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HEADER HYDROLASE 03-SEP-14 4UYZ
TITLE STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM II - 2.8A
CAVEAT 4UYZ NAG B 1452 IS PLANAR AT C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN NOTUM HOMOLOG;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RESIDUES 38-496;
COMPND 5 SYNONYM: NOTUM;
COMPND 6 EC: 3.1.1.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: GLYCOSYLATED AT N96;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: POLY ALA;
COMPND 11 CHAIN: E;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293T;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHLSEC;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 17 EXPRESSION_SYSTEM_CELL_LINE: HEK293T;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PHLSEC
KEYWDS HYDROLASE, WNT, ESTERASE, EXTRACELLULAR, ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZEBISCH,E.Y.JONES
REVDAT 1 25-FEB-15 4UYZ 0
JRNL AUTH S.KAKUGAWA,P.F.LANGTON,M.ZEBISCH,S.A.HOWELL,T.-H.CHANG,
JRNL AUTH 2 Y.LIU,T.FEIZI,G.BINEVA,N.O'REILLY,A.P.SNIJDERS,E.Y.JONES,
JRNL AUTH 3 J.-P.VINCENT
JRNL TITL NOTUM DEACYLATES WNT PROTEINS TO SUPPRESS SIGNALLING
JRNL TITL 2 ACTIVITY
JRNL REF NATURE 2015
JRNL REFN ESSN 1476-4687
JRNL DOI 10.1038/NATURE14259
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 96.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.93
REMARK 3 NUMBER OF REFLECTIONS : 37125
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) : 0.24899
REMARK 3 R VALUE (WORKING SET) : 0.24761
REMARK 3 FREE R VALUE : 0.29294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1143
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) : 2.800
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.873
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2549
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.68
REMARK 3 BIN R VALUE (WORKING SET) : 0.369
REMARK 3 BIN FREE R VALUE SET COUNT : 77
REMARK 3 BIN FREE R VALUE : 0.401
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10976
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 60.8
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.978
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.28
REMARK 3 B22 (A**2) : -3.92
REMARK 3 B33 (A**2) : 1.64
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -0.06
REMARK 3 B23 (A**2) : 0.00
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): 0.469
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.443
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 52.567
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.883
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.851
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11304 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15399 ; 1.267 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1379 ; 5.896 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 522 ;33.218 ;22.337
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1732 ;17.490 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 110 ;19.066 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1654 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8726 ; 0.005 ; 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): 5567 ; 0.916 ; 2.174
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6929 ; 1.649 ; 3.253
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5737 ; 1.135 ; 2.270
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 451
REMARK 3 ORIGIN FOR THE GROUP (A): 63.0104 -27.1863 9.2323
REMARK 3 T TENSOR
REMARK 3 T11: 0.0787 T22: 0.5262
REMARK 3 T33: 0.0422 T12: -0.0168
REMARK 3 T13: 0.0107 T23: -0.0519
REMARK 3 L TENSOR
REMARK 3 L11: 1.4455 L22: 0.5150
REMARK 3 L33: 1.9008 L12: 0.3566
REMARK 3 L13: 0.1645 L23: 0.7065
REMARK 3 S TENSOR
REMARK 3 S11: -0.1113 S12: -0.0530 S13: 0.0802
REMARK 3 S21: -0.1689 S22: 0.0477 S23: -0.0300
REMARK 3 S31: -0.1483 S32: -0.0206 S33: 0.0637
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 87 A 452
REMARK 3 ORIGIN FOR THE GROUP (A): 29.6177 -10.4429 41.7262
REMARK 3 T TENSOR
REMARK 3 T11: 0.0456 T22: 0.6676
REMARK 3 T33: 0.0697 T12: -0.0005
REMARK 3 T13: -0.0361 T23: -0.0899
REMARK 3 L TENSOR
REMARK 3 L11: 0.7177 L22: 1.2475
REMARK 3 L33: 1.5071 L12: -0.2226
REMARK 3 L13: 0.0596 L23: 0.8126
REMARK 3 S TENSOR
REMARK 3 S11: 0.0057 S12: 0.0463 S13: -0.1531
REMARK 3 S21: 0.0803 S22: -0.0915 S23: -0.0160
REMARK 3 S31: -0.1331 S32: -0.0290 S33: 0.0858
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 87 C 450
REMARK 3 ORIGIN FOR THE GROUP (A): 64.4630 38.0989 28.8750
REMARK 3 T TENSOR
REMARK 3 T11: 0.0749 T22: 0.5431
REMARK 3 T33: 0.0411 T12: 0.0669
REMARK 3 T13: -0.0274 T23: -0.0373
REMARK 3 L TENSOR
REMARK 3 L11: 1.5376 L22: 0.8592
REMARK 3 L33: 1.4980 L12: -0.1716
REMARK 3 L13: 0.4387 L23: 0.2988
REMARK 3 S TENSOR
REMARK 3 S11: -0.0977 S12: 0.0420 S13: -0.1735
REMARK 3 S21: 0.2457 S22: 0.1755 S23: -0.1132
REMARK 3 S31: 0.0105 S32: -0.0526 S33: -0.0778
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 87 D 472
REMARK 3 ORIGIN FOR THE GROUP (A): 32.2754 20.2252 -2.1352
REMARK 3 T TENSOR
REMARK 3 T11: 0.0173 T22: 0.5940
REMARK 3 T33: 0.0402 T12: 0.0289
REMARK 3 T13: 0.0039 T23: -0.0946
REMARK 3 L TENSOR
REMARK 3 L11: 0.6694 L22: 1.7276
REMARK 3 L33: 1.2005 L12: 0.2218
REMARK 3 L13: 0.4629 L23: 0.7654
REMARK 3 S TENSOR
REMARK 3 S11: -0.0259 S12: -0.0518 S13: 0.1062
REMARK 3 S21: -0.1061 S22: -0.1133 S23: 0.0093
REMARK 3 S31: 0.0270 S32: -0.0413 S33: 0.1392
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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 4UYZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-SEP-14.
