HEADER STRUCTURAL PROTEIN 07-JUN-16 5L8E
TITLE STRUCTURE OF UAF1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: WD REPEAT-CONTAINING PROTEIN 48;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: USP1-ASSOCIATED FACTOR 1,WD REPEAT ENDOSOMAL PROTEIN,P80;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: UNKNOWN;
COMPND 8 CHAIN: C;
COMPND 9 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: WDR48, KIAA1449, UAF1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 14 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS WDR48 ACTIVATES USP1/12/46 B PROPELLAR, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.DHARADHAR,T.SIXMA
REVDAT 3 10-JAN-24 5L8E 1 REMARK
REVDAT 2 30-NOV-16 5L8E 1 JRNL
REVDAT 1 28-SEP-16 5L8E 0
JRNL AUTH S.DHARADHAR,M.CLERICI,W.J.VAN DIJK,A.FISH,T.K.SIXMA
JRNL TITL A CONSERVED TWO-STEP BINDING FOR THE UAF1 REGULATOR TO THE
JRNL TITL 2 USP12 DEUBIQUITINATING ENZYME.
JRNL REF J.STRUCT.BIOL. V. 196 437 2016
JRNL REFN ESSN 1095-8657
JRNL PMID 27650958
JRNL DOI 10.1016/J.JSB.2016.09.011
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0151
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 61324
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3201
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4316
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.41
REMARK 3 BIN R VALUE (WORKING SET) : 0.3090
REMARK 3 BIN FREE R VALUE SET COUNT : 226
REMARK 3 BIN FREE R VALUE : 0.3150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8169
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 84
REMARK 3 SOLVENT ATOMS : 310
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.67000
REMARK 3 B22 (A**2) : -2.38000
REMARK 3 B33 (A**2) : -0.29000
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): 0.245
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.196
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.163
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.240
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8427 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8120 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11409 ; 1.235 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18667 ; 0.849 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1036 ; 6.421 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 368 ;36.237 ;24.076
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1462 ;12.596 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 56 ;14.613 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1305 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9393 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1911 ; 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): 4156 ; 2.478 ; 5.717
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4155 ; 2.478 ; 5.716
