP GLU LYS ASP PHE SER ARG LYS ILE
SEQRES 37 A 576 MET ARG TYR TRP SER ASN PHE ALA LYS THR GLY ASN PRO
SEQRES 38 A 576 ASN PRO ASN THR ALA SER SER GLU PHE PRO GLU TRP PRO
SEQRES 39 A 576 LYS HIS THR ALA HIS GLY ARG HIS TYR LEU GLU LEU GLY
SEQRES 40 A 576 LEU ASN THR SER PHE VAL GLY ARG GLY PRO ARG LEU ARG
SEQRES 41 A 576 GLN CYS ALA PHE TRP LYS LYS TYR LEU PRO GLN LEU VAL
SEQRES 42 A 576 ALA ALA THR SER ASN LEU PRO GLY PRO ALA PRO PRO SER
SEQRES 43 A 576 GLU PRO CYS GLU SER SER ALA PHE PHE TYR ARG PRO ASP
SEQRES 44 A 576 LEU ILE VAL LEU LEU VAL SER LEU LEU THR ALA THR VAL
SEQRES 45 A 576 ARG PHE ILE GLN
SEQRES 1 B 576 ASP ASN ASP PRO LEU VAL VAL ASN THR ASP LYS GLY ARG
SEQRES 2 B 576 ILE ARG GLY ILE THR VAL ASP ALA PRO SER GLY LYS LYS
SEQRES 3 B 576 VAL ASP VAL TRP LEU GLY ILE PRO TYR ALA GLN PRO PRO
SEQRES 4 B 576 VAL GLY PRO LEU ARG PHE ARG HIS PRO ARG PRO ALA GLU
SEQRES 5 B 576 LYS TRP THR GLY VAL LEU ASN THR THR THR PRO PRO ASN
SEQRES 6 B 576 SER CYS VAL GLN ILE VAL ASP THR VAL PHE GLY ASP PHE
SEQRES 7 B 576 PRO GLY ALA THR MET TRP ASN PRO ASN THR PRO LEU SER
SEQRES 8 B 576 GLU ASP CYS LEU TYR ILE ASN VAL VAL ALA PRO ARG PRO
SEQRES 9 B 576 ARG PRO LYS ASN ALA ALA VAL MET LEU TRP ILE PHE GLY
SEQRES 10 B 576 GLY GLY PHE TYR SER GLY THR ALA THR LEU ASP VAL TYR
SEQRES 11 B 576 ASP HIS ARG ALA LEU ALA SER GLU GLU ASN VAL ILE VAL
SEQRES 12 B 576 VAL SER LEU GLN TYR ARG VAL ALA SER LEU GLY PHE LEU
SEQRES 13 B 576 PHE LEU GLY THR PRO GLU ALA PRO GLY ASN ALA GLY LEU
SEQRES 14 B 576 PHE ASP GLN ASN LEU ALA LEU ARG TRP VAL ARG ASP ASN
SEQRES 15 B 576 ILE HIS ARG PHE GLY GLY ASP PRO SER ARG VAL THR LEU
SEQRES 16 B 576 PHE GLY GLU SER ALA GLY ALA VAL SER VAL SER LEU HIS
SEQRES 17 B 576 LEU LEU SER ALA LEU SER ARG ASP LEU PHE GLN ARG ALA
SEQRES 18 B 576 ILE LEU GLN SER GLY SER PRO THR ALA PRO TRP ALA LEU
SEQRES 19 B 576 VAL SER ARG GLU GLU ALA THR LEU ARG ALA LEU ARG LEU
SEQRES 20 B 576 ALA GLU ALA VAL GLY CYS PRO HIS GLU PRO SER LYS LEU
SEQRES 21 B 576 SER ASP ALA VAL GLU CYS LEU ARG GLY LYS ASP PRO HIS
SEQRES 22 B 576 VAL LEU VAL ASN ASN GLU TRP GLY THR LEU GLY ILE CYS
SEQRES 23 B 576 GLU PHE PRO PHE VAL PRO VAL VAL ASP GLY ALA PHE LEU
SEQRES 24 B 576 ASP GLU THR PRO GLN ARG SER LEU ALA SER GLY ARG PHE
SEQRES 25 B 576 LYS LYS THR GLU ILE LEU THR GLY SER ASN THR GLU GLU
SEQRES 26 B 576 GLY TYR TYR PHE ILE ILE TYR TYR LEU THR GLU LEU LEU
SEQRES 27 B 576 ARG LYS GLU GLU GLY VAL THR VAL THR ARG GLU GLU PHE
SEQRES 28 B 576 LEU GLN ALA VAL ARG GLU LEU ASN PRO TYR VAL ASN GLY