REMARK 100 THE PDBE ID CODE IS EBI-61677.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JAN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.02
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38300
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.80
REMARK 200 RESOLUTION RANGE LOW (A) : 58.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.1
REMARK 200 DATA REDUNDANCY : 2.1
REMARK 200 R MERGE (I) : 0.16
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.60
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 96.94000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 GLU A 35
REMARK 465 THR A 36
REMARK 465 GLY A 37
REMARK 465 ARG A 38
REMARK 465 THR A 39
REMARK 465 GLU A 40
REMARK 465 ALA A 41
REMARK 465 ALA A 42
REMARK 465 PRO A 43
REMARK 465 ALA A 44
REMARK 465 ALA A 45
REMARK 465 GLY A 46
REMARK 465 GLN A 47
REMARK 465 PRO A 48
REMARK 465 VAL A 49
REMARK 465 GLU A 50
REMARK 465 SER A 51
REMARK 465 PHE A 52
REMARK 465 PRO A 53
REMARK 465 LEU A 54
REMARK 465 ASP A 55
REMARK 465 PHE A 56
REMARK 465 THR A 57
REMARK 465 ALA A 58
REMARK 465 VAL A 59
REMARK 465 GLU A 60
REMARK 465 GLY A 61
REMARK 465 ASN A 62
REMARK 465 MET A 63
REMARK 465 ASP A 64
REMARK 465 SER A 65
REMARK 465 PHE A 66
REMARK 465 MET A 67
REMARK 465 ALA A 68
REMARK 465 GLN A 69
REMARK 465 VAL A 70
REMARK 465 LYS A 71
REMARK 465 SER A 72
REMARK 465 LEU A 73
REMARK 465 ALA A 74
REMARK 465 GLN A 75
REMARK 465 SER A 76
REMARK 465 LEU A 77
REMARK 465 TYR A 78
REMARK 465 PRO A 79
REMARK 465 CYS A 80
REMARK 465 SER A 81
REMARK 465 ALA A 82
REMARK 465 GLN A 83
REMARK 465 GLN A 84
REMARK 465 LEU A 85
REMARK 465 ASN A 86
REMARK 465 SER A 195
REMARK 465 GLU A 196
REMARK 465 LYS A 197
REMARK 465 ASN A 198
REMARK 465 THR A 352
REMARK 465 GLY A 353
REMARK 465 GLN A 354
REMARK 465 PRO A 355
REMARK 465 HIS A 419
REMARK 465 ASP A 420
REMARK 465 SER A 421
REMARK 465 HIS A 422
REMARK 465 LYS A 423
REMARK 465 ALA A 424
REMARK 465 SER A 425
REMARK 465 LYS A 426
REMARK 465 THR A 427
REMARK 465 PRO A 428
REMARK 465 LEU A 429
REMARK 465 LYS A 430
REMARK 465 GLY A 431
REMARK 465 ARG A 453
REMARK 465 ASP A 454
REMARK 465 GLN A 455
REMARK 465 PHE A 456
REMARK 465 THR A 457
REMARK 465 GLY A 458
REMARK 465 GLN A 459
REMARK 465 GLU A 460
REMARK 465 MET A 461
REMARK 465 ASN A 462
REMARK 465 VAL A 463
REMARK 465 ALA A 464
REMARK 465 GLN A 465
REMARK 465 PHE A 466
REMARK 465 LEU A 467
REMARK 465 MET A 468
REMARK 465 HIS A 469
REMARK 465 MET A 470
REMARK 465 GLY A 471
REMARK 465 PHE A 472
REMARK 465 ASP A 473
REMARK 465 MET A 474
REMARK 465 GLN A 475
REMARK 465 THR A 476
REMARK 465 VAL A 477
REMARK 465 ALA A 478
REMARK 465 GLN A 479
REMARK 465 PRO A 480
REMARK 465 GLN A 481
REMARK 465 GLY A 482
REMARK 465 LEU A 483
REMARK 465 GLU A 484
REMARK 465 PRO A 485
REMARK 465 SER A 486
REMARK 465 GLU A 487
REMARK 465 LEU A 488
REMARK 465 LEU A 489
REMARK 465 GLY A 490
REMARK 465 MET A 491
REMARK 465 LEU A 492
REMARK 465 SER A 493
REMARK 465 ASN A 494
REMARK 465 GLY A 495
REMARK 465 SER A 496
REMARK 465 GLY A 497
REMARK 465 THR A 498
REMARK 465 LYS A 499
REMARK 465 HIS A 500
REMARK 465 HIS A 501
REMARK 465 HIS A 502
REMARK 465 HIS A 503
REMARK 465 HIS A 504
REMARK 465 HIS A 505
REMARK 465 GLU B 35
REMARK 465 THR B 36
REMARK 465 GLY B 37
REMARK 465 ARG B 38
REMARK 465 THR B 39
REMARK 465 GLU B 40
REMARK 465 ALA B 41
REMARK 465 ALA B 42
REMARK 465 PRO B 43
REMARK 465 ALA B 44
REMARK 465 ALA B 45
REMARK 465 GLY B 46
REMARK 465 GLN B 47
REMARK 465 PRO B 48
REMARK 465 VAL B 49
REMARK 465 GLU B 50
REMARK 465 SER B 51
REMARK 465 PHE B 52
REMARK 465 PRO B 53
REMARK 465 LEU B 54
REMARK 465 ASP B 55
REMARK 465 PHE B 56
REMARK 465 THR B 57
REMARK 465 ALA B 58
REMARK 465 VAL B 59
REMARK 465 GLU B 60
REMARK 465 GLY B 61
REMARK 465 ASN B 62
REMARK 465 MET B 63
REMARK 465 ASP B 64
REMARK 465 SER B 65
REMARK 465 PHE B 66
REMARK 465 MET B 67
REMARK 465 ALA B 68
REMARK 465 GLN B 69
REMARK 465 VAL B 70
REMARK 465 LYS B 71
REMARK 465 SER B 72
REMARK 465 LEU B 73
REMARK 465 ALA B 74
REMARK 465 GLN B 75
REMARK 465 SER B 76
REMARK 465 LEU B 77
REMARK 465 TYR B 78
REMARK 465 PRO B 79
REMARK 465 CYS B 80
REMARK 465 SER B 81
REMARK 465 ALA B 82
REMARK 465 GLN B 83
REMARK 465 GLN B 84
REMARK 465 LEU B 85
REMARK 465 ASN B 86
REMARK 465 SER B 193
REMARK 465 LYS B 194
REMARK 465 SER B 195
REMARK 465 GLU B 196
REMARK 465 LYS B 197
REMARK 465 ASN B 198
REMARK 465 GLU B 199
REMARK 465 HIS B 350
REMARK 465 LEU B 351
REMARK 465 THR B 352
REMARK 465 GLY B 353
REMARK 465 GLN B 354
REMARK 465 PRO B 355
REMARK 465 VAL B 356
REMARK 465 GLN B 357
REMARK 465 GLU B 358
REMARK 465 GLY B 359
REMARK 465 LEU B 360
REMARK 465 ASP B 420
REMARK 465 SER B 421
REMARK 465 HIS B 422
REMARK 465 LYS B 423
REMARK 465 ALA B 424
REMARK 465 SER B 425
REMARK 465 LYS B 426
REMARK 465 THR B 427
REMARK 465 PRO B 428
REMARK 465 LEU B 429
REMARK 465 LYS B 430
REMARK 465 GLY B 431
REMARK 465 VAL B 452
REMARK 465 ARG B 453
REMARK 465 ASP B 454
REMARK 465 GLN B 455
REMARK 465 PHE B 456
REMARK 465 THR B 457
REMARK 465 GLY B 458
REMARK 465 GLN B 459
REMARK 465 GLU B 460
REMARK 465 MET B 461
REMARK 465 ASN B 462
REMARK 465 VAL B 463
REMARK 465 ALA B 464
REMARK 465 GLN B 465
REMARK 465 PHE B 466
REMARK 465 LEU B 467
REMARK 465 MET B 468
REMARK 465 HIS B 469
REMARK 465 MET B 470
REMARK 465 GLY B 471