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5185 ; 4.169 ; 8.554
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5186 ; 4.169 ; 8.555
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4271 ; 2.294 ; 5.982
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4272 ; 2.293 ; 5.982
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6224 ; 3.816 ; 8.849
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 9029 ; 6.256 ;64.355
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 9030 ; 6.256 ;64.361
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 : C 25 C 360
REMARK 3 ORIGIN FOR THE GROUP (A): 35.2232 10.2147 71.4706
REMARK 3 T TENSOR
REMARK 3 T11: 0.2351 T22: 0.2556
REMARK 3 T33: 0.2856 T12: 0.1529
REMARK 3 T13: -0.1901 T23: -0.1781
REMARK 3 L TENSOR
REMARK 3 L11: 2.9668 L22: 5.0801
REMARK 3 L33: 6.7291 L12: 3.8591
REMARK 3 L13: -4.4599 L23: -5.8395
REMARK 3 S TENSOR
REMARK 3 S11: -0.1824 S12: -0.2333 S13: -0.3085
REMARK 3 S21: -0.3233 S22: -0.2695 S23: -0.3640
REMARK 3 S31: 0.3338 S32: 0.3335 S33: 0.4519
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 12 C 24
REMARK 3 RESIDUE RANGE : C 361 C 560
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0000 0.0000 0.0000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0162 T22: 0.0162
REMARK 3 T33: 0.0162 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: -0.0000
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 : D 25 D 360
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0000 0.0000 0.0000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0162 T22: 0.0162
REMARK 3 T33: 0.0162 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: -0.0000
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 12 D 24
REMARK 3 RESIDUE RANGE : D 361 D 560
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0000 0.0000 0.0000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0162 T22: 0.0162
REMARK 3 T33: 0.0162 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: -0.0000
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.10
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5L8E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1200000320.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91997
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64580
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 49.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 1.00000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1VYH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 200MM TRI-SODIUM CITRATE,
REMARK 280 BIS-TRIS PROPANE CRYO -30% GLYCEROL, PH 6.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
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,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.80050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.33600
