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HEADER HYDROLASE 13-SEP-17 5YDJ
TITLE CRYSTAL STRUCTURE OF ANOPHELES GAMBIAE ACETYLCHOLINESTERASE IN COMPLEX
TITLE 2 WITH PMSF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: 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 ACETYLCHOLINESTERASE PMSF, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.HAN,H.GUAN,H.DING,C.LIAO,H.ROBINSON,J.LI
REVDAT 1 07-MAR-18 5YDJ 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. 3.04 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
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) : 3.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 50417
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) : 0.253
REMARK 3 R VALUE (WORKING SET) : 0.251
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2701
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) : 3.04
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.12
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3703
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3340
REMARK 3 BIN FREE R VALUE SET COUNT : 215
REMARK 3 BIN FREE R VALUE : 0.3710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8534
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 231
REMARK 3 SOLVENT ATOMS : 48
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.04000
REMARK 3 B12 (A**2) : 0.01000
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): 0.592
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.370
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.850
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.804
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9002 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 7936 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12304 ; 1.172 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18384 ; 3.819 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1074 ; 5.577 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 426 ;32.087 ;23.333
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1324 ;14.311 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 70 ;13.064 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1331 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9948 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1924 ; 0.011 ; 0.020
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): 4302 ; 3.750 ; 5.780
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4301 ; 3.740 ; 5.779
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5374 ; 5.811 ; 8.669
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5375 ; 5.811 ; 8.670
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4700 ; 4.406 ; 6.137
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4700 ; 4.260 ; 6.137
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6931 ; 5.823 ; 9.117
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 9647 ; 8.343 ;67.201
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 9648 ; 8.354 ;67.195
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5YDJ 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_1300005090.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAY-14
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 : NULL
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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51171
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.040
