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HEADER HYDROLASE 03-SEP-14 4WBH
TITLE STRUCTURE OF THE WNT DEACYLASE NOTUM - CRYSTAL FORM I APO - 2.2A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN NOTUM HOMOLOG;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 38-496;
COMPND 5 EC: 3.-.-.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: NOTUM, OK/SW-CL.30;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293T;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHLSEC
KEYWDS WNT, EXTRACELLULAR ESTERASE, ALPHA/BETA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZEBISCH,E.Y.JONES
REVDAT 1 25-FEB-15 4WBH 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. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 87.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 38158
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) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2013
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2802
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2830
REMARK 3 BIN FREE R VALUE SET COUNT : 140
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5574
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 59
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.64000
REMARK 3 B22 (A**2) : -0.70000
REMARK 3 B33 (A**2) : 0.06000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.291
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.226
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.186
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.789
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5777 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7872 ; 1.170 ; 1.943
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 697 ; 6.222 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 276 ;33.993 ;22.391
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 911 ;15.103 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;17.235 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 838 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4467 ; 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): 2794 ; 1.487 ; 3.048
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3483 ; 2.559 ; 4.556
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2981 ; 1.846 ; 3.309
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 8576 ; 5.155 ;25.385
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 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 : A 86 A 722
REMARK 3 ORIGIN FOR THE GROUP (A): 49.9997 -27.2715 -28.2823
REMARK 3 T TENSOR
REMARK 3 T11: 0.0204 T22: 0.1866
REMARK 3 T33: 0.0403 T12: 0.0182
REMARK 3 T13: -0.0253 T23: -0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 2.5871 L22: 0.3687
REMARK 3 L33: 0.2687 L12: -0.0016
REMARK 3 L13: 0.5283 L23: 0.1386
REMARK 3 S TENSOR
REMARK 3 S11: -0.0940 S12: 0.1717 S13: 0.2402
REMARK 3 S21: 0.0544 S22: 0.0898 S23: -0.0715
REMARK 3 S31: 0.0278 S32: 0.0367 S33: 0.0042
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 : B 86 B 737
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4234 -14.7081 -0.5079
REMARK 3 T TENSOR
REMARK 3 T11: 0.0258 T22: 0.2142
REMARK 3 T33: 0.0043 T12: 0.0303
REMARK 3 T13: 0.0012 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 0.8555 L22: 0.9948
REMARK 3 L33: 0.3293 L12: -0.4198
REMARK 3 L13: 0.0428 L23: -0.1688
REMARK 3 S TENSOR
REMARK 3 S11: 0.0539 S12: -0.0768 S13: -0.0458
REMARK 3 S21: -0.0105 S22: -0.0422 S23: 0.0542
REMARK 3 S31: -0.0115 S32: 0.0222 S33: -0.0117
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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4WBH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1000203471.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40214
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 67.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.60800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 32.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG3350, 100MM BISTRIS 6.0, 5%