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.80050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 74.33600
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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 TRP A 1
REMARK 465 SER A 2
REMARK 465 HIS A 3
REMARK 465 PRO A 4
REMARK 465 GLN A 5
REMARK 465 PHE A 6
REMARK 465 GLU A 7
REMARK 465 LYS A 8
REMARK 465 THR A 9
REMARK 465 ALA A 10
REMARK 465 GLY A 11
REMARK 465 ASN A 331
REMARK 465 PHE A 332
REMARK 465 ARG A 333
REMARK 465 ALA A 334
REMARK 465 SER A 335
REMARK 465 GLY A 336
REMARK 465 ASP A 337
REMARK 465 TYR A 338
REMARK 465 ASP A 339
REMARK 465 ASN A 340
REMARK 465 ASP A 341
REMARK 465 CYS A 342
REMARK 465 THR A 343
REMARK 465 ASN A 344
REMARK 465 PRO A 345
REMARK 465 ILE A 346
REMARK 465 THR A 347
REMARK 465 ASP A 483
REMARK 465 GLU A 484
REMARK 465 GLU A 485
REMARK 465 GLU A 486
REMARK 465 ASN A 487
REMARK 465 GLU A 488
REMARK 465 VAL A 489
REMARK 465 ASN A 490
REMARK 465 HIS A 491
REMARK 465 VAL A 492
REMARK 465 ASN A 493
REMARK 465 GLY A 494
REMARK 465 GLU A 495
REMARK 465 GLN A 496
REMARK 465 GLU A 497
REMARK 465 LYS A 561
REMARK 465 PHE A 562
REMARK 465 ASN A 563
REMARK 465 LYS A 564
REMARK 465 ILE A 565
REMARK 465 PRO A 566
REMARK 465 PHE A 567
REMARK 465 TYR A 568
REMARK 465 LEU A 569
REMARK 465 GLN A 570
REMARK 465 PRO A 571
REMARK 465 HIS A 572
REMARK 465 ALA A 573
REMARK 465 SER A 574
REMARK 465 SER A 575
REMARK 465 GLY A 576
REMARK 465 ALA A 577
REMARK 465 LYS A 578
REMARK 465 THR A 579
REMARK 465 LEU A 580
REMARK 465 TRP B 1
REMARK 465 SER B 2
REMARK 465 HIS B 3
REMARK 465 PRO B 4
REMARK 465 GLN B 5
REMARK 465 PHE B 6
REMARK 465 GLU B 7
REMARK 465 LYS B 8
REMARK 465 THR B 9
REMARK 465 ALA B 10
REMARK 465 GLY B 11
REMARK 465 ASN B 331
REMARK 465 PHE B 332
REMARK 465 ARG B 333
REMARK 465 ALA B 334
REMARK 465 SER B 335
REMARK 465 GLY B 336
REMARK 465 ASP B 337
REMARK 465 TYR B 338
REMARK 465 ASP B 339
REMARK 465 ASN B 340
REMARK 465 ASP B 341
REMARK 465 CYS B 342
REMARK 465 THR B 343
REMARK 465 ASN B 344
REMARK 465 PRO B 345
REMARK 465 ILE B 346
REMARK 465 THR B 347
REMARK 465 ASP B 483
REMARK 465 GLU B 484
REMARK 465 GLU B 485
REMARK 465 GLU B 486
REMARK 465 ASN B 487
REMARK 465 GLU B 488
REMARK 465 VAL B 489
REMARK 465 ASN B 490
REMARK 465 HIS B 491
REMARK 465 VAL B 492
REMARK 465 ASN B 493
REMARK 465 GLY B 494
REMARK 465 GLU B 495
REMARK 465 GLN B 496
REMARK 465 GLU B 497
REMARK 465 LYS B 561
REMARK 465 PHE B 562
REMARK 465 ASN B 563
REMARK 465 LYS B 564
REMARK 465 ILE B 565
REMARK 465 PRO B 566
REMARK 465 PHE B 567
REMARK 465 TYR B 568
REMARK 465 LEU B 569
REMARK 465 GLN B 570
REMARK 465 PRO B 571
REMARK 465 HIS B 572
REMARK 465 ALA B 573
REMARK 465 SER B 574
REMARK 465 SER B 575
REMARK 465 GLY B 576
REMARK 465 ALA B 577
REMARK 465 LYS B 578
REMARK 465 THR B 579
REMARK 465 LEU B 580
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 HIS A 73 -42.64 -175.11
