| content |
HEADER HYDROLASE 05-SEP-14 4UZL
TITLE STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM I MYRISTOLEATE
TITLE 2 COMPLEX - 2.1A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN NOTUM HOMOLOG;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 81-451;
COMPND 5 SYNONYM: NOTUM;
COMPND 6 EC: 3.1.1.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 OTHER_DETAILS: GLYCOSYLATED AT N96
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
KEYWDS HYDROLASE, WNT, ESTERASE, EXTRACELLULAR, ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZEBISCH,E.Y.JONES
REVDAT 1 25-FEB-15 4UZL 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. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 85.36
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.86
REMARK 3 NUMBER OF REFLECTIONS : 44863
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) : 0.21453
REMARK 3 R VALUE (WORKING SET) : 0.21358
REMARK 3 FREE R VALUE : 0.25332
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.4
REMARK 3 FREE R VALUE TEST SET COUNT : 1115
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) : 2.100
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.155
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3294
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.35
REMARK 3 BIN R VALUE (WORKING SET) : 0.334
REMARK 3 BIN FREE R VALUE SET COUNT : 75
REMARK 3 BIN FREE R VALUE : 0.372
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5535
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 45
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.6
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.249
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.48
REMARK 3 B22 (A**2) : 1.10
REMARK 3 B33 (A**2) : -0.63
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.228
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.191
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.194
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.499
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5751 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5314 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7829 ; 1.358 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12165 ; 0.800 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 689 ; 6.527 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 279 ;35.142 ;22.294
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 902 ;14.639 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 60 ;17.307 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 825 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6499 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1455 ; 0.001 ; 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): 2744 ; 1.895 ; 2.978
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2743 ; 1.896 ; 2.977
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3419 ; 3.088 ; 4.449
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3007 ; 2.169 ; 3.351
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 : 2
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 86 B 1452
REMARK 3 ORIGIN FOR THE GROUP (A): 15.1291 -18.2581 -0.6408
REMARK 3 T TENSOR
REMARK 3 T11: 0.3148 T22: 0.3713
REMARK 3 T33: 0.0661 T12: 0.0278
REMARK 3 T13: 0.0052 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 1.4394 L22: 0.9883
REMARK 3 L33: 1.0273 L12: -0.8266
REMARK 3 L13: 0.4681 L23: -0.0433
REMARK 3 S TENSOR
REMARK 3 S11: -0.1212 S12: 0.0466 S13: 0.0504
REMARK 3 S21: 0.1255 S22: -0.0000 S23: 0.1498
REMARK 3 S31: 0.1236 S32: 0.1342 S33: 0.1212
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 86 A 451
REMARK 3 ORIGIN FOR THE GROUP (A): 50.6213 -26.3547 -29.8339
REMARK 3 T TENSOR
REMARK 3 T11: 0.2053 T22: 0.5502
REMARK 3 T33: 0.2402 T12: -0.0405
REMARK 3 T13: 0.0632 T23: -0.1242
REMARK 3 L TENSOR
REMARK 3 L11: 1.8548 L22: 1.6044
REMARK 3 L33: 4.4910 L12: 0.6691
REMARK 3 L13: 0.3134 L23: 2.5312
REMARK 3 S TENSOR
REMARK 3 S11: 0.3707 S12: 0.1667 S13: -0.2960
REMARK 3 S21: -0.1531 S22: 0.5879 S23: -0.5847
REMARK 3 S31: -0.4827 S32: 0.7456 S33: -0.9586
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 4UZL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-SEP-14.