REMARK 280 GLYCEROL, 200MM AMMONIUM SULFATE, PH 6.0, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 293K
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 36.35100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 87.71650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.35100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 87.71650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 1790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 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 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 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 VAL A 452
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 GLU B 196
REMARK 465 LYS B 197
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 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 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 199 CG CD OE1 OE2
REMARK 470 GLN A 357 CG CD OE1 NE2
REMARK 470 GLU B 134 CG CD OE1 OE2
REMARK 470 GLN B 354 CG CD OE1 NE2
REMARK 470 GLN B 357 CG CD OE1 NE2
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 NH2 ARG B 292 NH2 ARG B 292 2555 1.50
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 -140.75 61.72
REMARK 500 TYR A 129 171.86 178.38
REMARK 500 SER A 232 -113.19 54.64
REMARK 500 TYR A 274 -70.49 -61.99
REMARK 500 ASN A 348 15.65 83.09
REMARK 500 GLU A 390 154.24 74.33
REMARK 500 ILE A 391 -37.00 -154.44
REMARK 500 VAL A 434 -34.85 -134.42
REMARK 500 SER A 439 58.07 -98.90
REMARK 500 TRP B 128 -137.75 70.50
REMARK 500 TYR B 129 175.81 175.51
REMARK 500 MET B 143 43.43 -146.42
REMARK 500 SER B 232 -124.61 62.28
REMARK 500 VAL B 280 -70.02 -109.37
REMARK 500 LEU B 351 56.87 -98.88
REMARK 500 GLN B 354 -161.51 59.88
REMARK 500 GLU B 390 159.56 67.94
REMARK 500 ILE B 391 -33.37 -159.90
REMARK 500 HIS B 444 8.97 85.39
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 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 601 bound
REMARK 800 to ASN B 96
DBREF 4WBH A 38 496 UNP Q6P988 NOTUM_HUMAN 38 496
DBREF 4WBH B 38 496 UNP Q6P988 NOTUM_HUMAN 38 496
SEQADV 4WBH GLU A 35 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH THR A 36 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH GLY A 37 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH GLY A 497 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH THR A 498 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH LYS A 499 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH HIS A 500 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH HIS A 501 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH HIS A 502 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH HIS A 503 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH HIS A 504 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH HIS A 505 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH GLU B 35 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH THR B 36 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH GLY B 37 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH GLY B 497 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH THR B 498 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH LYS B 499 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH HIS B 500 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH HIS B 501 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH HIS B 502 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH HIS B 503 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH HIS B 504 UNP Q6P988 EXPRESSION TAG
SEQADV 4WBH HIS B 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
HET CL A 601 1
HET CL A 602 1
HET CL A 603 1
HET NAG B 601 14
HET CL B 602 1
HET SO4 B 603 5
HETNAM CL CHLORIDE ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM SO4 SULFATE ION
FORMUL 3 CL 4(CL 1-)