REMARK 500 THR A 97 -4.46 89.81
REMARK 500 GLU A 130 50.88 38.53
REMARK 500 ARG A 274 -17.15 77.92
REMARK 500 ARG A 373 -48.04 -141.47
REMARK 500 HIS B 73 -40.91 178.34
REMARK 500 THR B 97 -0.81 83.74
REMARK 500 GLU B 130 51.26 39.66
REMARK 500 ASN B 156 42.96 -103.28
REMARK 500 ARG B 274 -16.77 74.68
REMARK 500 ARG B 373 -49.57 -138.75
REMARK 500 LYS B 400 55.87 -91.52
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 GOL A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 607
DBREF 5L8E A 9 580 UNP Q8TAF3 WDR48_HUMAN 9 580
DBREF 5L8E B 9 580 UNP Q8TAF3 WDR48_HUMAN 9 580
DBREF 5L8E C 106 110 PDB 5L8E 5L8E 106 110
SEQADV 5L8E TRP A 1 UNP Q8TAF3 EXPRESSION TAG
SEQADV 5L8E SER A 2 UNP Q8TAF3 EXPRESSION TAG
SEQADV 5L8E HIS A 3 UNP Q8TAF3 EXPRESSION TAG
SEQADV 5L8E PRO A 4 UNP Q8TAF3 EXPRESSION TAG
SEQADV 5L8E GLN A 5 UNP Q8TAF3 EXPRESSION TAG
SEQADV 5L8E PHE A 6 UNP Q8TAF3 EXPRESSION TAG
SEQADV 5L8E GLU A 7 UNP Q8TAF3 EXPRESSION TAG
SEQADV 5L8E LYS A 8 UNP Q8TAF3 EXPRESSION TAG
SEQADV 5L8E PHE A 369 UNP Q8TAF3 LEU 369 CONFLICT
SEQADV 5L8E TRP B 1 UNP Q8TAF3 EXPRESSION TAG
SEQADV 5L8E SER B 2 UNP Q8TAF3 EXPRESSION TAG
SEQADV 5L8E HIS B 3 UNP Q8TAF3 EXPRESSION TAG
SEQADV 5L8E PRO B 4 UNP Q8TAF3 EXPRESSION TAG
SEQADV 5L8E GLN B 5 UNP Q8TAF3 EXPRESSION TAG
SEQADV 5L8E PHE B 6 UNP Q8TAF3 EXPRESSION TAG
SEQADV 5L8E GLU B 7 UNP Q8TAF3 EXPRESSION TAG
SEQADV 5L8E LYS B 8 UNP Q8TAF3 EXPRESSION TAG
SEQADV 5L8E PHE B 369 UNP Q8TAF3 LEU 369 CONFLICT
SEQRES 1 A 580 TRP SER HIS PRO GLN PHE GLU LYS THR ALA GLY ARG ARG
SEQRES 2 A 580 LYS VAL GLN VAL SER TYR VAL ILE ARG ASP GLU VAL GLU
SEQRES 3 A 580 LYS TYR ASN ARG ASN GLY VAL ASN ALA LEU GLN LEU ASP
SEQRES 4 A 580 PRO ALA LEU ASN ARG LEU PHE THR ALA GLY ARG ASP SER
SEQRES 5 A 580 ILE ILE ARG ILE TRP SER VAL ASN GLN HIS LYS GLN ASP
SEQRES 6 A 580 PRO TYR ILE ALA SER MET GLU HIS HIS THR ASP TRP VAL
SEQRES 7 A 580 ASN ASP ILE VAL LEU CYS CYS ASN GLY LYS THR LEU ILE
SEQRES 8 A 580 SER ALA SER SER ASP THR THR VAL LYS VAL TRP ASN ALA
SEQRES 9 A 580 HIS LYS GLY PHE CYS MET SER THR LEU ARG THR HIS LYS
SEQRES 10 A 580 ASP TYR VAL LYS ALA LEU ALA TYR ALA LYS ASP LYS GLU
SEQRES 11 A 580 LEU VAL ALA SER ALA GLY LEU ASP ARG GLN ILE PHE LEU
SEQRES 12 A 580 TRP ASP VAL ASN THR LEU THR ALA LEU THR ALA SER ASN
SEQRES 13 A 580 ASN THR VAL THR THR SER SER LEU SER GLY ASN LYS ASP
SEQRES 14 A 580 SER ILE TYR SER LEU ALA MET ASN GLN LEU GLY THR ILE
SEQRES 15 A 580 ILE VAL SER GLY SER THR GLU LYS VAL LEU ARG VAL TRP
SEQRES 16 A 580 ASP PRO ARG THR CYS ALA LYS LEU MET LYS LEU LYS GLY
SEQRES 17 A 580 HIS THR ASP ASN VAL LYS ALA LEU LEU LEU ASN ARG ASP
SEQRES 18 A 580 GLY THR GLN CYS LEU SER GLY SER SER ASP GLY THR ILE
SEQRES 19 A 580 ARG LEU TRP SER LEU GLY GLN GLN ARG CYS ILE ALA THR
SEQRES 20 A 580 TYR ARG VAL HIS ASP GLU GLY VAL TRP ALA LEU GLN VAL