REMARK 200 RESOLUTION RANGE LOW (A) : 61.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 22.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 24.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.04
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.12
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: 5X61
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES BUFFER, 1.6M AMMONIUM
REMARK 280 SULFATE, PH 7.5, 277K, VAPOR DIFFUSION, HANGING DROP
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 74.72667
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 149.45333
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 112.09000
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 186.81667
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 37.36333
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: 9170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -358.0 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 MET A 1
REMARK 465 GLU A 2
REMARK 465 ILE A 3
REMARK 465 ARG A 4
REMARK 465 GLY A 5
REMARK 465 LEU A 6
REMARK 465 LEU A 7
REMARK 465 MET A 8
REMARK 465 GLY A 9
REMARK 465 ARG A 10
REMARK 465 LEU A 11
REMARK 465 ARG A 12
REMARK 465 LEU A 13
REMARK 465 GLY A 14
REMARK 465 ARG A 15
REMARK 465 ARG A 16
REMARK 465 MET A 17
REMARK 465 VAL A 18
REMARK 465 PRO A 19
REMARK 465 LEU A 20
REMARK 465 GLY A 21
REMARK 465 LEU A 22
REMARK 465 LEU A 23
REMARK 465 GLY A 24
REMARK 465 VAL A 25
REMARK 465 THR A 26
REMARK 465 ALA A 27
REMARK 465 LEU A 28
REMARK 465 LEU A 29
REMARK 465 LEU A 30
REMARK 465 ILE A 31
REMARK 465 LEU A 32
REMARK 465 PRO A 33
REMARK 465 PRO A 34
REMARK 465 PHE A 35
REMARK 465 ALA A 36
REMARK 465 LEU A 37
REMARK 465 VAL A 38
REMARK 465 GLN A 39
REMARK 465 GLY A 40
REMARK 465 ARG A 41
REMARK 465 HIS A 42
REMARK 465 HIS A 43
REMARK 465 GLU A 44
REMARK 465 LEU A 45
REMARK 465 ASN A 46
REMARK 465 ASN A 47
REMARK 465 GLY A 48
REMARK 465 ALA A 49
REMARK 465 ALA A 50
REMARK 465 ILE A 51
REMARK 465 GLY A 52
REMARK 465 SER A 53
REMARK 465 HIS A 54
REMARK 465 GLN A 55
REMARK 465 LEU A 56
REMARK 465 SER A 57
REMARK 465 ALA A 58
REMARK 465 ALA A 59
REMARK 465 ALA A 60
REMARK 465 GLY A 61
REMARK 465 VAL A 62
REMARK 465 GLY A 63
REMARK 465 LEU A 64
REMARK 465 ALA A 65
REMARK 465 SER A 66
REMARK 465 GLN A 67
REMARK 465 SER A 68
REMARK 465 ALA A 69
REMARK 465 GLN A 70
REMARK 465 SER A 71
REMARK 465 GLY A 72
REMARK 465 SER A 73
REMARK 465 LEU A 74
REMARK 465 ALA A 75
REMARK 465 SER A 76
REMARK 465 GLY A 77
REMARK 465 VAL A 78
REMARK 465 MET A 79
REMARK 465 SER A 80
REMARK 465 SER A 81
REMARK 465 VAL A 82
REMARK 465 PRO A 83
REMARK 465 ALA A 84
REMARK 465 ALA A 85
REMARK 465 GLY A 86
REMARK 465 ALA A 87
REMARK 465 SER A 88
REMARK 465 SER A 89
REMARK 465 SER A 90
REMARK 465 SER A 91
REMARK 465 SER A 92
REMARK 465 SER A 93
REMARK 465 SER A 94
REMARK 465 LEU A 95
REMARK 465 LEU A 96
REMARK 465 SER A 97
REMARK 465 SER A 98
REMARK 465 SER A 99
REMARK 465 ALA A 100
REMARK 465 GLU A 101
REMARK 465 ASP A 102
REMARK 465 ASP A 103
REMARK 465 VAL A 104
REMARK 465 ALA A 105
REMARK 465 ARG A 106
REMARK 465 ILE A 107
REMARK 465 THR A 108
REMARK 465 LEU A 109
REMARK 465 SER A 110
REMARK 465 LYS A 111
REMARK 465 ASP A 112
REMARK 465 ALA A 113
REMARK 465 ASP A 114
REMARK 465 ALA A 115
REMARK 465 PHE A 116
REMARK 465 PHE A 117
REMARK 465 THR A 118
REMARK 465 PRO A 119
REMARK 465 TYR A 120
REMARK 465 ILE A 121
REMARK 465 GLY A 122
REMARK 465 HIS A 123
REMARK 465 GLY A 124
REMARK 465 GLU A 125
REMARK 465 SER A 126