FORMUL 6 NAG C8 H15 N O6
FORMUL 8 SO4 O4 S 2-
FORMUL 9 HOH *59(H2 O)
HELIX 1 AA1 ASN A 132 MET A 143 1 12
HELIX 2 AA2 ARG A 144 SER A 148 5 5
HELIX 3 AA3 THR A 159 SER A 163 5 5
HELIX 4 AA4 MET A 203 GLY A 217 1 15
HELIX 5 AA5 ARG A 218 ALA A 223 5 6
HELIX 6 AA6 SER A 232 LEU A 252 1 21
HELIX 7 AA7 ALA A 286 ASN A 299 1 14
HELIX 8 AA8 PRO A 303 ARG A 308 1 6
HELIX 9 AA9 GLU A 314 PHE A 319 5 6
HELIX 10 AB1 PHE A 320 TYR A 325 1 6
HELIX 11 AB2 PRO A 326 LEU A 328 5 3
HELIX 12 AB3 GLU A 341 ASP A 347 1 7
HELIX 13 AB4 GLN A 357 LEU A 375 1 19
HELIX 14 AB5 ARG A 394 ASP A 399 5 6
HELIX 15 AB6 LEU A 407 LEU A 418 1 12
HELIX 16 AB7 ASN B 132 MET B 143 1 12
HELIX 17 AB8 ARG B 144 MET B 147 5 4
HELIX 18 AB9 THR B 159 SER B 163 5 5
HELIX 19 AC1 MET B 203 GLY B 217 1 15
HELIX 20 AC2 ARG B 218 ALA B 223 5 6
HELIX 21 AC3 SER B 232 LEU B 252 1 21
HELIX 22 AC4 ALA B 286 ASN B 299 1 14
HELIX 23 AC5 PRO B 303 ARG B 308 1 6
HELIX 24 AC6 GLU B 314 PHE B 319 5 6
HELIX 25 AC7 PHE B 320 TYR B 325 1 6
HELIX 26 AC8 PRO B 326 LEU B 328 5 3
HELIX 27 AC9 GLU B 341 ASP B 347 1 7
HELIX 28 AD1 GLN B 357 LEU B 375 1 19
HELIX 29 AD2 ARG B 394 ASP B 399 5 6
HELIX 30 AD3 LEU B 407 LEU B 418 1 12
SHEET 1 AA110 THR A 155 ARG A 156 0
SHEET 2 AA110 LEU A 89 LEU A 93 -1 N LEU A 89 O ARG A 156
SHEET 3 AA110 GLY A 108 LYS A 112 -1 O TYR A 109 N HIS A 92
SHEET 4 AA110 ASN A 176 ILE A 180 -1 O PHE A 179 N TYR A 110
SHEET 5 AA110 ARG A 119 LEU A 124 1 N PHE A 123 O ILE A 180
SHEET 6 AA110 VAL A 225 SER A 231 1 O LEU A 227 N TRP A 120
SHEET 7 AA110 GLN A 258 ASP A 264 1 O GLN A 258 N LEU A 226
SHEET 8 AA110 VAL A 332 VAL A 335 1 O VAL A 335 N ALA A 263
SHEET 9 AA110 SER A 381 ALA A 383 1 O PHE A 382 N VAL A 334
SHEET 10 AA110 HIS A 435 VAL A 437 1 O LEU A 436 N SER A 381
SHEET 1 AA2 2 PHE A 339 ASP A 340 0
SHEET 2 AA2 2 LEU A 387 SER A 388 1 O SER A 388 N PHE A 339
SHEET 1 AA3 2 GLN A 401 VAL A 402 0
SHEET 2 AA3 2 THR A 405 SER A 406 -1 O THR A 405 N VAL A 402
SHEET 1 AA410 THR B 155 ARG B 156 0
SHEET 2 AA410 LEU B 89 LEU B 93 -1 N LEU B 89 O ARG B 156
SHEET 3 AA410 GLY B 108 LYS B 112 -1 O TYR B 109 N HIS B 92
SHEET 4 AA410 ASN B 176 ILE B 180 -1 O PHE B 179 N TYR B 110
SHEET 5 AA410 ARG B 119 LEU B 124 1 N PHE B 123 O VAL B 178
SHEET 6 AA410 VAL B 225 SER B 231 1 O LEU B 227 N TRP B 120
SHEET 7 AA410 GLN B 258 ASP B 264 1 O ARG B 260 N LEU B 228
SHEET 8 AA410 VAL B 332 VAL B 335 1 O PHE B 333 N GLY B 261
SHEET 9 AA410 SER B 381 ALA B 383 1 O PHE B 382 N VAL B 334
SHEET 10 AA410 HIS B 435 VAL B 437 1 O LEU B 436 N ALA B 383
SHEET 1 AA5 2 PHE B 339 ASP B 340 0
SHEET 2 AA5 2 LEU B 387 SER B 388 1 O SER B 388 N PHE B 339
SHEET 1 AA6 2 GLN B 401 VAL B 402 0
SHEET 2 AA6 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 2.04
SSBOND 2 CYS A 130 CYS A 136 1555 1555 2.03
SSBOND 3 CYS A 279 CYS A 285 1555 1555 2.04
SSBOND 4 CYS A 306 CYS A 318 1555 1555 2.06
SSBOND 5 CYS A 386 CYS A 449 1555 1555 2.03
SSBOND 6 CYS A 413 CYS A 432 1555 1555 2.01
SSBOND 7 CYS A 440 CYS A 445 1555 1555 2.03
SSBOND 8 CYS B 101 CYS B 183 1555 1555 2.04
SSBOND 9 CYS B 130 CYS B 136 1555 1555 2.03
SSBOND 10 CYS B 279 CYS B 285 1555 1555 2.05
SSBOND 11 CYS B 306 CYS B 318 1555 1555 2.07
SSBOND 12 CYS B 386 CYS B 449 1555 1555 2.03
SSBOND 13 CYS B 413 CYS B 432 1555 1555 2.04
SSBOND 14 CYS B 440 CYS B 445 1555 1555 2.03
LINK ND2 ASN B 96 C1 NAG B 601 1555 1555 1.46
SITE 1 AC1 1 ARG A 409
SITE 1 AC2 1 HOH A 722
SITE 1 AC3 3 ARG A 90 HIS A 92 ARG A 218
SITE 1 AC4 1 ARG B 218
SITE 1 AC5 3 SER B 117 ARG B 119 ASN B 174
SITE 1 AC6 3 ASN B 96 GLU B 210 ARG B 213
CRYST1 72.702 175.433 60.764 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 0.013755 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005700 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016457 0.00000
TER 2784 THR A 451
TER 5593 THR B 451
MASTER 618 0 6 30 28 0 6 6 5656 2 50 74
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