HEADER CELL CYCLE 31-OCT-11 4A64
TITLE CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF HUMAN CUL4B AT 2.57A
TITLE 2 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CULLIN-4B;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 188-539;
COMPND 5 SYNONYM: CUL4B, CUL-4B;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: R3-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNIC-ZB
KEYWDS CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.VOLLMAR,V.AYINAMPUDI,C.COOPER,K.GUO,T.KROJER,J.R.C.MUNIZ,F.VON
AUTHOR 2 DELFT,J.WEIGELT,C.H.ARROWSMITH,C.BOUNTRA,A.EDWARDS,A.BULLOCK
REVDAT 2 24-JAN-18 4A64 1 JRNL
REVDAT 1 29-FEB-12 4A64 0
JRNL AUTH M.VOLLMAR,V.AYINAMPUDI,C.COOPER,K.GUO,T.KROJER,J.R.C.MUNIZ,
JRNL AUTH 2 F.VON DELFT,J.WEIGELT,C.H.ARROWSMITH,C.BOUNTRA,A.EDWARDS,
JRNL AUTH 3 A.BULLOCK
JRNL TITL CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF HUMAN CUL4B AT
JRNL TITL 2 2.57A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.57 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.57
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 55064
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) : 0.184
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2940
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) : 2.57
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3890
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 BIN R VALUE (WORKING SET) : 0.3470
REMARK 3 BIN FREE R VALUE SET COUNT : 208
REMARK 3 BIN FREE R VALUE : 0.4040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11036
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 253
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 67.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.70000
REMARK 3 B22 (A**2) : -0.56000
REMARK 3 B33 (A**2) : -2.45000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.54000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.529
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.274
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.206
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.020
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11315 ; 0.014 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 7742 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15255 ; 1.600 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18892 ; 1.414 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1362 ; 5.142 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 602 ;37.765 ;24.950
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2181 ;16.428 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 79 ;20.331 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1725 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12443 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2256 ; 0.006 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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 : 8
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 1 A 363
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4437 -9.1511 38.1586
REMARK 3 T TENSOR