REMARK 465 VAL A 127
REMARK 465 ARG A 128
REMARK 465 ILE A 129
REMARK 465 ILE A 130
REMARK 465 ASP A 131
REMARK 465 ALA A 132
REMARK 465 GLU A 133
REMARK 465 LEU A 134
REMARK 465 GLY A 135
REMARK 465 THR A 136
REMARK 465 LEU A 137
REMARK 465 GLU A 138
REMARK 465 HIS A 139
REMARK 465 VAL A 140
REMARK 465 HIS A 141
REMARK 465 SER A 142
REMARK 465 GLY A 143
REMARK 465 ALA A 144
REMARK 465 THR A 145
REMARK 465 PRO A 146
REMARK 465 ARG A 147
REMARK 465 ARG A 148
REMARK 465 ARG A 149
REMARK 465 GLY A 150
REMARK 465 LEU A 151
REMARK 465 THR A 152
REMARK 465 ARG A 153
REMARK 465 ARG A 154
REMARK 465 GLU A 155
REMARK 465 SER A 156
REMARK 465 ASN A 157
REMARK 465 SER A 158
REMARK 465 ASP A 159
REMARK 465 ALA A 160
REMARK 465 ASN A 161
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 MET B 1
REMARK 465 GLU B 2
REMARK 465 ILE B 3
REMARK 465 ARG B 4
REMARK 465 GLY B 5
REMARK 465 LEU B 6
REMARK 465 LEU B 7
REMARK 465 MET B 8
REMARK 465 GLY B 9
REMARK 465 ARG B 10
REMARK 465 LEU B 11
REMARK 465 ARG B 12
REMARK 465 LEU B 13
REMARK 465 GLY B 14
REMARK 465 ARG B 15
REMARK 465 ARG B 16
REMARK 465 MET B 17
REMARK 465 VAL B 18
REMARK 465 PRO B 19
REMARK 465 LEU B 20
REMARK 465 GLY B 21
REMARK 465 LEU B 22
REMARK 465 LEU B 23
REMARK 465 GLY B 24
REMARK 465 VAL B 25
REMARK 465 THR B 26
REMARK 465 ALA B 27
REMARK 465 LEU B 28
REMARK 465 LEU B 29
REMARK 465 LEU B 30
REMARK 465 ILE B 31
REMARK 465 LEU B 32
REMARK 465 PRO B 33
REMARK 465 PRO B 34
REMARK 465 PHE B 35
REMARK 465 ALA B 36
REMARK 465 LEU B 37
REMARK 465 VAL B 38
REMARK 465 GLN B 39
REMARK 465 GLY B 40
REMARK 465 ARG B 41
REMARK 465 HIS B 42
REMARK 465 HIS B 43
REMARK 465 GLU B 44
REMARK 465 LEU B 45
REMARK 465 ASN B 46
REMARK 465 ASN B 47
REMARK 465 GLY B 48
REMARK 465 ALA B 49
REMARK 465 ALA B 50
REMARK 465 ILE B 51
REMARK 465 GLY B 52
REMARK 465 SER B 53
REMARK 465 HIS B 54
REMARK 465 GLN B 55
REMARK 465 LEU B 56
REMARK 465 SER B 57
REMARK 465 ALA B 58
REMARK 465 ALA B 59
REMARK 465 ALA B 60
REMARK 465 GLY B 61
REMARK 465 VAL B 62
REMARK 465 GLY B 63
REMARK 465 LEU B 64
REMARK 465 ALA B 65
REMARK 465 SER B 66
REMARK 465 GLN B 67
REMARK 465 SER B 68
REMARK 465 ALA B 69
REMARK 465 GLN B 70
REMARK 465 SER B 71
REMARK 465 GLY B 72
REMARK 465 SER B 73
REMARK 465 LEU B 74
REMARK 465 ALA B 75
REMARK 465 SER B 76
REMARK 465 GLY B 77
REMARK 465 VAL B 78
REMARK 465 MET B 79
REMARK 465 SER B 80
REMARK 465 SER B 81
REMARK 465 VAL B 82
REMARK 465 PRO B 83
REMARK 465 ALA B 84
REMARK 465 ALA B 85
REMARK 465 GLY B 86
REMARK 465 ALA B 87
REMARK 465 SER B 88
REMARK 465 SER B 89
REMARK 465 SER B 90
REMARK 465 SER B 91
REMARK 465 SER B 92
REMARK 465 SER B 93
REMARK 465 SER B 94
REMARK 465 LEU B 95
REMARK 465 LEU B 96
REMARK 465 SER B 97
REMARK 465 SER B 98
REMARK 465 SER B 99
REMARK 465 ALA B 100
REMARK 465 GLU B 101
REMARK 465 ASP B 102
REMARK 465 ASP B 103
REMARK 465 VAL B 104
REMARK 465 ALA B 105
REMARK 465 ARG B 106
REMARK 465 ILE B 107
REMARK 465 THR B 108
REMARK 465 LEU B 109
REMARK 465 SER B 110
REMARK 465 LYS B 111
REMARK 465 ASP B 112
REMARK 465 ALA B 113
REMARK 465 ASP B 114
REMARK 465 ALA B 115
REMARK 465 PHE B 116
REMARK 465 PHE B 117
REMARK 465 THR B 118
REMARK 465 PRO B 119
REMARK 465 TYR B 120
REMARK 465 ILE B 121
REMARK 465 GLY B 122
REMARK 465 HIS B 123
REMARK 465 GLY B 124
REMARK 465 GLU B 125
REMARK 465 SER B 126
REMARK 465 VAL B 127
REMARK 465 ARG B 128
REMARK 465 ILE B 129
REMARK 465 ILE B 130
REMARK 465 ASP B 131
REMARK 465 ALA B 132