SEQRES 29 B 576 ALA ALA ARG GLN ALA ILE VAL PHE GLU TYR THR ASP TRP
SEQRES 30 B 576 THR GLU PRO ASP ASN PRO ASN SER ASN ARG ASP ALA LEU
SEQRES 31 B 576 ASP LYS MET VAL GLY ASP TYR HIS PHE THR CYS ASN VAL
SEQRES 32 B 576 ASN GLU PHE ALA GLN ARG TYR ALA GLU GLU GLY ASN ASN
SEQRES 33 B 576 VAL TYR MET TYR LEU TYR THR HIS ARG SER LYS GLY ASN
SEQRES 34 B 576 PRO TRP PRO ARG TRP THR GLY VAL MET HIS GLY ASP GLU
SEQRES 35 B 576 ILE ASN TYR VAL PHE GLY GLU PRO LEU ASN PRO THR LEU
SEQRES 36 B 576 GLY TYR THR GLU ASP GLU LYS ASP PHE SER ARG LYS ILE
SEQRES 37 B 576 MET ARG TYR TRP SER ASN PHE ALA LYS THR GLY ASN PRO
SEQRES 38 B 576 ASN PRO ASN THR ALA SER SER GLU PHE PRO GLU TRP PRO
SEQRES 39 B 576 LYS HIS THR ALA HIS GLY ARG HIS TYR LEU GLU LEU GLY
SEQRES 40 B 576 LEU ASN THR SER PHE VAL GLY ARG GLY PRO ARG LEU ARG
SEQRES 41 B 576 GLN CYS ALA PHE TRP LYS LYS TYR LEU PRO GLN LEU VAL
SEQRES 42 B 576 ALA ALA THR SER ASN LEU PRO GLY PRO ALA PRO PRO SER
SEQRES 43 B 576 GLU PRO CYS GLU SER SER ALA PHE PHE TYR ARG PRO ASP
SEQRES 44 B 576 LEU ILE VAL LEU LEU VAL SER LEU LEU THR ALA THR VAL
SEQRES 45 B 576 ARG PHE ILE GLN
MODRES 5YDH ASN A 670 ASN GLYCOSYLATION SITE
MODRES 5YDH ASN A 220 ASN GLYCOSYLATION SITE
MODRES 5YDH ASN B 220 ASN GLYCOSYLATION SITE
MODRES 5YDH ASN B 670 ASN GLYCOSYLATION SITE
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 SO4 A 809 5
HET SO4 A 810 5
HET NAG A 811 14
HET NAG A 812 14
HET NAG A 813 14
HET BMA A 814 11
HET MAN A 815 11
HET EPE A 816 15
HET EPE A 817 15
HET GOL A 818 6
HET GOL A 819 6
HET CO A 820 1
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 SO4 B 809 5
HET SO4 B 810 5
HET SO4 B 811 5
HET SO4 B 812 5
HET SO4 B 813 5
HET SO4 B 814 5
HET SO4 B 815 5
HET SO4 B 816 5
HET NAG B 817 14
HET NAG B 818 14
HET NAG B 819 14
HET BMA B 820 11
HET MAN B 821 11
HET MAN B 822 11
HET EPE B 823 15
HET GOL B 824 6
HET CO B 825 1
HETNAM SO4 SULFATE ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BMA BETA-D-MANNOSE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM GOL GLYCEROL
HETNAM CO COBALT (II) ION
HETSYN EPE HEPES
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 SO4 26(O4 S 2-)
FORMUL 13 NAG 6(C8 H15 N O6)
FORMUL 14 BMA 2(C6 H12 O6)
FORMUL 14 MAN 3(C6 H12 O6)
FORMUL 15 EPE 3(C8 H18 N2 O4 S)
FORMUL 17 GOL 3(C3 H8 O3)
FORMUL 19 CO 2(CO 2+)
FORMUL 41 HOH *12(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 ALA A 312 LEU A 317 1 6