REMARK 3 T11: 0.2101 T22: 0.0649
REMARK 3 T33: 0.1913 T12: -0.0216
REMARK 3 T13: -0.0248 T23: -0.0851
REMARK 3 L TENSOR
REMARK 3 L11: 2.7542 L22: 1.1211
REMARK 3 L33: 3.8841 L12: -0.8884
REMARK 3 L13: 2.6954 L23: -1.5528
REMARK 3 S TENSOR
REMARK 3 S11: -0.2823 S12: 0.0924 S13: 0.2423
REMARK 3 S21: 0.0572 S22: 0.0180 S23: -0.0556
REMARK 3 S31: -0.3342 S32: -0.0199 S33: 0.2643
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 364 A 533
REMARK 3 ORIGIN FOR THE GROUP (A): 48.0027 -44.8202 62.6735
REMARK 3 T TENSOR
REMARK 3 T11: 0.0950 T22: 0.1865
REMARK 3 T33: 0.2715 T12: 0.0005
REMARK 3 T13: 0.0017 T23: 0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 2.2826 L22: 10.1832
REMARK 3 L33: 2.0627 L12: -2.1401
REMARK 3 L13: 1.0316 L23: -2.4481
REMARK 3 S TENSOR
REMARK 3 S11: 0.0806 S12: -0.0791 S13: -0.0317
REMARK 3 S21: 0.2555 S22: -0.3039 S23: -1.0272
REMARK 3 S31: 0.2412 S32: 0.3121 S33: 0.2233
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 : B 1 B 364
REMARK 3 ORIGIN FOR THE GROUP (A): 28.6030 -60.0375 35.5289
REMARK 3 T TENSOR
REMARK 3 T11: 0.1329 T22: 0.0514
REMARK 3 T33: 0.1989 T12: -0.0803
REMARK 3 T13: 0.0116 T23: -0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 0.7132 L22: 1.5670
REMARK 3 L33: 7.1641 L12: -0.3462
REMARK 3 L13: -0.7179 L23: 2.1753
REMARK 3 S TENSOR
REMARK 3 S11: -0.1231 S12: 0.1038 S13: -0.0399
REMARK 3 S21: 0.0694 S22: -0.0194 S23: 0.0284
REMARK 3 S31: 0.3193 S32: -0.1320 S33: 0.1425
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 365 B 533
REMARK 3 ORIGIN FOR THE GROUP (A): 21.7316 -24.2430 71.5712
REMARK 3 T TENSOR
REMARK 3 T11: 0.0453 T22: 0.2115
REMARK 3 T33: 0.1198 T12: 0.0338
REMARK 3 T13: -0.0176 T23: -0.0719
REMARK 3 L TENSOR
REMARK 3 L11: 1.0968 L22: 8.7382
REMARK 3 L33: 2.8108 L12: 0.4669
REMARK 3 L13: 0.1599 L23: 3.3397
REMARK 3 S TENSOR
REMARK 3 S11: -0.1106 S12: -0.2816 S13: 0.1402
REMARK 3 S21: 0.2766 S22: -0.2293 S23: 0.6149
REMARK 3 S31: -0.0508 S32: -0.2976 S33: 0.3399
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 196 C 321
REMARK 3 ORIGIN FOR THE GROUP (A): 46.7574 -50.0396 28.9653
REMARK 3 T TENSOR
REMARK 3 T11: 0.0833 T22: 0.3206
REMARK 3 T33: 0.2719 T12: -0.0806
REMARK 3 T13: -0.0205 T23: 0.0435
REMARK 3 L TENSOR
REMARK 3 L11: 3.6670 L22: 5.8461
REMARK 3 L33: 7.6685 L12: -0.7921
REMARK 3 L13: 1.5308 L23: -1.7085
REMARK 3 S TENSOR
REMARK 3 S11: 0.1955 S12: -0.0573 S13: -0.0482
REMARK 3 S21: 0.4547 S22: -0.3896 S23: -0.6176
REMARK 3 S31: 0.1505 S32: 0.8032 S33: 0.1941
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 322 C 534
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3528 -22.0239 5.6970
REMARK 3 T TENSOR
REMARK 3 T11: 0.0888 T22: 0.1296
REMARK 3 T33: 0.0214 T12: -0.0570
REMARK 3 T13: 0.0035 T23: -0.0278
REMARK 3 L TENSOR
REMARK 3 L11: 5.3907 L22: 2.7419
REMARK 3 L33: 1.2088 L12: -2.8819
REMARK 3 L13: 1.7641 L23: -1.1396
REMARK 3 S TENSOR
REMARK 3 S11: -0.0514 S12: 0.1265 S13: 0.1662
REMARK 3 S21: -0.2197 S22: -0.0671 S23: -0.0938
REMARK 3 S31: -0.0724 S32: 0.0601 S33: 0.1185
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 196 D 313