REMARK 465 GLU B 133
REMARK 465 LEU B 134
REMARK 465 GLY B 135
REMARK 465 THR B 136
REMARK 465 LEU B 137
REMARK 465 GLU B 138
REMARK 465 HIS B 139
REMARK 465 VAL B 140
REMARK 465 HIS B 141
REMARK 465 SER B 142
REMARK 465 GLY B 143
REMARK 465 ALA B 144
REMARK 465 THR B 145
REMARK 465 PRO B 146
REMARK 465 ARG B 147
REMARK 465 ARG B 148
REMARK 465 ARG B 149
REMARK 465 GLY B 150
REMARK 465 LEU B 151
REMARK 465 THR B 152
REMARK 465 ARG B 153
REMARK 465 ARG B 154
REMARK 465 GLU B 155
REMARK 465 SER B 156
REMARK 465 ASN B 157
REMARK 465 SER B 158
REMARK 465 ASP B 159
REMARK 465 ALA B 160
REMARK 465 ASN B 161
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: 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 -21.02 73.30
REMARK 500 ASP A 238 50.42 -102.67
REMARK 500 LYS A 268 -67.42 -103.05
REMARK 500 TYR A 291 35.41 -95.90
REMARK 500 ALA A 312 -153.48 62.92
REMARK 500 PHE A 316 28.05 -143.28
REMARK 500 SEB A 360 -124.11 58.32
REMARK 500 GLN A 380 -74.89 -111.08
REMARK 500 VAL A 455 99.02 -68.97
REMARK 500 GLU A 485 77.68 -114.48
REMARK 500 LEU A 495 79.25 49.57
REMARK 500 TYR A 535 65.46 -113.84
REMARK 500 GLU A 540 74.94 -150.63
REMARK 500 PHE A 560 -72.57 -136.50
REMARK 500 SER A 672 38.75 -149.57
REMARK 500 PHE B 206 -21.33 69.86
REMARK 500 ASP B 233 99.07 -68.96
REMARK 500 ASP B 238 60.03 -118.37
REMARK 500 ASN B 269 46.75 -154.47
REMARK 500 PHE B 281 11.09 58.08
REMARK 500 TYR B 291 36.42 -88.40
REMARK 500 ALA B 312 -160.38 70.04
REMARK 500 PHE B 316 30.41 -142.73
REMARK 500 SEB B 360 -120.20 54.75
REMARK 500 GLN B 380 -73.65 -109.40
REMARK 500 PRO B 453 161.95 -47.40
REMARK 500 GLU B 485 65.07 -117.12
REMARK 500 LEU B 495 70.41 49.84
REMARK 500 TYR B 535 50.24 -117.20
REMARK 500 PHE B 560 -75.68 -126.19
REMARK 500 THR B 646 -20.91 89.85
REMARK 500 ALA B 647 83.36 60.91
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 CO A 817 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 416 CE1
REMARK 620 2 HIS A 416 NE2 37.5
REMARK 620 3 HOH A 916 O 99.2 134.0
REMARK 620 4 HOH A 906 O 140.8 104.7 120.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO B 820 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 416 CE1
REMARK 620 2 HIS B 416 NE2 30.8
REMARK 620 3 HOH B 917 O 101.4 116.5
REMARK 620 4 HOH B 916 O 140.4 159.4 80.9
REMARK 620 N 1 2 3
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 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 812
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 813
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 814
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 815
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 816
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CO A 817
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 812
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 813
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 814
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 815
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 816
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 817
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 818
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 819
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CO B 820
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 801 through NAG A 802 bound to ASN A 220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 803 bound
REMARK 800 to ASN A 670