REMARK 465 PHE B 472
REMARK 465 ASP B 473
REMARK 465 MET B 474
REMARK 465 GLN B 475
REMARK 465 THR B 476
REMARK 465 VAL B 477
REMARK 465 ALA B 478
REMARK 465 GLN B 479
REMARK 465 PRO B 480
REMARK 465 GLN B 481
REMARK 465 GLY B 482
REMARK 465 LEU B 483
REMARK 465 GLU B 484
REMARK 465 PRO B 485
REMARK 465 SER B 486
REMARK 465 GLU B 487
REMARK 465 LEU B 488
REMARK 465 LEU B 489
REMARK 465 GLY B 490
REMARK 465 MET B 491
REMARK 465 LEU B 492
REMARK 465 SER B 493
REMARK 465 ASN B 494
REMARK 465 GLY B 495
REMARK 465 SER B 496
REMARK 465 GLY B 497
REMARK 465 THR B 498
REMARK 465 LYS B 499
REMARK 465 HIS B 500
REMARK 465 HIS B 501
REMARK 465 HIS B 502
REMARK 465 HIS B 503
REMARK 465 HIS B 504
REMARK 465 HIS B 505
REMARK 465 GLU C 35
REMARK 465 THR C 36
REMARK 465 GLY C 37
REMARK 465 ARG C 38
REMARK 465 THR C 39
REMARK 465 GLU C 40
REMARK 465 ALA C 41
REMARK 465 ALA C 42
REMARK 465 PRO C 43
REMARK 465 ALA C 44
REMARK 465 ALA C 45
REMARK 465 GLY C 46
REMARK 465 GLN C 47
REMARK 465 PRO C 48
REMARK 465 VAL C 49
REMARK 465 GLU C 50
REMARK 465 SER C 51
REMARK 465 PHE C 52
REMARK 465 PRO C 53
REMARK 465 LEU C 54
REMARK 465 ASP C 55
REMARK 465 PHE C 56
REMARK 465 THR C 57
REMARK 465 ALA C 58
REMARK 465 VAL C 59
REMARK 465 GLU C 60
REMARK 465 GLY C 61
REMARK 465 ASN C 62
REMARK 465 MET C 63
REMARK 465 ASP C 64
REMARK 465 SER C 65
REMARK 465 PHE C 66
REMARK 465 MET C 67
REMARK 465 ALA C 68
REMARK 465 GLN C 69
REMARK 465 VAL C 70
REMARK 465 LYS C 71
REMARK 465 SER C 72
REMARK 465 LEU C 73
REMARK 465 ALA C 74
REMARK 465 GLN C 75
REMARK 465 SER C 76
REMARK 465 LEU C 77
REMARK 465 TYR C 78
REMARK 465 PRO C 79
REMARK 465 CYS C 80
REMARK 465 SER C 81
REMARK 465 ALA C 82
REMARK 465 GLN C 83
REMARK 465 GLN C 84
REMARK 465 LEU C 85
REMARK 465 ASN C 86
REMARK 465 LYS C 194
REMARK 465 SER C 195
REMARK 465 GLU C 196
REMARK 465 LYS C 197
REMARK 465 ASN C 198
REMARK 465 VAL C 349
REMARK 465 HIS C 350
REMARK 465 LEU C 351
REMARK 465 THR C 352
REMARK 465 GLY C 353
REMARK 465 GLN C 354
REMARK 465 PRO C 355
REMARK 465 VAL C 356
REMARK 465 GLN C 357
REMARK 465 HIS C 419
REMARK 465 ASP C 420
REMARK 465 SER C 421
REMARK 465 HIS C 422
REMARK 465 LYS C 423
REMARK 465 ALA C 424
REMARK 465 SER C 425
REMARK 465 LYS C 426
REMARK 465 THR C 427
REMARK 465 PRO C 428
REMARK 465 LEU C 429
REMARK 465 LYS C 430
REMARK 465 GLY C 431
REMARK 465 THR C 451
REMARK 465 VAL C 452
REMARK 465 ARG C 453
REMARK 465 ASP C 454
REMARK 465 GLN C 455
REMARK 465 PHE C 456
REMARK 465 THR C 457
REMARK 465 GLY C 458
REMARK 465 GLN C 459
REMARK 465 GLU C 460
REMARK 465 MET C 461
REMARK 465 ASN C 462
REMARK 465 VAL C 463
REMARK 465 ALA C 464
REMARK 465 GLN C 465
REMARK 465 PHE C 466
REMARK 465 LEU C 467
REMARK 465 MET C 468
REMARK 465 HIS C 469
REMARK 465 MET C 470
REMARK 465 GLY C 471
REMARK 465 PHE C 472
REMARK 465 ASP C 473
REMARK 465 MET C 474
REMARK 465 GLN C 475
REMARK 465 THR C 476
REMARK 465 VAL C 477
REMARK 465 ALA C 478
REMARK 465 GLN C 479
REMARK 465 PRO C 480
REMARK 465 GLN C 481
REMARK 465 GLY C 482
REMARK 465 LEU C 483
REMARK 465 GLU C 484
REMARK 465 PRO C 485
REMARK 465 SER C 486
REMARK 465 GLU C 487
REMARK 465 LEU C 488
REMARK 465 LEU C 489
REMARK 465 GLY C 490
REMARK 465 MET C 491
REMARK 465 LEU C 492
REMARK 465 SER C 493
REMARK 465 ASN C 494
REMARK 465 GLY C 495
REMARK 465 SER C 496
REMARK 465 GLY C 497
REMARK 465 THR C 498
REMARK 465 LYS C 499
REMARK 465 HIS C 500
REMARK 465 HIS C 501
REMARK 465 HIS C 502
REMARK 465 HIS C 503
REMARK 465 HIS C 504
REMARK 465 HIS C 505
REMARK 465 GLU D 35
REMARK 465 THR D 36
REMARK 465 GLY D 37
REMARK 465 ARG D 38
REMARK 465 THR D 39
REMARK 465 GLU D 40
REMARK 465 ALA D 41
REMARK 465 ALA D 42
REMARK 465 PRO D 43
REMARK 465 ALA D 44
REMARK 465 ALA D 45
REMARK 465 GLY D 46
REMARK 465 GLN D 47
REMARK 465 PRO D 48
REMARK 465 VAL D 49
REMARK 465 GLU D 50
REMARK 465 SER D 51
REMARK 465 PHE D 52
REMARK 465 PRO D 53
REMARK 465 LEU D 54
REMARK 465 ASP D 55
REMARK 465 PHE D 56
REMARK 465 THR D 57
REMARK 465 ALA D 58
REMARK 465 VAL D 59
REMARK 465 GLU D 60
REMARK 465 GLY D 61
REMARK 465 ASN D 62
REMARK 465 MET D 63
REMARK 465 ASP D 64
REMARK 465 SER D 65
REMARK 465 PHE D 66
REMARK 465 MET D 67
REMARK 465 ALA D 68
REMARK 465 GLN D 69
REMARK 465 VAL D 70
REMARK 465 LYS D 71
REMARK 465 SER D 72
REMARK 465 LEU D 73
REMARK 465 ALA D 74
REMARK 465 GLN D 75
REMARK 465 SER D 76
REMARK 465 LEU D 77
REMARK 465 TYR D 78
REMARK 465 PRO D 79
REMARK 465 CYS D 80
REMARK 465 SER D 81
REMARK 465 ALA D 82
REMARK 465 GLN D 83
REMARK 465 GLN D 84
REMARK 465 LEU D 85
REMARK 465 ASN D 86
REMARK 465 SER D 195
REMARK 465 GLU D 196
REMARK 465 LYS D 197
REMARK 465 HIS D 419
REMARK 465 ASP D 420
REMARK 465 SER D 421
REMARK 465 HIS D 422
REMARK 465 LYS D 423
REMARK 465 ALA D 424
REMARK 465 SER D 425
REMARK 465 LYS D 426
REMARK 465 THR D 427
REMARK 465 PRO D 428
REMARK 465 LEU D 429
REMARK 465 LYS D 430
REMARK 465 GLY D 431
REMARK 465 VAL D 452
REMARK 465 ASP D 473
REMARK 465 MET D 474
REMARK 465 GLN D 475
REMARK 465 THR D 476
REMARK 465 VAL D 477
REMARK 465 ALA D 478
REMARK 465 GLN D 479
REMARK 465 PRO D 480
REMARK 465 GLN D 481
REMARK 465 GLY D 482
REMARK 465 LEU D 483
REMARK 465 GLU D 484
REMARK 465 PRO D 485
REMARK 465 SER D 486
REMARK 465 GLU D 487
REMARK 465 LEU D 488
REMARK 465 LEU D 489
REMARK 465 GLY D 490
REMARK 465 MET D 491