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1304 -18.5240 44.1421
REMARK 3 T TENSOR
REMARK 3 T11: 0.2263 T22: 0.3734
REMARK 3 T33: 0.1688 T12: -0.0527
REMARK 3 T13: 0.1088 T23: -0.0845
REMARK 3 L TENSOR
REMARK 3 L11: 2.8092 L22: 4.3334
REMARK 3 L33: 5.4817 L12: 1.0618
REMARK 3 L13: 1.4644 L23: 1.5798
REMARK 3 S TENSOR
REMARK 3 S11: 0.1477 S12: -0.6612 S13: 0.0547
REMARK 3 S21: 0.7139 S22: -0.2144 S23: 0.2023
REMARK 3 S31: -0.3234 S32: -0.4570 S33: 0.0667
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 314 D 532
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9661 -46.0156 8.6078
REMARK 3 T TENSOR
REMARK 3 T11: 0.2506 T22: 0.1346
REMARK 3 T33: 0.0833 T12: -0.0477
REMARK 3 T13: -0.0165 T23: -0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 3.0360 L22: 3.3481
REMARK 3 L33: 3.6495 L12: -2.1123
REMARK 3 L13: -2.4345 L23: 1.8430
REMARK 3 S TENSOR
REMARK 3 S11: -0.0294 S12: 0.1170 S13: -0.2185
REMARK 3 S21: -0.3271 S22: -0.0590 S23: 0.1266
REMARK 3 S31: 0.4919 S32: 0.0007 S33: 0.0884
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 RIDING
REMARK 3 POSITIONS. U VALUES WITH TLS ADDED
REMARK 4
REMARK 4 4A64 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1290050158.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58043
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.570
REMARK 200 RESOLUTION RANGE LOW (A) : 19.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.57
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.73000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: PDB ENTRIES 1U6G, 1LDK, 1LDJ, 2HYE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG4000, 100 MM LISO4, 100 MM TRIS
REMARK 280 (PH 8.2)
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 78.54550
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 59610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, VAL 498 TO ARG
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, LEU 502 TO ASP
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, VAL 498 TO ARG
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, LEU 502 TO ASP
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, VAL 498 TO ARG
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, LEU 502 TO ASP
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, VAL 498 TO ARG
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, LEU 502 TO ASP
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 ILE A 534
REMARK 465 ASN A 535
REMARK 465 LYS A 536
REMARK 465 ARG A 537
REMARK 465 PRO A 538
REMARK 465 ASN A 539
REMARK 465 GLU B 492
REMARK 465 LYS B 493
REMARK 465 ASP B 494
REMARK 465 ILE B 534
REMARK 465 ASN B 535
REMARK 465 LYS B 536
REMARK 465 ARG B 537
REMARK 465 PRO B 538
REMARK 465 ASN B 539
REMARK 465 SER C 186
REMARK 465 MET C 187
REMARK 465 PRO C 188
REMARK 465 LYS C 189
REMARK 465 LEU C 190
REMARK 465 PRO C 191
REMARK 465 GLU C 192
REMARK 465 ASN C 193
REMARK 465 TYR C 194
REMARK 465 THR C 195
REMARK 465 LYS C 233
REMARK 465 ILE C 234
REMARK 465 SER C 235
REMARK 465 ALA C 236
REMARK 465 ASP C 260
REMARK 465 SER C 261