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 801 through NAG B 802 bound to ASN B 220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 803 bound
REMARK 800 to ASN B 670
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5X61 RELATED DB: PDB
DBREF 5YDJ A 1 737 UNP Q869C3 ACES_ANOGA 1 737
DBREF 5YDJ B 1 737 UNP Q869C3 ACES_ANOGA 1 737
SEQRES 1 A 737 MET GLU ILE ARG GLY LEU LEU MET GLY ARG LEU ARG LEU
SEQRES 2 A 737 GLY ARG ARG MET VAL PRO LEU GLY LEU LEU GLY VAL THR
SEQRES 3 A 737 ALA LEU LEU LEU ILE LEU PRO PRO PHE ALA LEU VAL GLN
SEQRES 4 A 737 GLY ARG HIS HIS GLU LEU ASN ASN GLY ALA ALA ILE GLY
SEQRES 5 A 737 SER HIS GLN LEU SER ALA ALA ALA GLY VAL GLY LEU ALA
SEQRES 6 A 737 SER GLN SER ALA GLN SER GLY SER LEU ALA SER GLY VAL
SEQRES 7 A 737 MET SER SER VAL PRO ALA ALA GLY ALA SER SER SER SER
SEQRES 8 A 737 SER SER SER LEU LEU SER SER SER ALA GLU ASP ASP VAL
SEQRES 9 A 737 ALA ARG ILE THR LEU SER LYS ASP ALA ASP ALA PHE PHE
SEQRES 10 A 737 THR PRO TYR ILE GLY HIS GLY GLU SER VAL ARG ILE ILE
SEQRES 11 A 737 ASP ALA GLU LEU GLY THR LEU GLU HIS VAL HIS SER GLY
SEQRES 12 A 737 ALA THR PRO ARG ARG ARG GLY LEU THR ARG ARG GLU SER
SEQRES 13 A 737 ASN SER ASP ALA ASN ASP ASN ASP PRO LEU VAL VAL ASN
SEQRES 14 A 737 THR ASP LYS GLY ARG ILE ARG GLY ILE THR VAL ASP ALA
SEQRES 15 A 737 PRO SER GLY LYS LYS VAL ASP VAL TRP LEU GLY ILE PRO
SEQRES 16 A 737 TYR ALA GLN PRO PRO VAL GLY PRO LEU ARG PHE ARG HIS
SEQRES 17 A 737 PRO ARG PRO ALA GLU LYS TRP THR GLY VAL LEU ASN THR
SEQRES 18 A 737 THR THR PRO PRO ASN SER CYS VAL GLN ILE VAL ASP THR
SEQRES 19 A 737 VAL PHE GLY ASP PHE PRO GLY ALA THR MET TRP ASN PRO
SEQRES 20 A 737 ASN THR PRO LEU SER GLU ASP CYS LEU TYR ILE ASN VAL
SEQRES 21 A 737 VAL ALA PRO ARG PRO ARG PRO LYS ASN ALA ALA VAL MET
SEQRES 22 A 737 LEU TRP ILE PHE GLY GLY GLY PHE TYR SER GLY THR ALA
SEQRES 23 A 737 THR LEU ASP VAL TYR ASP HIS ARG ALA LEU ALA SER GLU
SEQRES 24 A 737 GLU ASN VAL ILE VAL VAL SER LEU GLN TYR ARG VAL ALA
SEQRES 25 A 737 SER LEU GLY PHE LEU PHE LEU GLY THR PRO GLU ALA PRO
SEQRES 26 A 737 GLY ASN ALA GLY LEU PHE ASP GLN ASN LEU ALA LEU ARG
SEQRES 27 A 737 TRP VAL ARG ASP ASN ILE HIS ARG PHE GLY GLY ASP PRO
SEQRES 28 A 737 SER ARG VAL THR LEU PHE GLY GLU SEB ALA GLY ALA VAL
SEQRES 29 A 737 SER VAL SER LEU HIS LEU LEU SER ALA LEU SER ARG ASP
SEQRES 30 A 737 LEU PHE GLN ARG ALA ILE LEU GLN SER GLY SER PRO THR
SEQRES 31 A 737 ALA PRO TRP ALA LEU VAL SER ARG GLU GLU ALA THR LEU
SEQRES 32 A 737 ARG ALA LEU ARG LEU ALA GLU ALA VAL GLY CYS PRO HIS
SEQRES 33 A 737 GLU PRO SER LYS LEU SER ASP ALA VAL GLU CYS LEU ARG
SEQRES 34 A 737 GLY LYS ASP PRO HIS VAL LEU VAL ASN ASN GLU TRP GLY
SEQRES 35 A 737 THR LEU GLY ILE CYS GLU PHE PRO PHE VAL PRO VAL VAL
SEQRES 36 A 737 ASP GLY ALA PHE LEU ASP GLU THR PRO GLN ARG SER LEU
SEQRES 37 A 737 ALA SER GLY ARG PHE LYS LYS THR GLU ILE LEU THR GLY
SEQRES 38 A 737 SER ASN THR GLU GLU GLY TYR TYR PHE ILE ILE TYR TYR
SEQRES 39 A 737 LEU THR GLU LEU LEU ARG LYS GLU GLU GLY VAL THR VAL
SEQRES 40 A 737 THR ARG GLU GLU PHE LEU GLN ALA VAL ARG GLU LEU ASN
SEQRES 41 A 737 PRO TYR VAL ASN GLY ALA ALA ARG GLN ALA ILE VAL PHE
SEQRES 42 A 737 GLU TYR THR ASP TRP THR GLU PRO ASP ASN PRO ASN SER
SEQRES 43 A 737 ASN ARG ASP ALA LEU ASP LYS MET VAL GLY ASP TYR HIS
SEQRES 44 A 737 PHE THR CYS ASN VAL ASN GLU PHE ALA GLN ARG TYR ALA
SEQRES 45 A 737 GLU GLU GLY ASN ASN VAL TYR MET TYR LEU TYR THR HIS
SEQRES 46 A 737 ARG SER LYS GLY ASN PRO TRP PRO ARG TRP THR GLY VAL