REMARK 465 LEU D 492
REMARK 465 SER D 493
REMARK 465 ASN D 494
REMARK 465 GLY D 495
REMARK 465 SER D 496
REMARK 465 GLY D 497
REMARK 465 THR D 498
REMARK 465 LYS D 499
REMARK 465 HIS D 500
REMARK 465 HIS D 501
REMARK 465 HIS D 502
REMARK 465 HIS D 503
REMARK 465 HIS D 504
REMARK 465 HIS D 505
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 112 CG CD CE NZ
REMARK 470 ARG A 118 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 194 CG CD CE NZ
REMARK 470 GLU A 199 CG CD OE1 OE2
REMARK 470 ASP A 281 CG OD1 OD2
REMARK 470 GLN A 309 CG CD OE1 NE2
REMARK 470 TRP A 442 CG CD1 CD2 NE1 CE2 CE3 CZ2 CZ3
REMARK 470 TRP A 442 CH2
REMARK 470 HIS A 444 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 87 CG CD OE1 OE2
REMARK 470 ASP B 88 CG OD1 OD2
REMARK 470 LYS B 112 CG CD CE NZ
REMARK 470 GLU B 210 CG CD OE1 OE2
REMARK 470 ARG B 213 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 281 CG OD1 OD2
REMARK 470 ILE B 283 CG1 CG2 CD1
REMARK 470 ARG B 305 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 361 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 362 CG CD1 CD2
REMARK 470 ARG B 394 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 415 CG OD1 OD2
REMARK 470 HIS B 419 CG ND1 CD2 CE1 NE2
REMARK 470 HIS B 444 CG ND1 CD2 CE1 NE2
REMARK 470 GLU C 87 CG CD OE1 OE2
REMARK 470 GLU C 199 CG CD OE1 OE2
REMARK 470 ASP C 270 CG OD1 OD2
REMARK 470 ASP C 281 CG OD1 OD2
REMARK 470 GLU C 358 CG CD OE1 OE2
REMARK 470 GLN C 365 CG CD OE1 NE2
REMARK 470 THR C 405 OG1 CG2
REMARK 470 HIS C 444 CG ND1 CD2 CE1 NE2
REMARK 470 ASP D 88 CG OD1 OD2
REMARK 470 ASP D 281 CG OD1 OD2
REMARK 470 GLU D 312 CG CD OE1 OE2
REMARK 470 GLN D 354 CG CD OE1 NE2
REMARK 470 ARG D 372 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 403 CG CD CE NZ
REMARK 470 LEU D 418 CG CD1 CD2
REMARK 470 TRP D 442 CG CD1 CD2 NE1 CE2 CE3 CZ2 CZ3
REMARK 470 TRP D 442 CH2
REMARK 470 THR D 451 OG1 CG2
REMARK 470 ARG D 453 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 454 CG OD1 OD2
REMARK 470 GLN D 455 CG CD OE1 NE2
REMARK 470 PHE D 456 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR D 457 OG1 CG2
REMARK 470 GLN D 459 CG CD OE1 NE2
REMARK 470 GLU D 460 CG CD OE1 OE2
REMARK 470 ASN D 462 CG OD1 ND2
REMARK 470 GLN D 465 CG CD OE1 NE2
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 OG SER A 184 OD1 ASP A 186 1.95
REMARK 500 NH1 ARG B 139 OG SER B 185 1.98
REMARK 500 OG SER B 184 OD1 ASP B 186 2.10
REMARK 500 O ASP B 186 OG SER B 189 1.95
REMARK 500 OD2 ASP B 186 N GLY B 190 2.16
REMARK 500 O LYS B 272 OH TYR B 363 1.98
REMARK 500 NH2 ARG B 416 SG CYS B 432 2.18
REMARK 500 CG ASN C 132 OD1 ASN C 135 1.91
REMARK 500 OD1 ASN C 132 OD1 ASN C 135 1.94
REMARK 500 ND2 ASN C 132 OD1 ASN C 135 1.82
REMARK 500 NH1 ARG C 139 OG SER C 185 1.37
REMARK 500 O ASP C 186 OG SER C 189 1.94
REMARK 500 OE2 GLU C 210 NE ARG C 213 2.15
REMARK 500 OE2 GLU C 210 CZ ARG C 213 2.10
REMARK 500 OE2 GLU C 210 NH2 ARG C 213 1.81
REMARK 500 ND2 ASN C 271 OD1 ASP C 347 2.14
REMARK 500 ND2 ASN C 271 OD2 ASP C 347 1.91
REMARK 500 O LYS C 272 OH TYR C 363 2.18
REMARK 500 O ASP C 281 OG1 THR C 284 2.04
REMARK 500 O ASP D 186 OG SER D 189 1.98
REMARK 500 OE2 GLU D 210 NE ARG D 213 1.77
REMARK 500 OD1 ASN D 317 NZ LYS D 323 1.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS A 130 CA - CB - SG ANGL. DEV. = -8.1 DEGREES
REMARK 500 CYS A 183 CA - CB - SG ANGL. DEV. = -9.4 DEGREES
REMARK 500 CYS C 183 CA - CB - SG ANGL. DEV. = -7.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TRP A 128 -148.36 58.56
REMARK 500 SER A 232 -125.04 63.68
REMARK 500 ALA A 385 58.33 -91.43
REMARK 500 GLU A 390 132.15 83.72
REMARK 500 ILE A 391 -33.85 -139.31
REMARK 500 VAL A 402 -77.38 -106.80
REMARK 500 LYS A 403 59.04 -103.11
REMARK 500 HIS A 435 79.29 -100.17
REMARK 500 SER A 439 68.93 -108.94
REMARK 500 PRO A 441 0.27 -67.92
REMARK 500 TRP B 128 -148.53 64.04
REMARK 500 ILE B 161 -5.17 -57.71
REMARK 500 ASN B 169 68.15 -163.26
REMARK 500 SER B 232 -128.07 59.39
REMARK 500 CYS B 318 3.70 -69.35
REMARK 500 GLU B 390 146.78 79.74
REMARK 500 ILE B 391 -49.57 -145.09
REMARK 500 ASN C 96 96.04 -68.12
REMARK 500 TRP C 128 -156.89 68.85
REMARK 500 SER C 232 -122.55 57.51
REMARK 500 GLU C 390 156.97 78.69
REMARK 500 ILE C 391 -58.29 -147.71
REMARK 500 HIS C 396 7.98 -67.84
REMARK 500 VAL C 402 -63.35 -99.40
REMARK 500 CYS C 440 87.68 -160.64
REMARK 500 PRO C 441 40.04 -71.63
REMARK 500 HIS C 444 5.75 58.76
REMARK 500 ASN D 96 80.21 -67.45
REMARK 500 TRP D 128 -157.10 65.12
REMARK 500 ALA D 191 18.94 -143.36
REMARK 500 SER D 232 -126.95 66.97
REMARK 500 LEU D 252 36.76 -75.27
REMARK 500 CYS D 318 3.35 -61.03
REMARK 500 GLU D 390 130.02 72.37
REMARK 500 ILE D 391 -46.13 -134.07
REMARK 500 VAL D 402 -70.94 -105.51
REMARK 500 LYS D 403 55.86 -111.96
REMARK 500 HIS D 435 79.83 -110.84
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 CL B1453
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B1452 BOUND TO ASN B 96
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UYU RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACETYLASE NOTUM - CRYSTAL FORM
REMARK 900 I IODIDE COMPLEX - 2.3A
REMARK 900 RELATED ID: 4UYW RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM I
REMARK 900 HEPARIN FRAGMENT COMPLEX - 1.7A