REMARK 100 THE PDBE ID CODE IS EBI-61707.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL (PILATUS)
REMARK 200 DETECTOR MANUFACTURER : DECTRIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46049
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.10
REMARK 200 RESOLUTION RANGE LOW (A) : 74.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 7.2
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.70
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 (%): 45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 %W/V POLYETHYLENE GLYCOL
REMARK 280 6000, 0.1 M CITRATE PH 5.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 37.06150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 85.36150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.06150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 85.36150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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 78
REMARK 465 THR A 79
REMARK 465 GLY 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 LYS A 194
REMARK 465 SER A 195
REMARK 465 GLU A 196
REMARK 465 LYS A 197
REMARK 465 ASN A 198
REMARK 465 GLU A 199
REMARK 465 THR A 352
REMARK 465 GLY A 353
REMARK 465 GLN A 354
REMARK 465 PRO A 355
REMARK 465 VAL A 356
REMARK 465 GLN A 357
REMARK 465 GLU A 358
REMARK 465 GLY A 359
REMARK 465 LEU A 360
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 GLY A 452
REMARK 465 THR A 453
REMARK 465 HIS A 454
REMARK 465 HIS A 455
REMARK 465 HIS A 456
REMARK 465 HIS A 457
REMARK 465 HIS A 458
REMARK 465 HIS A 459
REMARK 465 HIS A 460
REMARK 465 HIS A 461
REMARK 465 HIS A 462
REMARK 465 HIS A 463
REMARK 465 GLU B 78
REMARK 465 THR B 79
REMARK 465 GLY 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 LYS B 197
REMARK 465 ASN B 198
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 HIS B 419
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 GLY B 452
REMARK 465 THR B 453
REMARK 465 HIS B 454
REMARK 465 HIS B 455
REMARK 465 HIS B 456
REMARK 465 HIS B 457
REMARK 465 HIS B 458
REMARK 465 HIS B 459
REMARK 465 HIS B 460
REMARK 465 HIS B 461
REMARK 465 HIS B 462
REMARK 465 HIS B 463
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 GLU A 87 CG CD OE1 OE2
REMARK 470 ARG A 372 NE CZ NH1 NH2
REMARK 470 LYS B 194 CD CE NZ
REMARK 470 GLU B 196 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU A 167 OG SER B 406 1554 2.10
REMARK 500 OD1 ASP A 278 NH1 ARG B 296 1655 2.15
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 ARG A 115 116.11 -39.45
REMARK 500 TRP A 128 -134.22 57.10
REMARK 500 TYR A 129 169.05 174.17
REMARK 500 SER A 185 26.71 44.12
REMARK 500 ALA A 232 -124.41 65.52
REMARK 500 VAL A 280 -75.64 -113.15
REMARK 500 GLN A 309 31.39 -88.72
REMARK 500 ASN A 348 55.94 71.81
REMARK 500 ALA A 383 75.90 -120.00
REMARK 500 HIS A 389 116.97 -160.53
REMARK 500 GLU A 390 155.30 73.05
REMARK 500 ILE A 391 -34.59 -161.20
REMARK 500 TRP B 128 -140.91 64.56
REMARK 500 MET B 143 50.74 -142.14
REMARK 500 ALA B 232 -126.72 60.43
REMARK 500 PHE B 339 75.57 -119.98
REMARK 500 GLU B 390 160.99 71.96
REMARK 500 ILE B 391 -38.72 -168.50
REMARK 500 HIS B 444 50.81 39.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 MYRISTOLEIC ACID (MRO): Z-TETRADEC-9-ENOIC ACID
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYZ B1453
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYZ A1452
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