SEQRES 47 A 737 MET HIS GLY ASP GLU ILE ASN TYR VAL PHE GLY GLU PRO
SEQRES 48 A 737 LEU ASN PRO THR LEU GLY TYR THR GLU ASP GLU LYS ASP
SEQRES 49 A 737 PHE SER ARG LYS ILE MET ARG TYR TRP SER ASN PHE ALA
SEQRES 50 A 737 LYS THR GLY ASN PRO ASN PRO ASN THR ALA SER SER GLU
SEQRES 51 A 737 PHE PRO GLU TRP PRO LYS HIS THR ALA HIS GLY ARG HIS
SEQRES 52 A 737 TYR LEU GLU LEU GLY LEU ASN THR SER PHE VAL GLY ARG
SEQRES 53 A 737 GLY PRO ARG LEU ARG GLN CYS ALA PHE TRP LYS LYS TYR
SEQRES 54 A 737 LEU PRO GLN LEU VAL ALA ALA THR SER ASN LEU PRO GLY
SEQRES 55 A 737 PRO ALA PRO PRO SER GLU PRO CYS GLU SER SER ALA PHE
SEQRES 56 A 737 PHE TYR ARG PRO ASP LEU ILE VAL LEU LEU VAL SER LEU
SEQRES 57 A 737 LEU THR ALA THR VAL ARG PHE ILE GLN
SEQRES 1 B 737 MET GLU ILE ARG GLY LEU LEU MET GLY ARG LEU ARG LEU
SEQRES 2 B 737 GLY ARG ARG MET VAL PRO LEU GLY LEU LEU GLY VAL THR
SEQRES 3 B 737 ALA LEU LEU LEU ILE LEU PRO PRO PHE ALA LEU VAL GLN
SEQRES 4 B 737 GLY ARG HIS HIS GLU LEU ASN ASN GLY ALA ALA ILE GLY
SEQRES 5 B 737 SER HIS GLN LEU SER ALA ALA ALA GLY VAL GLY LEU ALA
SEQRES 6 B 737 SER GLN SER ALA GLN SER GLY SER LEU ALA SER GLY VAL
SEQRES 7 B 737 MET SER SER VAL PRO ALA ALA GLY ALA SER SER SER SER
SEQRES 8 B 737 SER SER SER LEU LEU SER SER SER ALA GLU ASP ASP VAL
SEQRES 9 B 737 ALA ARG ILE THR LEU SER LYS ASP ALA ASP ALA PHE PHE
SEQRES 10 B 737 THR PRO TYR ILE GLY HIS GLY GLU SER VAL ARG ILE ILE
SEQRES 11 B 737 ASP ALA GLU LEU GLY THR LEU GLU HIS VAL HIS SER GLY
SEQRES 12 B 737 ALA THR PRO ARG ARG ARG GLY LEU THR ARG ARG GLU SER
SEQRES 13 B 737 ASN SER ASP ALA ASN ASP ASN ASP PRO LEU VAL VAL ASN
SEQRES 14 B 737 THR ASP LYS GLY ARG ILE ARG GLY ILE THR VAL ASP ALA
SEQRES 15 B 737 PRO SER GLY LYS LYS VAL ASP VAL TRP LEU GLY ILE PRO
SEQRES 16 B 737 TYR ALA GLN PRO PRO VAL GLY PRO LEU ARG PHE ARG HIS
SEQRES 17 B 737 PRO ARG PRO ALA GLU LYS TRP THR GLY VAL LEU ASN THR
SEQRES 18 B 737 THR THR PRO PRO ASN SER CYS VAL GLN ILE VAL ASP THR
SEQRES 19 B 737 VAL PHE GLY ASP PHE PRO GLY ALA THR MET TRP ASN PRO
SEQRES 20 B 737 ASN THR PRO LEU SER GLU ASP CYS LEU TYR ILE ASN VAL
SEQRES 21 B 737 VAL ALA PRO ARG PRO ARG PRO LYS ASN ALA ALA VAL MET
SEQRES 22 B 737 LEU TRP ILE PHE GLY GLY GLY PHE TYR SER GLY THR ALA
SEQRES 23 B 737 THR LEU ASP VAL TYR ASP HIS ARG ALA LEU ALA SER GLU
SEQRES 24 B 737 GLU ASN VAL ILE VAL VAL SER LEU GLN TYR ARG VAL ALA
SEQRES 25 B 737 SER LEU GLY PHE LEU PHE LEU GLY THR PRO GLU ALA PRO
SEQRES 26 B 737 GLY ASN ALA GLY LEU PHE ASP GLN ASN LEU ALA LEU ARG
SEQRES 27 B 737 TRP VAL ARG ASP ASN ILE HIS ARG PHE GLY GLY ASP PRO
SEQRES 28 B 737 SER ARG VAL THR LEU PHE GLY GLU SEB ALA GLY ALA VAL
SEQRES 29 B 737 SER VAL SER LEU HIS LEU LEU SER ALA LEU SER ARG ASP
SEQRES 30 B 737 LEU PHE GLN ARG ALA ILE LEU GLN SER GLY SER PRO THR
SEQRES 31 B 737 ALA PRO TRP ALA LEU VAL SER ARG GLU GLU ALA THR LEU
SEQRES 32 B 737 ARG ALA LEU ARG LEU ALA GLU ALA VAL GLY CYS PRO HIS
SEQRES 33 B 737 GLU PRO SER LYS LEU SER ASP ALA VAL GLU CYS LEU ARG
SEQRES 34 B 737 GLY LYS ASP PRO HIS VAL LEU VAL ASN ASN GLU TRP GLY
SEQRES 35 B 737 THR LEU GLY ILE CYS GLU PHE PRO PHE VAL PRO VAL VAL
SEQRES 36 B 737 ASP GLY ALA PHE LEU ASP GLU THR PRO GLN ARG SER LEU
SEQRES 37 B 737 ALA SER GLY ARG PHE LYS LYS THR GLU ILE LEU THR GLY
SEQRES 38 B 737 SER ASN THR GLU GLU GLY TYR TYR PHE ILE ILE TYR TYR
SEQRES 39 B 737 LEU THR GLU LEU LEU ARG LYS GLU GLU GLY VAL THR VAL
SEQRES 40 B 737 THR ARG GLU GLU PHE LEU GLN ALA VAL ARG GLU LEU ASN