SEQRES 21 A 580 ASN ASP ALA PHE THR HIS VAL TYR SER GLY GLY ARG ASP
SEQRES 22 A 580 ARG LYS ILE TYR CYS THR ASP LEU ARG ASN PRO ASP ILE
SEQRES 23 A 580 ARG VAL LEU ILE CYS GLU GLU LYS ALA PRO VAL LEU LYS
SEQRES 24 A 580 MET GLU LEU ASP ARG SER ALA ASP PRO PRO PRO ALA ILE
SEQRES 25 A 580 TRP VAL ALA THR THR LYS SER THR VAL ASN LYS TRP THR
SEQRES 26 A 580 LEU LYS GLY ILE HIS ASN PHE ARG ALA SER GLY ASP TYR
SEQRES 27 A 580 ASP ASN ASP CYS THR ASN PRO ILE THR PRO LEU CYS THR
SEQRES 28 A 580 GLN PRO ASP GLN VAL ILE LYS GLY GLY ALA SER ILE ILE
SEQRES 29 A 580 GLN CYS HIS ILE PHE ASN ASP LYS ARG HIS ILE LEU THR
SEQRES 30 A 580 LYS ASP THR ASN ASN ASN VAL ALA TYR TRP ASP VAL LEU
SEQRES 31 A 580 LYS ALA CYS LYS VAL GLU ASP LEU GLY LYS VAL ASP PHE
SEQRES 32 A 580 GLU ASP GLU ILE LYS LYS ARG PHE LYS MET VAL TYR VAL
SEQRES 33 A 580 PRO ASN TRP PHE SER VAL ASP LEU LYS THR GLY MET LEU
SEQRES 34 A 580 THR ILE THR LEU ASP GLU SER ASP CYS PHE ALA ALA TRP
SEQRES 35 A 580 VAL SER ALA LYS ASP ALA GLY PHE SER SER PRO ASP GLY
SEQRES 36 A 580 SER ASP PRO LYS LEU ASN LEU GLY GLY LEU LEU LEU GLN
SEQRES 37 A 580 ALA LEU LEU GLU TYR TRP PRO ARG THR HIS VAL ASN PRO
SEQRES 38 A 580 MET ASP GLU GLU GLU ASN GLU VAL ASN HIS VAL ASN GLY
SEQRES 39 A 580 GLU GLN GLU ASN ARG VAL GLN LYS GLY ASN GLY TYR PHE
SEQRES 40 A 580 GLN VAL PRO PRO HIS THR PRO VAL ILE PHE GLY GLU ALA
SEQRES 41 A 580 GLY GLY ARG THR LEU PHE ARG LEU LEU CYS ARG ASP SER
SEQRES 42 A 580 GLY GLY GLU THR GLU SER MET LEU LEU ASN GLU THR VAL
SEQRES 43 A 580 PRO GLN TRP VAL ILE ASP ILE THR VAL ASP LYS ASN MET
SEQRES 44 A 580 PRO LYS PHE ASN LYS ILE PRO PHE TYR LEU GLN PRO HIS
SEQRES 45 A 580 ALA SER SER GLY ALA LYS THR LEU
SEQRES 1 B 580 TRP SER HIS PRO GLN PHE GLU LYS THR ALA GLY ARG ARG
SEQRES 2 B 580 LYS VAL GLN VAL SER TYR VAL ILE ARG ASP GLU VAL GLU
SEQRES 3 B 580 LYS TYR ASN ARG ASN GLY VAL ASN ALA LEU GLN LEU ASP
SEQRES 4 B 580 PRO ALA LEU ASN ARG LEU PHE THR ALA GLY ARG ASP SER
SEQRES 5 B 580 ILE ILE ARG ILE TRP SER VAL ASN GLN HIS LYS GLN ASP
SEQRES 6 B 580 PRO TYR ILE ALA SER MET GLU HIS HIS THR ASP TRP VAL
SEQRES 7 B 580 ASN ASP ILE VAL LEU CYS CYS ASN GLY LYS THR LEU ILE
SEQRES 8 B 580 SER ALA SER SER ASP THR THR VAL LYS VAL TRP ASN ALA
SEQRES 9 B 580 HIS LYS GLY PHE CYS MET SER THR LEU ARG THR HIS LYS
SEQRES 10 B 580 ASP TYR VAL LYS ALA LEU ALA TYR ALA LYS ASP LYS GLU
SEQRES 11 B 580 LEU VAL ALA SER ALA GLY LEU ASP ARG GLN ILE PHE LEU
SEQRES 12 B 580 TRP ASP VAL ASN THR LEU THR ALA LEU THR ALA SER ASN
SEQRES 13 B 580 ASN THR VAL THR THR SER SER LEU SER GLY ASN LYS ASP
SEQRES 14 B 580 SER ILE TYR SER LEU ALA MET ASN GLN LEU GLY THR ILE
SEQRES 15 B 580 ILE VAL SER GLY SER THR GLU LYS VAL LEU ARG VAL TRP
SEQRES 16 B 580 ASP PRO ARG THR CYS ALA LYS LEU MET LYS LEU LYS GLY
SEQRES 17 B 580 HIS THR ASP ASN VAL LYS ALA LEU LEU LEU ASN ARG ASP