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 DEACYLASE NOTUM - CRYSTAL FORM I
REMARK 900 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: 4UYZ RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM II
REMARK 900 - 2.8A
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 DEACYLASE 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 THE WNT DEACYLASE NOTUM - CRYSTAL FORM
REMARK 900 III - 1.4A
REMARK 900 RELATED ID: 4UZK RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE NOTUM FROM DROSOPHILA -
REMARK 900 CRYSTAL FORM II - 1.9A
REMARK 900 RELATED ID: 4UZQ RELATED DB: PDB
REMARK 900 STRUCTURE OF THE WNT DEACYLASE NOTUM IN COMPLEX WITH
REMARK 900 O-PALMITOLEOYL SERINE - CRYSTAL FORM IX - 1.5A
DBREF 4UZL A 81 451 UNP Q6P988 NOTUM_HUMAN 81 451
DBREF 4UZL B 81 451 UNP Q6P988 NOTUM_HUMAN 81 451
SEQADV 4UZL GLU A 78 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL THR A 79 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL GLY A 80 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL GLY A 452 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL THR A 453 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL HIS A 454 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL HIS A 455 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL HIS A 456 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL HIS A 457 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL HIS A 458 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL HIS A 459 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL HIS A 460 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL HIS A 461 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL HIS A 462 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL HIS A 463 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL ALA A 232 UNP Q6P988 SER 232 ENGINEERED MUTATION
SEQADV 4UZL SER A 330 UNP Q6P988 CYS 330 ENGINEERED MUTATION
SEQADV 4UZL GLU B 78 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL THR B 79 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL GLY B 80 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL GLY B 452 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL THR B 453 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL HIS B 454 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL HIS B 455 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL HIS B 456 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL HIS B 457 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL HIS B 458 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL HIS B 459 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL HIS B 460 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL HIS B 461 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL HIS B 462 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL HIS B 463 UNP Q6P988 EXPRESSION TAG
SEQADV 4UZL ALA B 232 UNP Q6P988 SER 232 ENGINEERED MUTATION
SEQADV 4UZL SER B 330 UNP Q6P988 CYS 330 ENGINEERED MUTATION
SEQRES 1 A 386 GLU THR GLY SER ALA GLN GLN LEU ASN GLU ASP LEU ARG
SEQRES 2 A 386 LEU HIS LEU LEU LEU ASN THR SER VAL THR CYS ASN ASP
SEQRES 3 A 386 GLY SER PRO ALA GLY TYR TYR LEU LYS GLU SER ARG GLY
SEQRES 4 A 386 SER ARG ARG TRP LEU LEU PHE LEU GLU GLY GLY TRP TYR
SEQRES 5 A 386 CYS PHE ASN ARG GLU ASN CYS ASP SER ARG TYR ASP THR
SEQRES 6 A 386 MET ARG ARG LEU MET SER SER ARG ASP TRP PRO ARG THR