REMARK 465 ASN C 535
REMARK 465 LYS C 536
REMARK 465 ARG C 537
REMARK 465 PRO C 538
REMARK 465 ASN C 539
REMARK 465 SER D 186
REMARK 465 MET D 187
REMARK 465 PRO D 188
REMARK 465 LYS D 189
REMARK 465 LEU D 190
REMARK 465 PRO D 191
REMARK 465 GLU D 192
REMARK 465 ASN D 193
REMARK 465 TYR D 194
REMARK 465 THR D 195
REMARK 465 SER D 231
REMARK 465 TYR D 232
REMARK 465 LYS D 233
REMARK 465 ILE D 234
REMARK 465 SER D 235
REMARK 465 ALA D 236
REMARK 465 SER D 261
REMARK 465 ASN D 490
REMARK 465 PRO D 491
REMARK 465 GLU D 492
REMARK 465 LYS D 493
REMARK 465 ASP D 494
REMARK 465 LYS D 495
REMARK 465 THR D 496
REMARK 465 MET D 497
REMARK 465 ARG D 498
REMARK 465 GLN D 499
REMARK 465 PHE D 533
REMARK 465 ILE D 534
REMARK 465 ASN D 535
REMARK 465 LYS D 536
REMARK 465 ARG D 537
REMARK 465 PRO D 538
REMARK 465 ASN D 539
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 189 CD CE NZ
REMARK 470 LYS A 240 CE NZ
REMARK 470 SER A 261 OG
REMARK 470 GLN A 299 CG CD OE1 NE2
REMARK 470 ARG A 466 CG CD NE CZ NH1 NH2
REMARK 470 SER A 485 OG
REMARK 470 THR A 486 OG1 CG2
REMARK 470 ILE A 487 CG1 CG2 CD1
REMARK 470 ILE A 489 CG1 CG2 CD1
REMARK 470 ASN A 490 CG OD1 ND2
REMARK 470 GLU A 492 CG CD OE1 OE2
REMARK 470 LYS A 493 CG CD CE NZ
REMARK 470 ASP A 494 CG OD1 OD2
REMARK 470 LYS A 495 CG CD CE NZ
REMARK 470 THR A 496 OG1 CG2
REMARK 470 LYS A 521 CD CE NZ
REMARK 470 GLU A 531 CD OE1 OE2
REMARK 470 LYS B 189 CD CE NZ
REMARK 470 ASP B 260 CG OD1 OD2
REMARK 470 SER B 261 OG
REMARK 470 GLN B 299 CG CD OE1 NE2
REMARK 470 LYS B 323 CE NZ
REMARK 470 ARG B 466 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 489 CG1 CG2 CD1
REMARK 470 ASN B 490 CG OD1 ND2
REMARK 470 LYS B 495 CG CD CE NZ
REMARK 470 LYS B 521 CD CE NZ
REMARK 470 LYS B 527 CD CE NZ
REMARK 470 LYS C 201 CD CE NZ
REMARK 470 TYR C 232 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE C 254 CG1 CG2 CD1
REMARK 470 GLU C 259 CG CD OE1 OE2
REMARK 470 LEU C 262 CG CD1 CD2
REMARK 470 SER C 320 OG
REMARK 470 GLN C 322 CG CD OE1 NE2
REMARK 470 LYS C 323 CG CD CE NZ
REMARK 470 ARG C 377 NE CZ NH1 NH2
REMARK 470 GLU C 492 CG CD OE1 OE2
REMARK 470 LYS C 493 CG CD CE NZ
REMARK 470 ILE C 534 CG1 CG2 CD1
REMARK 470 GLU D 197 CG CD OE1 OE2
REMARK 470 LYS D 203 CE NZ
REMARK 470 LYS D 240 CD CE NZ
REMARK 470 GLU D 259 CG CD OE1 OE2
REMARK 470 LYS D 481 CG CD CE NZ
REMARK 470 ILE D 487 CG1 CG2 CD1
REMARK 470 VAL D 488 CG1 CG2
REMARK 470 ILE D 489 CG1 CG2 CD1
REMARK 470 LEU D 501 CG CD1 CD2
REMARK 470 LYS D 521 CD CE NZ
REMARK 470 PHE D 530 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU D 531 CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH C 2019 O HOH C 2020 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 255 CG HIS A 255 CD2 0.057
REMARK 500 HIS B 397 CG HIS B 397 CD2 0.056
REMARK 500 HIS C 397 CG HIS C 397 CD2 0.063
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 MET A 387 CG - SD - CE ANGL. DEV. = -12.1 DEGREES
REMARK 500 LEU B 410 CB - CG - CD2 ANGL. DEV. = -11.3 DEGREES