SEQRES 18 B 580 GLY THR GLN CYS LEU SER GLY SER SER ASP GLY THR ILE
SEQRES 19 B 580 ARG LEU TRP SER LEU GLY GLN GLN ARG CYS ILE ALA THR
SEQRES 20 B 580 TYR ARG VAL HIS ASP GLU GLY VAL TRP ALA LEU GLN VAL
SEQRES 21 B 580 ASN ASP ALA PHE THR HIS VAL TYR SER GLY GLY ARG ASP
SEQRES 22 B 580 ARG LYS ILE TYR CYS THR ASP LEU ARG ASN PRO ASP ILE
SEQRES 23 B 580 ARG VAL LEU ILE CYS GLU GLU LYS ALA PRO VAL LEU LYS
SEQRES 24 B 580 MET GLU LEU ASP ARG SER ALA ASP PRO PRO PRO ALA ILE
SEQRES 25 B 580 TRP VAL ALA THR THR LYS SER THR VAL ASN LYS TRP THR
SEQRES 26 B 580 LEU LYS GLY ILE HIS ASN PHE ARG ALA SER GLY ASP TYR
SEQRES 27 B 580 ASP ASN ASP CYS THR ASN PRO ILE THR PRO LEU CYS THR
SEQRES 28 B 580 GLN PRO ASP GLN VAL ILE LYS GLY GLY ALA SER ILE ILE
SEQRES 29 B 580 GLN CYS HIS ILE PHE ASN ASP LYS ARG HIS ILE LEU THR
SEQRES 30 B 580 LYS ASP THR ASN ASN ASN VAL ALA TYR TRP ASP VAL LEU
SEQRES 31 B 580 LYS ALA CYS LYS VAL GLU ASP LEU GLY LYS VAL ASP PHE
SEQRES 32 B 580 GLU ASP GLU ILE LYS LYS ARG PHE LYS MET VAL TYR VAL
SEQRES 33 B 580 PRO ASN TRP PHE SER VAL ASP LEU LYS THR GLY MET LEU
SEQRES 34 B 580 THR ILE THR LEU ASP GLU SER ASP CYS PHE ALA ALA TRP
SEQRES 35 B 580 VAL SER ALA LYS ASP ALA GLY PHE SER SER PRO ASP GLY
SEQRES 36 B 580 SER ASP PRO LYS LEU ASN LEU GLY GLY LEU LEU LEU GLN
SEQRES 37 B 580 ALA LEU LEU GLU TYR TRP PRO ARG THR HIS VAL ASN PRO
SEQRES 38 B 580 MET ASP GLU GLU GLU ASN GLU VAL ASN HIS VAL ASN GLY
SEQRES 39 B 580 GLU GLN GLU ASN ARG VAL GLN LYS GLY ASN GLY TYR PHE
SEQRES 40 B 580 GLN VAL PRO PRO HIS THR PRO VAL ILE PHE GLY GLU ALA
SEQRES 41 B 580 GLY GLY ARG THR LEU PHE ARG LEU LEU CYS ARG ASP SER
SEQRES 42 B 580 GLY GLY GLU THR GLU SER MET LEU LEU ASN GLU THR VAL
SEQRES 43 B 580 PRO GLN TRP VAL ILE ASP ILE THR VAL ASP LYS ASN MET
SEQRES 44 B 580 PRO LYS PHE ASN LYS ILE PRO PHE TYR LEU GLN PRO HIS
SEQRES 45 B 580 ALA SER SER GLY ALA LYS THR LEU
SEQRES 1 C 5 UNK UNK UNK UNK UNK
HET GOL A 601 6
HET GOL A 602 6
HET GOL A 603 6
HET GOL A 604 6
HET GOL A 605 6
HET GOL A 606 6
HET GOL A 607 6
HET GOL B 601 6
HET GOL B 602 6
HET GOL B 603 6
HET GOL B 604 6
HET GOL B 605 6
HET GOL B 606 6
HET GOL B 607 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 GOL 14(C3 H8 O3)
FORMUL 18 HOH *310(H2 O)
HELIX 1 AA1 LYS A 127 LYS A 129 5 3
HELIX 2 AA2 VAL A 146 ALA A 151 1 6
HELIX 3 AA3 ASP A 402 ARG A 410 1 9
HELIX 4 AA4 LEU A 462 LEU A 471 1 10
HELIX 5 AA5 TRP A 474 HIS A 478 5 5
HELIX 6 AA6 ARG A 531 SER A 533 5 3
HELIX 7 AA7 GLY A 535 VAL A 546 1 12
HELIX 8 AA8 PRO A 547 VAL A 555 1 9
HELIX 9 AA9 LYS B 127 LYS B 129 5 3
HELIX 10 AB1 VAL B 146 ALA B 151 1 6
HELIX 11 AB2 ASP B 402 ARG B 410 1 9
HELIX 12 AB3 ASP B 434 PHE B 439 1 6
HELIX 13 AB4 LEU B 462 LEU B 471 1 10
HELIX 14 AB5 TRP B 474 HIS B 478 5 5
HELIX 15 AB6 ARG B 531 SER B 533 5 3
HELIX 16 AB7 GLY B 535 VAL B 546 1 12
HELIX 17 AB8 PRO B 547 VAL B 555 1 9