REMARK 900 RELATED ID: 4UZ1 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM
REMARK 900 III - 1.4A
REMARK 900 RELATED ID: 4UZ5 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM IV
REMARK 900 - 2.1A
REMARK 900 RELATED ID: 4UZ6 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM V
REMARK 900 - SOS COMPLEX - 1.9A
REMARK 900 RELATED ID: 4UZ7 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACETYLASE NOTUM - CRYSTAL FORM
REMARK 900 VII - SOS COMPLEX - 2.2A
REMARK 900 RELATED ID: 4UZ9 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACETYLASE NOTUM - CRYSTAL FORM
REMARK 900 VII - SOS COMPLEX - 2.2A
REMARK 900 RELATED ID: 4UZA RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM
REMARK 900 VIII - PHOSPHATE COMPLEX - 2.4A
REMARK 900 RELATED ID: 4UZJ RELATED DB: PDB
REMARK 900 STRUCTURE OF A WNT SIGNAL REGULATOR FROM DROSOPHILA -
REMARK 900 CRYSTAL FORM I - 2.4A
REMARK 900 RELATED ID: 4UZK RELATED DB: PDB
REMARK 900 STRUCTURE OF A WNT SIGNAL REGULATOR FROM DROSOPHILA -
REMARK 900 CRYSTAL FORM II - 1.9A
REMARK 900 RELATED ID: 4UZL RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM I
REMARK 900 MYRISTOLEATE COMPLEX - 2.1A
REMARK 900 RELATED ID: 4UZQ RELATED DB: PDB
REMARK 900 STRUCTURE OF A WNT SIGNAL REGULATOR COMPLEX - CRYSTAL
REMARK 900 FORM IX - 1.5A
DBREF 4UYZ A 38 496 UNP Q6P988 NOTUM_HUMAN 38 496
DBREF 4UYZ B 38 496 UNP Q6P988 NOTUM_HUMAN 38 496
DBREF 4UYZ C 38 496 UNP Q6P988 NOTUM_HUMAN 38 496
DBREF 4UYZ D 38 496 UNP Q6P988 NOTUM_HUMAN 38 496
DBREF 4UYZ E 7 16 PDB 4UYZ 4UYZ 7 16
SEQADV 4UYZ GLU A 35 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ THR A 36 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ GLY A 37 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ GLY A 497 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ THR A 498 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ LYS A 499 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS A 500 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS A 501 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS A 502 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS A 503 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS A 504 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS A 505 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ GLU B 35 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ THR B 36 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ GLY B 37 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ GLY B 497 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ THR B 498 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ LYS B 499 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS B 500 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS B 501 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS B 502 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS B 503 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS B 504 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS B 505 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ GLU C 35 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ THR C 36 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ GLY C 37 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ GLY C 497 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ THR C 498 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ LYS C 499 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS C 500 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS C 501 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS C 502 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS C 503 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS C 504 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS C 505 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ GLU D 35 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ THR D 36 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ GLY D 37 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ GLY D 497 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ THR D 498 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ LYS D 499 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS D 500 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS D 501 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS D 502 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS D 503 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS D 504 UNP Q6P988 EXPRESSION TAG
SEQADV 4UYZ HIS D 505 UNP Q6P988 EXPRESSION TAG
SEQRES 1 A 471 GLU THR GLY ARG THR GLU ALA ALA PRO ALA ALA GLY GLN
SEQRES 2 A 471 PRO VAL GLU SER PHE PRO LEU ASP PHE THR ALA VAL GLU
SEQRES 3 A 471 GLY ASN MET ASP SER PHE MET ALA GLN VAL LYS SER LEU
SEQRES 4 A 471 ALA GLN SER LEU TYR PRO CYS SER ALA GLN GLN LEU ASN
SEQRES 5 A 471 GLU ASP LEU ARG LEU HIS LEU LEU LEU ASN THR SER VAL
SEQRES 6 A 471 THR CYS ASN ASP GLY SER PRO ALA GLY TYR TYR LEU LYS
SEQRES 7 A 471 GLU SER ARG GLY SER ARG ARG TRP LEU LEU PHE LEU GLU
SEQRES 8 A 471 GLY GLY TRP TYR CYS PHE ASN ARG GLU ASN CYS ASP SER
SEQRES 9 A 471 ARG TYR ASP THR MET ARG ARG LEU MET SER SER ARG ASP
SEQRES 10 A 471 TRP PRO ARG THR ARG THR GLY THR GLY ILE LEU SER SER
SEQRES 11 A 471 GLN PRO GLU GLU ASN PRO TYR TRP TRP ASN ALA ASN MET
SEQRES 12 A 471 VAL PHE ILE PRO TYR CYS SER SER ASP VAL TRP SER GLY