REMARK 500 ARG C 286 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 LEU D 410 CB - CG - CD2 ANGL. DEV. = -10.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 191 103.39 -57.03
REMARK 500 ASP A 196 5.07 88.14
REMARK 500 THR A 213 -158.96 -99.08
REMARK 500 GLU A 259 24.32 -74.22
REMARK 500 ASP A 263 132.67 -38.85
REMARK 500 ILE A 318 -70.91 -111.92
REMARK 500 TYR A 413 -9.12 -144.79
REMARK 500 ASN A 490 74.56 -116.93
REMARK 500 PRO B 191 104.46 -59.03
REMARK 500 ASP B 196 4.81 86.71
REMARK 500 GLU B 259 25.56 -75.51
REMARK 500 ASP B 263 133.27 -39.99
REMARK 500 ILE B 318 -70.50 -111.78
REMARK 500 TYR B 413 -6.48 -145.10
REMARK 500 ASN B 490 70.22 -117.41
REMARK 500 ASP C 263 132.91 -39.47
REMARK 500 TYR C 413 -10.04 -144.40
REMARK 500 ASN C 490 67.26 -117.06
REMARK 500 ASN C 490 68.09 -117.76
REMARK 500 PHE C 533 -33.45 -140.26
REMARK 500 GLU D 259 25.96 -77.36
REMARK 500 ILE D 318 -72.21 -111.24
REMARK 500 TYR D 413 -8.67 -142.29
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 EDO A 1534
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1535
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1536
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1537
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1534
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1535
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1533
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4A0C RELATED DB: PDB
REMARK 900 STRUCTURE OF THE CAND1-CUL4B-RBX1 COMPLEX
REMARK 900 RELATED ID: 4A0L RELATED DB: PDB
REMARK 900 STRUCTURE OF DDB1-DDB2-CUL4B-RBX1 BOUND TO A 12 BP ABASIC SITE
REMARK 900 CONTAINING DNA-DUPLEX
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 STARTING RESIDUES SER186 AND MET187 ARE DUE TO CLONING
DBREF 4A64 A 188 539 UNP Q13620 CUL4B_HUMAN 188 539
DBREF 4A64 B 188 539 UNP Q13620 CUL4B_HUMAN 188 539
DBREF 4A64 C 188 539 UNP Q13620 CUL4B_HUMAN 188 539
DBREF 4A64 D 188 539 UNP Q13620 CUL4B_HUMAN 188 539
SEQADV 4A64 SER A 186 UNP Q13620 EXPRESSION TAG
SEQADV 4A64 MET A 187 UNP Q13620 EXPRESSION TAG
SEQADV 4A64 ARG A 498 UNP Q13620 VAL 498 ENGINEERED MUTATION
SEQADV 4A64 ASP A 502 UNP Q13620 LEU 502 ENGINEERED MUTATION
SEQADV 4A64 SER B 186 UNP Q13620 EXPRESSION TAG
SEQADV 4A64 MET B 187 UNP Q13620 EXPRESSION TAG
SEQADV 4A64 ARG B 498 UNP Q13620 VAL 498 ENGINEERED MUTATION
SEQADV 4A64 ASP B 502 UNP Q13620 LEU 502 ENGINEERED MUTATION
SEQADV 4A64 SER C 186 UNP Q13620 EXPRESSION TAG
SEQADV 4A64 MET C 187 UNP Q13620 EXPRESSION TAG
SEQADV 4A64 ARG C 498 UNP Q13620 VAL 498 ENGINEERED MUTATION
SEQADV 4A64 ASP C 502 UNP Q13620 LEU 502 ENGINEERED MUTATION
SEQADV 4A64 SER D 186 UNP Q13620 EXPRESSION TAG
SEQADV 4A64 MET D 187 UNP Q13620 EXPRESSION TAG
SEQADV 4A64 ARG D 498 UNP Q13620 VAL 498 ENGINEERED MUTATION
SEQADV 4A64 ASP D 502 UNP Q13620 LEU 502 ENGINEERED MUTATION
SEQRES 1 A 354 SER MET PRO LYS LEU PRO GLU ASN TYR THR ASP GLU THR
SEQRES 2 A 354 TRP GLN LYS LEU LYS GLU ALA VAL GLU ALA ILE GLN ASN
SEQRES 3 A 354 SER THR SER ILE LYS TYR ASN LEU GLU GLU LEU TYR GLN
SEQRES 4 A 354 ALA VAL GLU ASN LEU CYS SER TYR LYS ILE SER ALA ASN
SEQRES 5 A 354 LEU TYR LYS GLN LEU ARG GLN ILE CYS GLU ASP HIS ILE