SHEET 1 AA1 5 SER A 421 ASP A 423 0
SHEET 2 AA1 5 LEU A 429 LEU A 433 -1 O THR A 432 N SER A 421
SHEET 3 AA1 5 VAL A 15 ILE A 21 -1 N VAL A 17 O LEU A 433
SHEET 4 AA1 5 PRO A 514 GLU A 519 -1 O GLY A 518 N GLN A 16
SHEET 5 AA1 5 THR A 524 LEU A 529 -1 O LEU A 528 N VAL A 515
SHEET 1 AA2 4 VAL A 33 ASP A 39 0
SHEET 2 AA2 4 ARG A 44 GLY A 49 -1 O ARG A 44 N ASP A 39
SHEET 3 AA2 4 ILE A 54 SER A 58 -1 O TRP A 57 N LEU A 45
SHEET 4 AA2 4 TYR A 67 MET A 71 -1 O MET A 71 N ILE A 54
SHEET 1 AA3 4 VAL A 78 CYS A 84 0
SHEET 2 AA3 4 THR A 89 SER A 94 -1 O THR A 89 N CYS A 84
SHEET 3 AA3 4 VAL A 99 ASN A 103 -1 O TRP A 102 N LEU A 90
SHEET 4 AA3 4 PHE A 108 LEU A 113 -1 O MET A 110 N VAL A 101
SHEET 1 AA4 4 VAL A 120 ALA A 126 0
SHEET 2 AA4 4 LEU A 131 GLY A 136 -1 O LEU A 131 N ALA A 126
SHEET 3 AA4 4 ILE A 141 ASP A 145 -1 O TRP A 144 N VAL A 132
SHEET 4 AA4 4 SER A 162 LEU A 164 -1 O SER A 162 N LEU A 143
SHEET 1 AA5 2 THR A 158 THR A 160 0
SHEET 2 AA5 2 UNK C 107 UNK C 109 -1 O UNK C 108 N VAL A 159
SHEET 1 AA6 4 ILE A 171 MET A 176 0
SHEET 2 AA6 4 ILE A 183 SER A 187 -1 O VAL A 184 N ALA A 175
SHEET 3 AA6 4 LEU A 192 ASP A 196 -1 O TRP A 195 N ILE A 183
SHEET 4 AA6 4 ALA A 201 LEU A 206 -1 O LEU A 206 N LEU A 192
SHEET 1 AA7 4 VAL A 213 LEU A 218 0
SHEET 2 AA7 4 GLN A 224 SER A 229 -1 O LEU A 226 N LEU A 217
SHEET 3 AA7 4 ILE A 234 SER A 238 -1 O TRP A 237 N CYS A 225
SHEET 4 AA7 4 ARG A 243 TYR A 248 -1 O TYR A 248 N ILE A 234
SHEET 1 AA8 4 VAL A 255 VAL A 260 0
SHEET 2 AA8 4 HIS A 266 GLY A 271 -1 O TYR A 268 N GLN A 259
SHEET 3 AA8 4 LYS A 275 ASP A 280 -1 O THR A 279 N VAL A 267
SHEET 4 AA8 4 ARG A 287 GLU A 292 -1 O ILE A 290 N ILE A 276
SHEET 1 AA9 4 VAL A 297 LEU A 302 0
SHEET 2 AA9 4 ALA A 311 THR A 316 -1 O ALA A 315 N LYS A 299
SHEET 3 AA9 4 VAL A 321 THR A 325 -1 O TRP A 324 N ILE A 312
SHEET 4 AA9 4 GLN A 355 ILE A 357 -1 O GLN A 355 N LYS A 323
SHEET 1 AB1 4 ILE A 363 ILE A 368 0
SHEET 2 AB1 4 HIS A 374 ASP A 379 -1 O LEU A 376 N HIS A 367
SHEET 3 AB1 4 VAL A 384 ASP A 388 -1 O TRP A 387 N ILE A 375
SHEET 4 AB1 4 CYS A 393 GLY A 399 -1 O VAL A 395 N TYR A 386
SHEET 1 AB2 2 TRP A 442 SER A 444 0
SHEET 2 AB2 2 LYS A 459 ASN A 461 -1 O LEU A 460 N VAL A 443
SHEET 1 AB3 5 SER B 421 ASP B 423 0
SHEET 2 AB3 5 LEU B 429 LEU B 433 -1 O THR B 432 N SER B 421
SHEET 3 AB3 5 VAL B 15 ILE B 21 -1 N VAL B 17 O LEU B 433
SHEET 4 AB3 5 PRO B 514 GLU B 519 -1 O ILE B 516 N SER B 18
SHEET 5 AB3 5 THR B 524 LEU B 529 -1 O LEU B 528 N VAL B 515
SHEET 1 AB4 4 VAL B 33 ASP B 39 0
SHEET 2 AB4 4 ARG B 44 GLY B 49 -1 O ARG B 44 N ASP B 39
SHEET 3 AB4 4 ILE B 54 SER B 58 -1 O TRP B 57 N LEU B 45
SHEET 4 AB4 4 TYR B 67 MET B 71 -1 O MET B 71 N ILE B 54
SHEET 1 AB5 4 VAL B 78 CYS B 84 0
SHEET 2 AB5 4 THR B 89 SER B 94 -1 O THR B 89 N CYS B 84
SHEET 3 AB5 4 VAL B 99 ASN B 103 -1 O TRP B 102 N LEU B 90