SEQRES 41 B 737 PRO TYR VAL ASN GLY ALA ALA ARG GLN ALA ILE VAL PHE
SEQRES 42 B 737 GLU TYR THR ASP TRP THR GLU PRO ASP ASN PRO ASN SER
SEQRES 43 B 737 ASN ARG ASP ALA LEU ASP LYS MET VAL GLY ASP TYR HIS
SEQRES 44 B 737 PHE THR CYS ASN VAL ASN GLU PHE ALA GLN ARG TYR ALA
SEQRES 45 B 737 GLU GLU GLY ASN ASN VAL TYR MET TYR LEU TYR THR HIS
SEQRES 46 B 737 ARG SER LYS GLY ASN PRO TRP PRO ARG TRP THR GLY VAL
SEQRES 47 B 737 MET HIS GLY ASP GLU ILE ASN TYR VAL PHE GLY GLU PRO
SEQRES 48 B 737 LEU ASN PRO THR LEU GLY TYR THR GLU ASP GLU LYS ASP
SEQRES 49 B 737 PHE SER ARG LYS ILE MET ARG TYR TRP SER ASN PHE ALA
SEQRES 50 B 737 LYS THR GLY ASN PRO ASN PRO ASN THR ALA SER SER GLU
SEQRES 51 B 737 PHE PRO GLU TRP PRO LYS HIS THR ALA HIS GLY ARG HIS
SEQRES 52 B 737 TYR LEU GLU LEU GLY LEU ASN THR SER PHE VAL GLY ARG
SEQRES 53 B 737 GLY PRO ARG LEU ARG GLN CYS ALA PHE TRP LYS LYS TYR
SEQRES 54 B 737 LEU PRO GLN LEU VAL ALA ALA THR SER ASN LEU PRO GLY
SEQRES 55 B 737 PRO ALA PRO PRO SER GLU PRO CYS GLU SER SER ALA PHE
SEQRES 56 B 737 PHE TYR ARG PRO ASP LEU ILE VAL LEU LEU VAL SER LEU
SEQRES 57 B 737 LEU THR ALA THR VAL ARG PHE ILE GLN
MODRES 5YDJ SEB A 360 SER MODIFIED RESIDUE
MODRES 5YDJ SEB B 360 SER MODIFIED RESIDUE
HET SEB A 360 16
HET SEB B 360 16
HET NAG A 801 14
HET NAG A 802 14
HET NAG A 803 14
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 SO4 A 811 5
HET SO4 A 812 5
HET SO4 A 813 5
HET SO4 A 814 5
HET SO4 A 815 5
HET SO4 A 816 5
HET CO A 817 1
HET NAG B 801 14
HET NAG B 802 14
HET NAG B 803 14
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 SO4 B 817 5
HET SO4 B 818 5
HET SO4 B 819 5
HET CO B 820 1
HETNAM SEB O-BENZYLSULFONYL-SERINE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM SO4 SULFATE ION
HETNAM CO COBALT (II) ION
FORMUL 1 SEB 2(C10 H13 N O5 S)
FORMUL 3 NAG 6(C8 H15 N O6)
FORMUL 5 SO4 29(O4 S 2-)
FORMUL 18 CO 2(CO 2+)
FORMUL 38 HOH *48(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 LEU A 288 TYR A 291 5 4
HELIX 4 AA4 ASP A 292 ASN A 301 1 10
HELIX 5 AA5 ALA A 312 LEU A 317 1 6
HELIX 6 AA6 ASN A 327 ILE A 344 1 18
HELIX 7 AA7 HIS A 345 PHE A 347 5 3
HELIX 8 AA8 SEB A 360 SER A 372 1 13
HELIX 9 AA9 SER A 397 GLY A 413 1 17
HELIX 10 AB1 LEU A 421 LYS A 431 1 11
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 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 573 1 14
HELIX 18 AB9 PRO A 593 GLY A 597 5 5
HELIX 19 AC1 ASP A 602 PHE A 608 1 7
HELIX 20 AC2 THR A 619 GLY A 640 1 22
HELIX 21 AC3 ARG A 679 LYS A 688 1 10
HELIX 22 AC4 LYS A 688 SER A 698 1 11
HELIX 23 AC5 VAL B 201 ARG B 205 5 5
HELIX 24 AC6 PHE B 239 MET B 244 1 6
HELIX 25 AC7 LEU B 288 TYR B 291 5 4
HELIX 26 AC8 ASP B 292 ASN B 301 1 10
HELIX 27 AC9 VAL B 311 LEU B 317 1 7
HELIX 28 AD1 ASN B 327 ILE B 344 1 18
HELIX 29 AD2 HIS B 345 PHE B 347 5 3
HELIX 30 AD3 SEB B 360 SER B 372 1 13
HELIX 31 AD4 SER B 397 GLY B 413 1 17
HELIX 32 AD5 LEU B 421 LYS B 431 1 11
HELIX 33 AD6 ASP B 432 ASN B 438 1 7
HELIX 34 AD7 THR B 463 SER B 470 1 8
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 GLY B 640 1 22
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 188 N VAL A 180
SHEET 3 AA211 TYR A 257 PRO A 263 -1 O ILE A 258 N ILE A 194
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 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 PHE A 318 THR A 321 0
SHEET 2 AA3 2 ALA A 324 PRO A 325 -1 O ALA A 324 N LEU A 319
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 174
SHEET 1 AA511 ILE B 178 ASP B 181 0