SEQRES 7 A 386 ARG THR GLY THR GLY ILE LEU SER SER GLN PRO GLU GLU
SEQRES 8 A 386 ASN PRO TYR TRP TRP ASN ALA ASN MET VAL PHE ILE PRO
SEQRES 9 A 386 TYR CYS SER SER ASP VAL TRP SER GLY ALA SER SER LYS
SEQRES 10 A 386 SER GLU LYS ASN GLU TYR ALA PHE MET GLY ALA LEU ILE
SEQRES 11 A 386 ILE GLN GLU VAL VAL ARG GLU LEU LEU GLY ARG GLY LEU
SEQRES 12 A 386 SER GLY ALA LYS VAL LEU LEU LEU ALA GLY SER ALA ALA
SEQRES 13 A 386 GLY GLY THR GLY VAL LEU LEU ASN VAL ASP ARG VAL ALA
SEQRES 14 A 386 GLU GLN LEU GLU LYS LEU GLY TYR PRO ALA ILE GLN VAL
SEQRES 15 A 386 ARG GLY LEU ALA ASP SER GLY TRP PHE LEU ASP ASN LYS
SEQRES 16 A 386 GLN TYR ARG HIS THR ASP CYS VAL ASP THR ILE THR CYS
SEQRES 17 A 386 ALA PRO THR GLU ALA ILE ARG ARG GLY ILE ARG TYR TRP
SEQRES 18 A 386 ASN GLY VAL VAL PRO GLU ARG CYS ARG ARG GLN PHE GLN
SEQRES 19 A 386 GLU GLY GLU GLU TRP ASN CYS PHE PHE GLY TYR LYS VAL
SEQRES 20 A 386 TYR PRO THR LEU ARG SER PRO VAL PHE VAL VAL GLN TRP
SEQRES 21 A 386 LEU PHE ASP GLU ALA GLN LEU THR VAL ASP ASN VAL HIS
SEQRES 22 A 386 LEU THR GLY GLN PRO VAL GLN GLU GLY LEU ARG LEU TYR
SEQRES 23 A 386 ILE GLN ASN LEU GLY ARG GLU LEU ARG HIS THR LEU LYS
SEQRES 24 A 386 ASP VAL PRO ALA SER PHE ALA PRO ALA CYS LEU SER HIS
SEQRES 25 A 386 GLU ILE ILE ILE ARG SER HIS TRP THR ASP VAL GLN VAL
SEQRES 26 A 386 LYS GLY THR SER LEU PRO ARG ALA LEU HIS CYS TRP ASP
SEQRES 27 A 386 ARG SER LEU HIS ASP SER HIS LYS ALA SER LYS THR PRO
SEQRES 28 A 386 LEU LYS GLY CYS PRO VAL HIS LEU VAL ASP SER CYS PRO
SEQRES 29 A 386 TRP PRO HIS CYS ASN PRO SER CYS PRO THR GLY THR HIS
SEQRES 30 A 386 HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 386 GLU THR GLY SER ALA GLN GLN LEU ASN GLU ASP LEU ARG
SEQRES 2 B 386 LEU HIS LEU LEU LEU ASN THR SER VAL THR CYS ASN ASP
SEQRES 3 B 386 GLY SER PRO ALA GLY TYR TYR LEU LYS GLU SER ARG GLY
SEQRES 4 B 386 SER ARG ARG TRP LEU LEU PHE LEU GLU GLY GLY TRP TYR
SEQRES 5 B 386 CYS PHE ASN ARG GLU ASN CYS ASP SER ARG TYR ASP THR
SEQRES 6 B 386 MET ARG ARG LEU MET SER SER ARG ASP TRP PRO ARG THR
SEQRES 7 B 386 ARG THR GLY THR GLY ILE LEU SER SER GLN PRO GLU GLU
SEQRES 8 B 386 ASN PRO TYR TRP TRP ASN ALA ASN MET VAL PHE ILE PRO
SEQRES 9 B 386 TYR CYS SER SER ASP VAL TRP SER GLY ALA SER SER LYS
SEQRES 10 B 386 SER GLU LYS ASN GLU TYR ALA PHE MET GLY ALA LEU ILE
SEQRES 11 B 386 ILE GLN GLU VAL VAL ARG GLU LEU LEU GLY ARG GLY LEU
SEQRES 12 B 386 SER GLY ALA LYS VAL LEU LEU LEU ALA GLY SER ALA ALA
SEQRES 13 B 386 GLY GLY THR GLY VAL LEU LEU ASN VAL ASP ARG VAL ALA
SEQRES 14 B 386 GLU GLN LEU GLU LYS LEU GLY TYR PRO ALA ILE GLN VAL
SEQRES 15 B 386 ARG GLY LEU ALA ASP SER GLY TRP PHE LEU ASP ASN LYS
SEQRES 16 B 386 GLN TYR ARG HIS THR ASP CYS VAL ASP THR ILE THR CYS
SEQRES 17 B 386 ALA PRO THR GLU ALA ILE ARG ARG GLY ILE ARG TYR TRP
SEQRES 18 B 386 ASN GLY VAL VAL PRO GLU ARG CYS ARG ARG GLN PHE GLN
SEQRES 19 B 386 GLU GLY GLU GLU TRP ASN CYS PHE PHE GLY TYR LYS VAL
SEQRES 20 B 386 TYR PRO THR LEU ARG SER PRO VAL PHE VAL VAL GLN TRP
SEQRES 21 B 386 LEU PHE ASP GLU ALA GLN LEU THR VAL ASP ASN VAL HIS
SEQRES 22 B 386 LEU THR GLY GLN PRO VAL GLN GLU GLY LEU ARG LEU TYR
SEQRES 23 B 386 ILE GLN ASN LEU GLY ARG GLU LEU ARG HIS THR LEU LYS
SEQRES 24 B 386 ASP VAL PRO ALA SER PHE ALA PRO ALA CYS LEU SER HIS
SEQRES 25 B 386 GLU ILE ILE ILE ARG SER HIS TRP THR ASP VAL GLN VAL
SEQRES 26 B 386 LYS GLY THR SER LEU PRO ARG ALA LEU HIS CYS TRP ASP
SEQRES 27 B 386 ARG SER LEU HIS ASP SER HIS LYS ALA SER LYS THR PRO