SEQRES 13 A 471 ALA SER SER LYS SER GLU LYS ASN GLU TYR ALA PHE MET
SEQRES 14 A 471 GLY ALA LEU ILE ILE GLN GLU VAL VAL ARG GLU LEU LEU
SEQRES 15 A 471 GLY ARG GLY LEU SER GLY ALA LYS VAL LEU LEU LEU ALA
SEQRES 16 A 471 GLY SER SER ALA GLY GLY THR GLY VAL LEU LEU ASN VAL
SEQRES 17 A 471 ASP ARG VAL ALA GLU GLN LEU GLU LYS LEU GLY TYR PRO
SEQRES 18 A 471 ALA ILE GLN VAL ARG GLY LEU ALA ASP SER GLY TRP PHE
SEQRES 19 A 471 LEU ASP ASN LYS GLN TYR ARG HIS THR ASP CYS VAL ASP
SEQRES 20 A 471 THR ILE THR CYS ALA PRO THR GLU ALA ILE ARG ARG GLY
SEQRES 21 A 471 ILE ARG TYR TRP ASN GLY VAL VAL PRO GLU ARG CYS ARG
SEQRES 22 A 471 ARG GLN PHE GLN GLU GLY GLU GLU TRP ASN CYS PHE PHE
SEQRES 23 A 471 GLY TYR LYS VAL TYR PRO THR LEU ARG CYS PRO VAL PHE
SEQRES 24 A 471 VAL VAL GLN TRP LEU PHE ASP GLU ALA GLN LEU THR VAL
SEQRES 25 A 471 ASP ASN VAL HIS LEU THR GLY GLN PRO VAL GLN GLU GLY
SEQRES 26 A 471 LEU ARG LEU TYR ILE GLN ASN LEU GLY ARG GLU LEU ARG
SEQRES 27 A 471 HIS THR LEU LYS ASP VAL PRO ALA SER PHE ALA PRO ALA
SEQRES 28 A 471 CYS LEU SER HIS GLU ILE ILE ILE ARG SER HIS TRP THR
SEQRES 29 A 471 ASP VAL GLN VAL LYS GLY THR SER LEU PRO ARG ALA LEU
SEQRES 30 A 471 HIS CYS TRP ASP ARG SER LEU HIS ASP SER HIS LYS ALA
SEQRES 31 A 471 SER LYS THR PRO LEU LYS GLY CYS PRO VAL HIS LEU VAL
SEQRES 32 A 471 ASP SER CYS PRO TRP PRO HIS CYS ASN PRO SER CYS PRO
SEQRES 33 A 471 THR VAL ARG ASP GLN PHE THR GLY GLN GLU MET ASN VAL
SEQRES 34 A 471 ALA GLN PHE LEU MET HIS MET GLY PHE ASP MET GLN THR
SEQRES 35 A 471 VAL ALA GLN PRO GLN GLY LEU GLU PRO SER GLU LEU LEU
SEQRES 36 A 471 GLY MET LEU SER ASN GLY SER GLY THR LYS HIS HIS HIS
SEQRES 37 A 471 HIS HIS HIS
SEQRES 1 B 471 GLU THR GLY ARG THR GLU ALA ALA PRO ALA ALA GLY GLN
SEQRES 2 B 471 PRO VAL GLU SER PHE PRO LEU ASP PHE THR ALA VAL GLU
SEQRES 3 B 471 GLY ASN MET ASP SER PHE MET ALA GLN VAL LYS SER LEU
SEQRES 4 B 471 ALA GLN SER LEU TYR PRO CYS SER ALA GLN GLN LEU ASN
SEQRES 5 B 471 GLU ASP LEU ARG LEU HIS LEU LEU LEU ASN THR SER VAL
SEQRES 6 B 471 THR CYS ASN ASP GLY SER PRO ALA GLY TYR TYR LEU LYS
SEQRES 7 B 471 GLU SER ARG GLY SER ARG ARG TRP LEU LEU PHE LEU GLU
SEQRES 8 B 471 GLY GLY TRP TYR CYS PHE ASN ARG GLU ASN CYS ASP SER
SEQRES 9 B 471 ARG TYR ASP THR MET ARG ARG LEU MET SER SER ARG ASP
SEQRES 10 B 471 TRP PRO ARG THR ARG THR GLY THR GLY ILE LEU SER SER
SEQRES 11 B 471 GLN PRO GLU GLU ASN PRO TYR TRP TRP ASN ALA ASN MET
SEQRES 12 B 471 VAL PHE ILE PRO TYR CYS SER SER ASP VAL TRP SER GLY
SEQRES 13 B 471 ALA SER SER LYS SER GLU LYS ASN GLU TYR ALA PHE MET
SEQRES 14 B 471 GLY ALA LEU ILE ILE GLN GLU VAL VAL ARG GLU LEU LEU
SEQRES 15 B 471 GLY ARG GLY LEU SER GLY ALA LYS VAL LEU LEU LEU ALA
SEQRES 16 B 471 GLY SER SER ALA GLY GLY THR GLY VAL LEU LEU ASN VAL
SEQRES 17 B 471 ASP ARG VAL ALA GLU GLN LEU GLU LYS LEU GLY TYR PRO
SEQRES 18 B 471 ALA ILE GLN VAL ARG GLY LEU ALA ASP SER GLY TRP PHE
SEQRES 19 B 471 LEU ASP ASN LYS GLN TYR ARG HIS THR ASP CYS VAL ASP
SEQRES 20 B 471 THR ILE THR CYS ALA PRO THR GLU ALA ILE ARG ARG GLY
SEQRES 21 B 471 ILE ARG TYR TRP ASN GLY VAL VAL PRO GLU ARG CYS ARG
SEQRES 22 B 471 ARG GLN PHE GLN GLU GLY GLU GLU TRP ASN CYS PHE PHE
SEQRES 23 B 471 GLY TYR LYS VAL TYR PRO THR LEU ARG CYS PRO VAL PHE
SEQRES 24 B 471 VAL VAL GLN TRP LEU PHE ASP GLU ALA GLN LEU THR VAL
SEQRES 25 B 471 ASP ASN VAL HIS LEU THR GLY GLN PRO VAL GLN GLU GLY
SEQRES 26 B 471 LEU ARG LEU TYR ILE GLN ASN LEU GLY ARG GLU LEU ARG
SEQRES 27 B 471 HIS THR LEU LYS ASP VAL PRO ALA SER PHE ALA PRO ALA
SEQRES 28 B 471 CYS LEU SER HIS GLU ILE ILE ILE ARG SER HIS TRP THR
SEQRES 29 B 471 ASP VAL GLN VAL LYS GLY THR SER LEU PRO ARG ALA LEU
SEQRES 30 B 471 HIS CYS TRP ASP ARG SER LEU HIS ASP SER HIS LYS ALA
SEQRES 31 B 471 SER LYS THR PRO LEU LYS GLY CYS PRO VAL HIS LEU VAL
SEQRES 32 B 471 ASP SER CYS PRO TRP PRO HIS CYS ASN PRO SER CYS PRO
SEQRES 33 B 471 THR VAL ARG ASP GLN PHE THR GLY GLN GLU MET ASN VAL
SEQRES 34 B 471 ALA GLN PHE LEU MET HIS MET GLY PHE ASP MET GLN THR
SEQRES 35 B 471 VAL ALA GLN PRO GLN GLY LEU GLU PRO SER GLU LEU LEU
SEQRES 36 B 471 GLY MET LEU SER ASN GLY SER GLY THR LYS HIS HIS HIS
SEQRES 37 B 471 HIS HIS HIS
SEQRES 1 C 471 GLU THR GLY ARG THR GLU ALA ALA PRO ALA ALA GLY GLN
SEQRES 2 C 471 PRO VAL GLU SER PHE PRO LEU ASP PHE THR ALA VAL GLU
SEQRES 3 C 471 GLY ASN MET ASP SER PHE MET ALA GLN VAL LYS SER LEU
SEQRES 4 C 471 ALA GLN SER LEU TYR PRO CYS SER ALA GLN GLN LEU ASN
SEQRES 5 C 471 GLU ASP LEU ARG LEU HIS LEU LEU LEU ASN THR SER VAL
SEQRES 6 C 471 THR CYS ASN ASP GLY SER PRO ALA GLY TYR TYR LEU LYS
SEQRES 7 C 471 GLU SER ARG GLY SER ARG ARG TRP LEU LEU PHE LEU GLU
SEQRES 8 C 471 GLY GLY TRP TYR CYS PHE ASN ARG GLU ASN CYS ASP SER
SEQRES 9 C 471 ARG TYR ASP THR MET ARG ARG LEU MET SER SER ARG ASP
SEQRES 10 C 471 TRP PRO ARG THR ARG THR GLY THR GLY ILE LEU SER SER
SEQRES 11 C 471 GLN PRO GLU GLU ASN PRO TYR TRP TRP ASN ALA ASN MET
SEQRES 12 C 471 VAL PHE ILE PRO TYR CYS SER SER ASP VAL TRP SER GLY
SEQRES 13 C 471 ALA SER SER LYS SER GLU LYS ASN GLU TYR ALA PHE MET
SEQRES 14 C 471 GLY ALA LEU ILE ILE GLN GLU VAL VAL ARG GLU LEU LEU
SEQRES 15 C 471 GLY ARG GLY LEU SER GLY ALA LYS VAL LEU LEU LEU ALA
SEQRES 16 C 471 GLY SER SER ALA GLY GLY THR GLY VAL LEU LEU ASN VAL
SEQRES 17 C 471 ASP ARG VAL ALA GLU GLN LEU GLU LYS LEU GLY TYR PRO