SHEET 2 AA511 LYS B 187 PRO B 195 -1 O VAL B 190 N ILE B 178
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 ASP B 350 N ALA B 270
SHEET 7 AA511 ALA B 382 GLN B 385 1 O GLN B 385 N GLY B 358
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 583 N SER B 482
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
SSBOND 1 CYS A 228 CYS A 255 1555 1555 2.03
SSBOND 2 CYS A 414 CYS A 427 1555 1555 2.03
SSBOND 3 CYS A 562 CYS A 683 1555 1555 2.03
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 2.03
LINK ND2 ASN A 220 C1 NAG A 801 1555 1555 1.44
LINK C GLU A 359 N SEB A 360 1555 1555 1.34
LINK C SEB A 360 N ALA A 361 1555 1555 1.34
LINK CE1 HIS A 416 CO CO A 817 1555 1555 2.16
LINK NE2 HIS A 416 CO CO A 817 1555 1555 1.82
LINK ND2 ASN A 670 C1 NAG A 803 1555 1555 1.45
LINK ND2 ASN B 220 C1 NAG B 801 1555 1555 1.45
LINK C GLU B 359 N SEB B 360 1555 1555 1.34
LINK C SEB B 360 N ALA B 361 1555 1555 1.34
LINK CE1 HIS B 416 CO CO B 820 1555 1555 2.49
LINK NE2 HIS B 416 CO CO B 820 1555 1555 1.82
LINK ND2 ASN B 670 C1 NAG B 803 1555 1555 1.45
LINK O4 NAG A 801 C1 NAG A 802 1555 1555 1.52
LINK CO CO A 817 O HOH A 916 1555 1555 1.75
LINK CO CO A 817 O HOH A 906 1555 1555 1.73
LINK O4 NAG B 801 C1 NAG B 802 1555 1555 1.45
LINK CO CO B 820 O HOH B 917 1555 1555 1.73
LINK CO CO B 820 O HOH B 916 1555 1555 1.74
CISPEP 1 ARG A 264 PRO A 265 0 0.01
CISPEP 2 GLY A 677 PRO A 678 0 1.91
CISPEP 3 ARG B 264 PRO B 265 0 2.57
CISPEP 4 GLY B 677 PRO B 678 0 5.52
SITE 1 AC1 2 ARG A 353 LYS A 638
SITE 1 AC2 1 ASN A 524
SITE 1 AC3 4 SER A 397 ARG A 398 GLU A 399 VAL A 455
SITE 1 AC4 4 THR A 658 HIS A 660 GLY A 661 HIS A 663
SITE 1 AC5 4 SER A 470 ARG A 472 HOH A 904 PRO B 203
SITE 1 AC6 5 ARG A 376 LYS A 474 LYS A 475 GLN B 198
SITE 2 AC6 5 GLU B 213
SITE 1 AC7 6 THR A 321 SER A 419 LYS A 420 LEU A 421
SITE 2 AC7 6 SER A 422 HOH A 901
SITE 1 AC8 3 THR A 536 ASP A 537 TRP A 538
SITE 1 AC9 2 ASN A 545 ARG A 594
SITE 1 AD1 5 LEU A 192 VAL A 261 TYR A 291 ASP A 292
SITE 2 AD1 5 HIS A 293
SITE 1 AD2 3 VAL A 435 ASN A 438 ASN A 439
SITE 1 AD3 2 ASN A 226 SER A 252
SITE 1 AD4 3 TRP A 441 GLY A 442 LEU A 444
SITE 1 AD5 3 HIS A 416 HOH A 906 HOH A 916
SITE 1 AD6 6 GLU A 213 ARG B 376 PHE B 473 LYS B 474
SITE 2 AD6 6 LYS B 475 HOH B 919
SITE 1 AD7 2 ARG B 353 LYS B 638
SITE 1 AD8 4 PRO A 203 SER B 470 ARG B 472 HOH B 905
SITE 1 AD9 3 SER B 397 ARG B 398 SO4 B 818
SITE 1 AE1 1 ARG B 594
SITE 1 AE2 2 ASN B 524 ARG B 528
SITE 1 AE3 3 GLU B 503 ARG B 594 HOH B 915
SITE 1 AE4 3 LYS B 187 ARG B 264 PRO B 265
SITE 1 AE5 3 ARG B 631 PRO B 644 PHE B 651
SITE 1 AE6 3 ARG B 174 THR B 216 GLY B 217
SITE 1 AE7 3 ARG B 176 VAL B 218 HOH B 901
SITE 1 AE8 5 ARG A 681 THR B 536 ASP B 537 TRP B 538
SITE 2 AE8 5 THR B 539
SITE 1 AE9 2 ARG B 174 HOH B 901
SITE 1 AF1 4 ARG A 662 GLU B 540 PRO B 541 ASP B 542
SITE 1 AF2 4 LEU B 395 VAL B 396 SER B 397 SO4 B 807
SITE 1 AF3 4 GLN A 198 ARG B 376 ARG B 472 PHE B 473
SITE 1 AF4 4 GLU B 410 HIS B 416 HOH B 916 HOH B 917
SITE 1 AF5 2 ARG A 176 ASN A 220
SITE 1 AF6 1 ASN A 670
SITE 1 AF7 3 SER A 184 ARG B 176 ASN B 220
SITE 1 AF8 1 ASN B 670
CRYST1 147.650 147.650 224.180 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 0.006773 0.003910 0.000000 0.00000
SCALE2 0.000000 0.007821 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004461 0.00000
TER 4268 ASN A 699
TER 8536 ASN B 699
MASTER 870 0 39 45 30 0 40 6 8813 2 291 114
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