SEQRES 28 B 386 LEU LYS GLY CYS PRO VAL HIS LEU VAL ASP SER CYS PRO
SEQRES 29 B 386 TRP PRO HIS CYS ASN PRO SER CYS PRO THR GLY THR HIS
SEQRES 30 B 386 HIS HIS HIS HIS HIS HIS HIS HIS HIS
HET NAG B1452 14
HET MYZ B1453 16
HET MYZ A1452 16
HETNAM MYZ MYRISTOLEIC ACID
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN MYZ Z-TETRADEC-9-ENOIC ACID
FORMUL 3 MYZ 2(C14 H26 O2)
FORMUL 4 NAG C8 H15 N O6
FORMUL 5 HOH *45(H2 O)
HELIX 1 1 ASN A 132 MET A 143 1 12
HELIX 2 2 ARG A 144 SER A 148 5 5
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 ALA A 232 LEU A 252 1 21
HELIX 6 6 ALA A 286 TRP A 298 1 13
HELIX 7 7 PRO A 303 ARG A 308 1 6
HELIX 8 8 GLU A 314 PHE A 319 5 6
HELIX 9 9 PHE A 320 TYR A 325 1 6
HELIX 10 10 PRO A 326 LEU A 328 5 3
HELIX 11 11 GLU A 341 ASP A 347 1 7
HELIX 12 12 ARG A 361 LEU A 375 1 15
HELIX 13 13 ARG A 394 ASP A 399 5 6
HELIX 14 14 LEU A 407 SER A 417 1 11
HELIX 15 15 ASN B 132 MET B 143 1 12
HELIX 16 16 ARG B 144 SER B 148 5 5
HELIX 17 17 THR B 159 SER B 163 5 5
HELIX 18 18 MET B 203 GLY B 217 1 15
HELIX 19 19 ARG B 218 ALA B 223 5 6
HELIX 20 20 ALA B 232 GLY B 253 1 22
HELIX 21 21 ALA B 286 ASN B 299 1 14
HELIX 22 22 PRO B 303 ARG B 308 1 6
HELIX 23 23 GLU B 314 PHE B 319 5 6
HELIX 24 24 PHE B 320 TYR B 325 1 6
HELIX 25 25 PRO B 326 LEU B 328 5 3
HELIX 26 26 GLU B 341 ASP B 347 1 7
HELIX 27 27 GLN B 357 LEU B 375 1 19
HELIX 28 28 ARG B 394 ASP B 399 5 6
HELIX 29 29 LEU B 407 LEU B 418 1 12
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 AB 2 PHE A 339 ASP A 340 0
SHEET 2 AB 2 LEU A 387 SER A 388 1 N SER A 388 O PHE A 339
SHEET 1 AC 2 GLN A 401 VAL A 402 0
SHEET 2 AC 2 THR A 405 SER A 406 -1 O THR A 405 N VAL A 402
SHEET 1 BA10 THR B 155 ARG B 156 0
SHEET 2 BA10 LEU B 89 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 BB 2 PHE B 339 ASP B 340 0
SHEET 2 BB 2 LEU B 387 SER B 388 1 N SER B 388 O PHE B 339
SHEET 1 BC 2 GLN B 401 VAL B 402 0
SHEET 2 BC 2 THR B 405 SER B 406 -1 O THR B 405 N VAL B 402
SSBOND 1 CYS A 101 CYS A 183 1555 1555 2.06
SSBOND 2 CYS A 130 CYS A 136 1555 1555 2.04
SSBOND 3 CYS A 279 CYS A 285 1555 1555 2.05
SSBOND 4 CYS A 306 CYS A 318 1555 1555 2.07
SSBOND 5 CYS A 386 CYS A 449 1555 1555 2.02
SSBOND 6 CYS A 413 CYS A 432 1555 1555 2.05
SSBOND 7 CYS A 440 CYS A 445 1555 1555 2.03
SSBOND 8 CYS B 101 CYS B 183 1555 1555 2.10
SSBOND 9 CYS B 130 CYS B 136 1555 1555 2.02
SSBOND 10 CYS B 279 CYS B 285 1555 1555 2.08
SSBOND 11 CYS B 306 CYS B 318 1555 1555 2.12
SSBOND 12 CYS B 386 CYS B 449 1555 1555 2.03
SSBOND 13 CYS B 413 CYS B 432 1555 1555 2.05
SSBOND 14 CYS B 440 CYS B 445 1555 1555 2.05
LINK ND2 ASN B 96 C1 NAG B1452 1555 1555 1.45
SITE 1 AC1 11 GLY B 127 TRP B 128 TYR B 129 ALA B 232
SITE 2 AC1 11 ALA B 233 THR B 236 PHE B 268 ILE B 291
SITE 3 AC1 11 VAL B 346 HIS B 389 HOH B2005
SITE 1 AC2 8 GLY A 127 TRP A 128 ALA A 232 ALA A 233
SITE 2 AC2 8 THR A 236 PHE A 268 ILE A 291 HIS A 389
SITE 1 AC3 4 GLN A 258 ASN B 96 VAL B 99 ARG B 213
CRYST1 74.123 170.723 61.568 90.00 90.00 90.00 P 21 21 2 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 0.013491 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005857 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016242 0.00000
MTRIX1 1 -0.902000 0.432000 0.019000 72.37300 1
MTRIX2 1 0.432000 0.902000 -0.007000 -16.19700 1
MTRIX3 1 -0.020000 0.001000 -1.000000 -29.89100 1
TER 2755 THR A 451
TER 5537 THR B 451
MASTER 491 0 3 29 28 0 6 9 5626 2 75 60
END |