SHEET 4 AB5 4 PHE B 108 LEU B 113 -1 O LEU B 113 N VAL B 99
SHEET 1 AB6 4 VAL B 120 ALA B 126 0
SHEET 2 AB6 4 LEU B 131 GLY B 136 -1 O LEU B 131 N ALA B 126
SHEET 3 AB6 4 ILE B 141 ASP B 145 -1 O TRP B 144 N VAL B 132
SHEET 4 AB6 4 SER B 163 LEU B 164 -1 O LEU B 164 N ILE B 141
SHEET 1 AB7 4 ILE B 171 MET B 176 0
SHEET 2 AB7 4 ILE B 183 SER B 187 -1 O VAL B 184 N ALA B 175
SHEET 3 AB7 4 LEU B 192 ASP B 196 -1 O ARG B 193 N SER B 185
SHEET 4 AB7 4 ALA B 201 LEU B 206 -1 O LEU B 206 N LEU B 192
SHEET 1 AB8 4 VAL B 213 LEU B 218 0
SHEET 2 AB8 4 GLN B 224 SER B 229 -1 O GLY B 228 N ALA B 215
SHEET 3 AB8 4 ILE B 234 SER B 238 -1 O TRP B 237 N CYS B 225
SHEET 4 AB8 4 ARG B 243 TYR B 248 -1 O TYR B 248 N ILE B 234
SHEET 1 AB9 4 VAL B 255 VAL B 260 0
SHEET 2 AB9 4 HIS B 266 GLY B 271 -1 O TYR B 268 N GLN B 259
SHEET 3 AB9 4 LYS B 275 ASP B 280 -1 O THR B 279 N VAL B 267
SHEET 4 AB9 4 ARG B 287 GLU B 292 -1 O ILE B 290 N ILE B 276
SHEET 1 AC1 4 VAL B 297 LEU B 302 0
SHEET 2 AC1 4 ALA B 311 THR B 316 -1 O ALA B 315 N LYS B 299
SHEET 3 AC1 4 VAL B 321 THR B 325 -1 O ASN B 322 N VAL B 314
SHEET 4 AC1 4 GLN B 355 ILE B 357 -1 O ILE B 357 N VAL B 321
SHEET 1 AC2 4 ILE B 363 ILE B 368 0
SHEET 2 AC2 4 HIS B 374 ASP B 379 -1 O LEU B 376 N HIS B 367
SHEET 3 AC2 4 VAL B 384 ASP B 388 -1 O TRP B 387 N ILE B 375
SHEET 4 AC2 4 CYS B 393 GLY B 399 -1 O VAL B 395 N TYR B 386
SHEET 1 AC3 2 TRP B 442 SER B 444 0
SHEET 2 AC3 2 LYS B 459 ASN B 461 -1 O LEU B 460 N VAL B 443
CISPEP 1 ASP A 307 PRO A 308 0 -1.62
SITE 1 AC1 6 ARG A 50 ARG A 272 GOL A 602 HOH A 805
SITE 2 AC1 6 LYS B 378 ASN B 382
SITE 1 AC2 6 ASN A 31 ARG A 50 LYS A 425 GOL A 601
SITE 2 AC2 6 HOH A 719 GLN B 365
SITE 1 AC3 7 HIS A 73 CYS A 109 MET A 110 SER A 111
SITE 2 AC3 7 THR A 112 GOL A 605 GLU B 536
SITE 1 AC4 5 LYS A 318 SER A 319 GLY A 359 HOH A 715
SITE 2 AC4 5 HOH A 718
SITE 1 AC5 4 SER A 111 THR A 112 GOL A 603 HOH A 709
SITE 1 AC6 4 HIS A 73 LYS A 100 ARG A 114 ARG A 527
SITE 1 AC7 4 LYS A 168 ARG A 193 LYS A 202 LYS A 205
SITE 1 AC8 7 LYS A 378 ASN A 382 ARG B 50 ARG B 272
SITE 2 AC8 7 THR B 317 GOL B 602 HOH B 821
SITE 1 AC9 6 GLU A 404 ASN B 31 GOL B 601 HOH B 745
SITE 2 AC9 6 HOH B 752 HOH B 798
SITE 1 AD1 3 LYS B 168 ARG B 193 LYS B 205
SITE 1 AD2 4 HIS B 73 LYS B 100 ARG B 527 GOL B 607
SITE 1 AD3 4 THR B 112 ASN B 157 GOL B 607 HOH B 710
SITE 1 AD4 5 SER B 319 GLY B 360 SER B 362 THR B 380
SITE 2 AD4 5 HOH B 825
SITE 1 AD5 9 GLU A 536 HIS B 73 CYS B 109 MET B 110
SITE 2 AD5 9 THR B 112 GOL B 604 GOL B 605 HOH B 703
SITE 3 AD5 9 HOH B 710
CRYST1 73.303 131.601 148.672 90.00 90.00 90.00 P 2 21 21 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 0.013642 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007599 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006726 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