SEQRES 18 C 471 ALA ILE GLN VAL ARG GLY LEU ALA ASP SER GLY TRP PHE
SEQRES 19 C 471 LEU ASP ASN LYS GLN TYR ARG HIS THR ASP CYS VAL ASP
SEQRES 20 C 471 THR ILE THR CYS ALA PRO THR GLU ALA ILE ARG ARG GLY
SEQRES 21 C 471 ILE ARG TYR TRP ASN GLY VAL VAL PRO GLU ARG CYS ARG
SEQRES 22 C 471 ARG GLN PHE GLN GLU GLY GLU GLU TRP ASN CYS PHE PHE
SEQRES 23 C 471 GLY TYR LYS VAL TYR PRO THR LEU ARG CYS PRO VAL PHE
SEQRES 24 C 471 VAL VAL GLN TRP LEU PHE ASP GLU ALA GLN LEU THR VAL
SEQRES 25 C 471 ASP ASN VAL HIS LEU THR GLY GLN PRO VAL GLN GLU GLY
SEQRES 26 C 471 LEU ARG LEU TYR ILE GLN ASN LEU GLY ARG GLU LEU ARG
SEQRES 27 C 471 HIS THR LEU LYS ASP VAL PRO ALA SER PHE ALA PRO ALA
SEQRES 28 C 471 CYS LEU SER HIS GLU ILE ILE ILE ARG SER HIS TRP THR
SEQRES 29 C 471 ASP VAL GLN VAL LYS GLY THR SER LEU PRO ARG ALA LEU
SEQRES 30 C 471 HIS CYS TRP ASP ARG SER LEU HIS ASP SER HIS LYS ALA
SEQRES 31 C 471 SER LYS THR PRO LEU LYS GLY CYS PRO VAL HIS LEU VAL
SEQRES 32 C 471 ASP SER CYS PRO TRP PRO HIS CYS ASN PRO SER CYS PRO
SEQRES 33 C 471 THR VAL ARG ASP GLN PHE THR GLY GLN GLU MET ASN VAL
SEQRES 34 C 471 ALA GLN PHE LEU MET HIS MET GLY PHE ASP MET GLN THR
SEQRES 35 C 471 VAL ALA GLN PRO GLN GLY LEU GLU PRO SER GLU LEU LEU
SEQRES 36 C 471 GLY MET LEU SER ASN GLY SER GLY THR LYS HIS HIS HIS
SEQRES 37 C 471 HIS HIS HIS
SEQRES 1 D 471 GLU THR GLY ARG THR GLU ALA ALA PRO ALA ALA GLY GLN
SEQRES 2 D 471 PRO VAL GLU SER PHE PRO LEU ASP PHE THR ALA VAL GLU
SEQRES 3 D 471 GLY ASN MET ASP SER PHE MET ALA GLN VAL LYS SER LEU
SEQRES 4 D 471 ALA GLN SER LEU TYR PRO CYS SER ALA GLN GLN LEU ASN
SEQRES 5 D 471 GLU ASP LEU ARG LEU HIS LEU LEU LEU ASN THR SER VAL
SEQRES 6 D 471 THR CYS ASN ASP GLY SER PRO ALA GLY TYR TYR LEU LYS
SEQRES 7 D 471 GLU SER ARG GLY SER ARG ARG TRP LEU LEU PHE LEU GLU
SEQRES 8 D 471 GLY GLY TRP TYR CYS PHE ASN ARG GLU ASN CYS ASP SER
SEQRES 9 D 471 ARG TYR ASP THR MET ARG ARG LEU MET SER SER ARG ASP
SEQRES 10 D 471 TRP PRO ARG THR ARG THR GLY THR GLY ILE LEU SER SER
SEQRES 11 D 471 GLN PRO GLU GLU ASN PRO TYR TRP TRP ASN ALA ASN MET
SEQRES 12 D 471 VAL PHE ILE PRO TYR CYS SER SER ASP VAL TRP SER GLY
SEQRES 13 D 471 ALA SER SER LYS SER GLU LYS ASN GLU TYR ALA PHE MET
SEQRES 14 D 471 GLY ALA LEU ILE ILE GLN GLU VAL VAL ARG GLU LEU LEU
SEQRES 15 D 471 GLY ARG GLY LEU SER GLY ALA LYS VAL LEU LEU LEU ALA
SEQRES 16 D 471 GLY SER SER ALA GLY GLY THR GLY VAL LEU LEU ASN VAL
SEQRES 17 D 471 ASP ARG VAL ALA GLU GLN LEU GLU LYS LEU GLY TYR PRO
SEQRES 18 D 471 ALA ILE GLN VAL ARG GLY LEU ALA ASP SER GLY TRP PHE
SEQRES 19 D 471 LEU ASP ASN LYS GLN TYR ARG HIS THR ASP CYS VAL ASP
SEQRES 20 D 471 THR ILE THR CYS ALA PRO THR GLU ALA ILE ARG ARG GLY
SEQRES 21 D 471 ILE ARG TYR TRP ASN GLY VAL VAL PRO GLU ARG CYS ARG
SEQRES 22 D 471 ARG GLN PHE GLN GLU GLY GLU GLU TRP ASN CYS PHE PHE
SEQRES 23 D 471 GLY TYR LYS VAL TYR PRO THR LEU ARG CYS PRO VAL PHE
SEQRES 24 D 471 VAL VAL GLN TRP LEU PHE ASP GLU ALA GLN LEU THR VAL
SEQRES 25 D 471 ASP ASN VAL HIS LEU THR GLY GLN PRO VAL GLN GLU GLY
SEQRES 26 D 471 LEU ARG LEU TYR ILE GLN ASN LEU GLY ARG GLU LEU ARG
SEQRES 27 D 471 HIS THR LEU LYS ASP VAL PRO ALA SER PHE ALA PRO ALA
SEQRES 28 D 471 CYS LEU SER HIS GLU ILE ILE ILE ARG SER HIS TRP THR
SEQRES 29 D 471 ASP VAL GLN VAL LYS GLY THR SER LEU PRO ARG ALA LEU
SEQRES 30 D 471 HIS CYS TRP ASP ARG SER LEU HIS ASP SER HIS LYS ALA
SEQRES 31 D 471 SER LYS THR PRO LEU LYS GLY CYS PRO VAL HIS LEU VAL
SEQRES 32 D 471 ASP SER CYS PRO TRP PRO HIS CYS ASN PRO SER CYS PRO
SEQRES 33 D 471 THR VAL ARG ASP GLN PHE THR GLY GLN GLU MET ASN VAL
SEQRES 34 D 471 ALA GLN PHE LEU MET HIS MET GLY PHE ASP MET GLN THR
SEQRES 35 D 471 VAL ALA GLN PRO GLN GLY LEU GLU PRO SER GLU LEU LEU
SEQRES 36 D 471 GLY MET LEU SER ASN GLY SER GLY THR LYS HIS HIS HIS
SEQRES 37 D 471 HIS HIS HIS
SEQRES 1 E 10 ALA ALA ALA ALA ALA ALA ALA ALA ALA ALA
HET NAG B1452 14
HET CL B1453 1
HETNAM CL CHLORIDE ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 6 CL CL 1-
FORMUL 7 NAG C8 H15 N O6
HELIX 1 1 ASN A 132 MET A 143 1 12
HELIX 2 2 ARG A 144 MET A 147 5 4
HELIX 3 3 THR A 159 SER A 163 5 5
HELIX 4 4 MET A 203 GLY A 217 1 15
HELIX 5 5 ARG A 218 ALA A 223 5 6
HELIX 6 6 SER A 232 GLY A 253 1 22
HELIX 7 7 ALA A 286 ASN A 299 1 14
HELIX 8 8 PRO A 303 ARG A 308 1 6
HELIX 9 9 GLU A 314 PHE A 319 5 6
HELIX 10 10 PHE A 320 TYR A 325 1 6
HELIX 11 11 PRO A 326 LEU A 328 5 3
HELIX 12 12 ASP A 340 ASP A 347 1 8
HELIX 13 13 GLN A 357 LEU A 375 1 19
HELIX 14 14 ARG A 394 ASP A 399 5 6
HELIX 15 15 SER A 406 LEU A 418 1 13
HELIX 16 16 ASN B 132 MET B 143 1 12
HELIX 17 17 ARG B 144 MET B 147 5 4
HELIX 18 18 THR B 159 SER B 163 5 5
HELIX 19 19 MET B 203 ARG B 218 1 16
HELIX 20 20 GLY B 219 ALA B 223 5 5
HELIX 21 21 SER B 232 LEU B 252 1 21
HELIX 22 22 ALA B 286 ASN B 299 1 14
HELIX 23 23 PRO B 303 PHE B 310 1 8
HELIX 24 24 GLU B 314 PHE B 319 5 6
HELIX 25 25 PHE B 320 TYR B 325 1 6
HELIX 26 26 PRO B 326 LEU B 328 5 3
HELIX 27 27 ASP B 340 ASP B 347 1 8
HELIX 28 28 ARG B 361 LEU B 375 1 15
HELIX 29 29 ARG B 394 ASP B 399 5 6
HELIX 30 30 SER B 406 HIS B 419 1 14
HELIX 31 31 ASN C 132 MET C 143 1 12
HELIX 32 32 ARG C 144 MET C 147 5 4
HELIX 33 33 THR C 159 SER C 163 5 5
HELIX 34 34 MET C 203 GLY C 217 1 15
HELIX 35 35 SER C 232 GLY C 253 1 22
HELIX 36 36 ALA C 286 ASN C 299 1 14
HELIX 37 37 PRO C 303 ARG C 308 1 6