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 LEU A 421 ARG A 429 1 9
HELIX 11 AB2 ASP A 432 ASN A 438 1 7
HELIX 12 AB3 THR A 463 GLY A 471 1 9
HELIX 13 AB4 GLY A 487 TYR A 494 1 8
HELIX 14 AB5 THR A 508 ASN A 520 1 13
HELIX 15 AB6 GLY A 525 TYR A 535 1 11
HELIX 16 AB7 ASN A 543 PHE A 560 1 18
HELIX 17 AB8 PHE A 560 GLU A 574 1 15
HELIX 18 AB9 PRO A 593 GLY A 597 5 5
HELIX 19 AC1 GLU A 603 PHE A 608 1 6
HELIX 20 AC2 GLY A 609 ASN A 613 5 5
HELIX 21 AC3 THR A 619 GLY A 640 1 22
HELIX 22 AC4 ARG A 679 LYS A 688 1 10
HELIX 23 AC5 LYS A 688 THR A 697 1 10
HELIX 24 AC6 VAL B 201 ARG B 205 5 5
HELIX 25 AC7 PHE B 239 MET B 244 1 6
HELIX 26 AC8 LEU B 288 TYR B 291 5 4
HELIX 27 AC9 ASP B 292 ASN B 301 1 10
HELIX 28 AD1 ALA B 312 LEU B 317 1 6
HELIX 29 AD2 ASN B 327 ILE B 344 1 18
HELIX 30 AD3 SER B 360 SER B 372 1 13
HELIX 31 AD4 SER B 397 GLY B 413 1 17
HELIX 32 AD5 LEU B 421 ARG B 429 1 9
HELIX 33 AD6 ASP B 432 ASN B 438 1 7
HELIX 34 AD7 THR B 463 GLY B 471 1 9
HELIX 35 AD8 GLY B 487 TYR B 494 1 8
HELIX 36 AD9 THR B 508 ASN B 520 1 13
HELIX 37 AE1 GLY B 525 TYR B 535 1 11
HELIX 38 AE2 ASN B 543 PHE B 560 1 18
HELIX 39 AE3 PHE B 560 GLU B 573 1 14
HELIX 40 AE4 PRO B 593 GLY B 597 5 5
HELIX 41 AE5 GLU B 603 PHE B 608 1 6
HELIX 42 AE6 GLY B 609 ASN B 613 5 5
HELIX 43 AE7 THR B 619 THR B 639 1 21
HELIX 44 AE8 ARG B 679 LYS B 688 1 10
HELIX 45 AE9 LYS B 688 SER B 698 1 11
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 PHE A 357 N LEU A 274
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 583 N SER A 482
SHEET 10 AA211 HIS A 663 LEU A 667 1 O LEU A 667 N LEU A 582
SHEET 11 AA211 VAL A 674 ARG A 676 -1 O GLY A 675 N TYR A 664
SHEET 1 AA3 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 ILE B 175 N VAL B 168
SHEET 3 AA4 3 VAL B 218 ASN B 220 1 O LEU B 219 N ARG B 174
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 VAL B 260 N TRP B 191
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 665 N MET B 580
SHEET 11 AA511 VAL B 674 ARG B 676 -1 O GLY B 675 N TYR B 664
SSBOND 1 CYS A 228 CYS A 255 1555 1555 2.04
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 2.02
SSBOND 6 CYS B 562 CYS B 683 1555 1555 2.04
LINK ND2 ASN A 220 C1 NAG A 812 1555 1555 1.45
LINK NE2 HIS A 416 CO CO A 820 1555 1555 2.21
LINK ND2 ASN A 670 C1 NAG A 811 1555 1555 1.45
LINK ND2 ASN B 220 C1 NAG B 818 1555 1555 1.44
LINK NE2 HIS B 416 CO CO B 825 1555 1555 2.25
LINK ND2 ASN B 670 C1 NAG B 817 1555 1555 1.44
LINK O4 NAG A 812 C1 NAG A 813 1555 1555 1.44
LINK O4 NAG A 813 C1 BMA A 814 1555 1555 1.45
LINK O3 BMA A 814 C1 MAN A 815 1555 1555 1.45
LINK O4 NAG B 818 C1 NAG B 819 1555 1555 1.45
LINK O4 NAG B 819 C1 BMA B 820 1555 1555 1.45
LINK O3 BMA B 820 C1 MAN B 822 1555 1555 1.45
LINK O6 BMA B 820 C1 MAN B 821 1555 1555 1.45
CISPEP 1 ARG A 264 PRO A 265 0 7.23
CISPEP 2 GLY A 677 PRO A 678 0 -0.17
CISPEP 3 ARG B 264 PRO B 265 0 3.64
CISPEP 4 GLY B 677 PRO B 678 0 0.94
SITE 1 AC1 2 ARG A 353 LYS A 638
SITE 1 AC2 3 VAL A 523 ASN A 524 ARG A 528
SITE 1 AC3 3 SER A 397 ARG A 398 GLU A 399
SITE 1 AC4 3 SER A 470 ARG A 472 PRO B 203
SITE 1 AC5 5 ARG A 376 PHE A 473 LYS A 474 LYS A 475
SITE 2 AC5 5 GLU B 213
SITE 1 AC6 5 THR A 321 SER A 419 LYS A 420 LEU A 421
SITE 2 AC6 5 SER A 422
SITE 1 AC7 5 THR A 536 ASP A 537 TRP A 538 THR A 539
SITE 2 AC7 5 ARG B 681
SITE 1 AC8 3 GLU A 503 GLY A 504 ARG A 594
SITE 1 AC9 6 LEU A 192 VAL A 261 TYR A 291 ASP A 292
SITE 2 AC9 6 HIS A 293 ARG A 294
SITE 1 AD1 6 GLU A 485 TYR A 488 ARG A 548 ASP A 549
SITE 2 AD1 6 TRP A 595 GLY A 597
SITE 1 AD2 5 ILE A 231 TYR A 282 TRP A 441 TYR A 489
SITE 2 AD2 5 TYR A 493
SITE 1 AD3 3 GLY A 442 LEU A 444 TYR A 494
SITE 1 AD4 4 GLY A 279 GLY A 280 TYR A 282 SER A 360
SITE 1 AD5 2 THR A 658 HIS A 663
SITE 1 AD6 1 HIS A 416
SITE 1 AD7 2 ARG B 353 LYS B 638
SITE 1 AD8 2 SER B 470 ARG B 472
SITE 1 AD9 3 SER B 397 ARG B 398 GLU B 399
SITE 1 AE1 3 THR B 658 GLY B 661 HIS B 663
SITE 1 AE2 2 GLY B 504 ARG B 594
SITE 1 AE3 2 ASN B 524 ARG B 528
SITE 1 AE4 2 ARG B 528 GLN B 529
SITE 1 AE5 2 GLU B 503 ARG B 594
SITE 1 AE6 2 ARG B 264 PRO B 265
SITE 1 AE7 4 ARG B 631 ASN B 635 PRO B 644 PHE B 651
SITE 1 AE8 3 ARG B 174 THR B 216 GLY B 217
SITE 1 AE9 2 GLY B 217 VAL B 218
SITE 1 AF1 5 ARG A 681 THR B 536 ASP B 537 TRP B 538
SITE 2 AF1 5 THR B 539
SITE 1 AF2 1 ARG B 174
SITE 1 AF3 3 ASN B 259 ALA B 286 HIS B 293
SITE 1 AF4 2 GLY B 442 LEU B 444
SITE 1 AF5 3 TYR B 282 TRP B 441 TYR B 493
SITE 1 AF6 5 GLY B 278 GLY B 279 GLY B 280 SER B 360
SITE 2 AF6 5 TYR B 489
SITE 1 AF7 1 HIS B 416
SITE 1 AF8 2 ARG A 176 ASN A 220
SITE 1 AF9 1 ASN A 670
SITE 1 AG1 3 SER A 184 ARG B 176 ASN B 220
SITE 1 AG2 1 ASN B 670
CRYST1 148.659 148.659 226.021 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 0.006727 0.003884 0.000000 0.00000
SCALE2 0.000000 0.007767 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004424 0.00000
TER 4258 ASN A 699
TER 8516 ASN B 699
MASTER 544 0 45 45 30 0 46 6 8860 2 352 90
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