HELIX 38 38 GLU C 314 PHE C 319 5 6
HELIX 39 39 PHE C 320 TYR C 325 1 6
HELIX 40 40 PRO C 326 LEU C 328 5 3
HELIX 41 41 ASP C 340 ASN C 348 1 9
HELIX 42 42 GLU C 358 LYS C 376 1 19
HELIX 43 43 ARG C 394 ASP C 399 5 6
HELIX 44 44 SER C 406 LEU C 418 1 13
HELIX 45 45 ASN D 132 MET D 143 1 12
HELIX 46 46 ARG D 144 MET D 147 5 4
HELIX 47 47 THR D 159 SER D 163 5 5
HELIX 48 48 MET D 203 ARG D 218 1 16
HELIX 49 49 GLY D 219 ALA D 223 5 5
HELIX 50 50 SER D 232 LEU D 252 1 21
HELIX 51 51 ALA D 286 ASN D 299 1 14
HELIX 52 52 PRO D 303 ARG D 308 1 6
HELIX 53 53 GLU D 314 PHE D 319 5 6
HELIX 54 54 PHE D 320 TYR D 325 1 6
HELIX 55 55 GLU D 341 ASP D 347 1 7
HELIX 56 56 GLN D 357 LEU D 375 1 19
HELIX 57 57 ARG D 394 VAL D 400 5 7
HELIX 58 58 SER D 406 LEU D 418 1 13
HELIX 59 59 ASN D 462 MET D 470 1 9
HELIX 60 60 ALA E 9 ALA E 16 1 8
SHEET 1 AA10 THR A 155 ARG A 156 0
SHEET 2 AA10 LEU A 89 LEU A 93 -1 O LEU A 89 N ARG A 156
SHEET 3 AA10 GLY A 108 LYS A 112 -1 O TYR A 109 N HIS A 92
SHEET 4 AA10 ASN A 176 ILE A 180 -1 O MET A 177 N LYS A 112
SHEET 5 AA10 ARG A 119 LEU A 124 1 O ARG A 119 N ASN A 176
SHEET 6 AA10 VAL A 225 SER A 231 1 O VAL A 225 N TRP A 120
SHEET 7 AA10 GLN A 258 ASP A 264 1 O GLN A 258 N LEU A 226
SHEET 8 AA10 VAL A 332 VAL A 335 1 O PHE A 333 N ALA A 263
SHEET 9 AA10 SER A 381 ALA A 383 1 N PHE A 382 O VAL A 334
SHEET 10 AA10 HIS A 435 VAL A 437 1 O LEU A 436 N ALA A 383
SHEET 1 BA10 THR B 155 THR B 157 0
SHEET 2 BA10 ASP B 88 LEU B 93 -1 O LEU B 89 N ARG B 156
SHEET 3 BA10 GLY B 108 LYS B 112 -1 O TYR B 109 N HIS B 92
SHEET 4 BA10 ASN B 176 ILE B 180 -1 O MET B 177 N LYS B 112
SHEET 5 BA10 ARG B 119 LEU B 124 1 O ARG B 119 N ASN B 176
SHEET 6 BA10 VAL B 225 SER B 231 1 O VAL B 225 N TRP B 120
SHEET 7 BA10 GLN B 258 ASP B 264 1 O GLN B 258 N LEU B 226
SHEET 8 BA10 VAL B 332 VAL B 335 1 O PHE B 333 N ALA B 263
SHEET 9 BA10 SER B 381 ALA B 383 1 N PHE B 382 O VAL B 334
SHEET 10 BA10 HIS B 435 VAL B 437 1 O LEU B 436 N ALA B 383
SHEET 1 CA10 THR C 155 ARG C 156 0
SHEET 2 CA10 LEU C 89 LEU C 93 -1 O LEU C 89 N ARG C 156
SHEET 3 CA10 GLY C 108 LYS C 112 -1 O TYR C 109 N HIS C 92
SHEET 4 CA10 ASN C 176 ILE C 180 -1 O MET C 177 N LYS C 112
SHEET 5 CA10 ARG C 119 LEU C 124 1 O ARG C 119 N ASN C 176
SHEET 6 CA10 VAL C 225 SER C 231 1 O VAL C 225 N TRP C 120
SHEET 7 CA10 GLN C 258 ASP C 264 1 O GLN C 258 N LEU C 226
SHEET 8 CA10 VAL C 332 VAL C 335 1 O PHE C 333 N ALA C 263
SHEET 9 CA10 SER C 381 ALA C 383 1 N PHE C 382 O VAL C 334
SHEET 10 CA10 HIS C 435 VAL C 437 1 O LEU C 436 N ALA C 383
SHEET 1 DA10 THR D 155 ARG D 156 0
SHEET 2 DA10 LEU D 89 LEU D 93 -1 O LEU D 89 N ARG D 156
SHEET 3 DA10 GLY D 108 LYS D 112 -1 O TYR D 109 N HIS D 92
SHEET 4 DA10 ASN D 176 ILE D 180 -1 O MET D 177 N LYS D 112
SHEET 5 DA10 ARG D 119 LEU D 124 1 O ARG D 119 N ASN D 176
SHEET 6 DA10 VAL D 225 SER D 231 1 O VAL D 225 N TRP D 120
SHEET 7 DA10 GLN D 258 ASP D 264 1 O GLN D 258 N LEU D 226
SHEET 8 DA10 VAL D 332 VAL D 335 1 O PHE D 333 N ALA D 263
SHEET 9 DA10 SER D 381 ALA D 383 1 N PHE D 382 O VAL D 334
SHEET 10 DA10 HIS D 435 VAL D 437 1 O LEU D 436 N ALA D 383
SHEET 1 DB 2 PHE D 339 ASP D 340 0
SHEET 2 DB 2 LEU D 387 SER D 388
SSBOND 1 CYS A 101 CYS A 183 1555 1555 2.05
SSBOND 2 CYS A 130 CYS A 136 1555 1555 2.04
SSBOND 3 CYS A 279 CYS A 285 1555 1555 2.03
SSBOND 4 CYS A 306 CYS A 318 1555 1555 2.04
SSBOND 5 CYS A 386 CYS A 449 1555 1555 2.04
SSBOND 6 CYS A 413 CYS A 432 1555 1555 2.02
SSBOND 7 CYS A 440 CYS A 445 1555 1555 2.04
SSBOND 8 CYS B 101 CYS B 183 1555 1555 2.06
SSBOND 9 CYS B 130 CYS B 136 1555 1555 2.04
SSBOND 10 CYS B 279 CYS B 285 1555 1555 2.03
SSBOND 11 CYS B 306 CYS B 318 1555 1555 2.05
SSBOND 12 CYS B 386 CYS B 449 1555 1555 2.03
SSBOND 13 CYS B 413 CYS B 432 1555 1555 2.03
SSBOND 14 CYS B 440 CYS B 445 1555 1555 2.03
SSBOND 15 CYS C 101 CYS C 183 1555 1555 2.03
SSBOND 16 CYS C 130 CYS C 136 1555 1555 2.02
SSBOND 17 CYS C 279 CYS C 285 1555 1555 2.02
SSBOND 18 CYS C 306 CYS C 318 1555 1555 2.07
SSBOND 19 CYS C 386 CYS C 449 1555 1555 2.03
SSBOND 20 CYS C 413 CYS C 432 1555 1555 2.02
SSBOND 21 CYS C 440 CYS C 445 1555 1555 2.03
SSBOND 22 CYS D 101 CYS D 183 1555 1555 2.04
SSBOND 23 CYS D 130 CYS D 136 1555 1555 2.05
SSBOND 24 CYS D 279 CYS D 285 1555 1555 2.03
SSBOND 25 CYS D 306 CYS D 318 1555 1555 2.05
SSBOND 26 CYS D 386 CYS D 449 1555 1555 2.02
SSBOND 27 CYS D 413 CYS D 432 1555 1555 2.03
LINK ND2 ASN B 96 C1 NAG B1452 1555 1555 1.46
SITE 1 AC1 1 ARG B 416
SITE 1 AC2 1 ASN B 96
CRYST1 60.829 193.880 75.717 90.00 91.88 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.016440 0.000000 0.000540 0.00000
SCALE2 0.000000 0.005158 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013214 0.00000
MTRIX1 1 -1.000000 -0.003000 -0.015000 92.84500 1
MTRIX2 1 0.011000 0.586000 -0.810000 11.69000 1
MTRIX3 1 0.011000 -0.810000 -0.586000 24.68700 1
MTRIX1 2 -0.998000 0.045000 -0.043000 93.58000 1
MTRIX2 2 -0.061000 -0.587000 0.808000 -7.96800 1
MTRIX3 2 0.011000 0.809000 0.588000 -6.55000 1
MTRIX1 3 0.996000 0.061000 -0.058000 -3.82300 1
MTRIX2 3 0.061000 -0.998000 0.010000 8.51800 1
MTRIX3 3 -0.057000 -0.013000 -0.998000 40.67400 1
TER 2731 VAL A 452
TER 5364 THR B 451
TER 8041 PRO C 450
TER 10930 PHE D 472
TER 10981 ALA E 16
MASTER 1046 0 2 60 42 0 2 1510991 5 69 149
END |