SEQRES 6 A 354 LYS ALA GLN ILE HIS GLN PHE ARG GLU ASP SER LEU ASP
SEQRES 7 A 354 SER VAL LEU PHE LEU LYS LYS ILE ASP ARG CYS TRP GLN
SEQRES 8 A 354 ASN HIS CYS ARG GLN MET ILE MET ILE ARG SER ILE PHE
SEQRES 9 A 354 LEU PHE LEU ASP ARG THR TYR VAL LEU GLN ASN SER MET
SEQRES 10 A 354 LEU PRO SER ILE TRP ASP MET GLY LEU GLU LEU PHE ARG
SEQRES 11 A 354 ALA HIS ILE ILE SER ASP GLN LYS VAL GLN ASN LYS THR
SEQRES 12 A 354 ILE ASP GLY ILE LEU LEU LEU ILE GLU ARG GLU ARG ASN
SEQRES 13 A 354 GLY GLU ALA ILE ASP ARG SER LEU LEU ARG SER LEU LEU
SEQRES 14 A 354 SER MET LEU SER ASP LEU GLN ILE TYR GLN ASP SER PHE
SEQRES 15 A 354 GLU GLN ARG PHE LEU GLU GLU THR ASN ARG LEU TYR ALA
SEQRES 16 A 354 ALA GLU GLY GLN LYS LEU MET GLN GLU ARG GLU VAL PRO
SEQRES 17 A 354 GLU TYR LEU HIS HIS VAL ASN LYS ARG LEU GLU GLU GLU
SEQRES 18 A 354 ALA ASP ARG LEU ILE THR TYR LEU ASP GLN THR THR GLN
SEQRES 19 A 354 LYS SER LEU ILE ALA THR VAL GLU LYS GLN LEU LEU GLY
SEQRES 20 A 354 GLU HIS LEU THR ALA ILE LEU GLN LYS GLY LEU ASN ASN
SEQRES 21 A 354 LEU LEU ASP GLU ASN ARG ILE GLN ASP LEU SER LEU LEU
SEQRES 22 A 354 TYR GLN LEU PHE SER ARG VAL ARG GLY GLY VAL GLN VAL
SEQRES 23 A 354 LEU LEU GLN GLN TRP ILE GLU TYR ILE LYS ALA PHE GLY
SEQRES 24 A 354 SER THR ILE VAL ILE ASN PRO GLU LYS ASP LYS THR MET
SEQRES 25 A 354 ARG GLN GLU LEU ASP ASP PHE LYS ASP LYS VAL ASP HIS
SEQRES 26 A 354 ILE ILE ASP ILE CYS PHE LEU LYS ASN GLU LYS PHE ILE
SEQRES 27 A 354 ASN ALA MET LYS GLU ALA PHE GLU THR PHE ILE ASN LYS
SEQRES 28 A 354 ARG PRO ASN
SEQRES 1 B 354 SER MET PRO LYS LEU PRO GLU ASN TYR THR ASP GLU THR
SEQRES 2 B 354 TRP GLN LYS LEU LYS GLU ALA VAL GLU ALA ILE GLN ASN
SEQRES 3 B 354 SER THR SER ILE LYS TYR ASN LEU GLU GLU LEU TYR GLN
SEQRES 4 B 354 ALA VAL GLU ASN LEU CYS SER TYR LYS ILE SER ALA ASN
SEQRES 5 B 354 LEU TYR LYS GLN LEU ARG GLN ILE CYS GLU ASP HIS ILE
SEQRES 6 B 354 LYS ALA GLN ILE HIS GLN PHE ARG GLU ASP SER LEU ASP
SEQRES 7 B 354 SER VAL LEU PHE LEU LYS LYS ILE ASP ARG CYS TRP GLN
SEQRES 8 B 354 ASN HIS CYS ARG GLN MET ILE MET ILE ARG SER ILE PHE
SEQRES 9 B 354 LEU PHE LEU ASP ARG THR TYR VAL LEU GLN ASN SER MET
SEQRES 10 B 354 LEU PRO SER ILE TRP ASP MET GLY LEU GLU LEU PHE ARG
SEQRES 11 B 354 ALA HIS ILE ILE SER ASP GLN LYS VAL GLN ASN LYS THR
SEQRES 12 B 354 ILE ASP GLY ILE LEU LEU LEU ILE GLU ARG GLU ARG ASN
SEQRES 13 B 354 GLY GLU ALA ILE ASP ARG SER LEU LEU ARG SER LEU LEU
SEQRES 14 B 354 SER MET LEU SER ASP LEU GLN ILE TYR GLN ASP SER PHE
SEQRES 15 B 354 GLU GLN ARG PHE LEU GLU GLU THR ASN ARG LEU TYR ALA
SEQRES 16 B 354 ALA GLU GLY GLN LYS LEU MET GLN GLU ARG GLU VAL PRO
SEQRES 17 B 354 GLU TYR LEU HIS HIS VAL ASN LYS ARG LEU GLU GLU GLU
SEQRES 18 B 354 ALA ASP ARG LEU ILE THR TYR LEU ASP GLN THR THR GLN
SEQRES 19 B 354 LYS SER LEU ILE ALA THR VAL GLU LYS GLN LEU LEU GLY
SEQRES 20 B 354 GLU HIS LEU THR ALA ILE LEU GLN LYS GLY LEU ASN ASN
SEQRES 21 B 354 LEU LEU ASP GLU ASN ARG ILE GLN ASP LEU SER LEU LEU
SEQRES 22 B 354 TYR GLN LEU PHE SER ARG VAL ARG GLY GLY VAL GLN VAL
SEQRES 23 B 354 LEU LEU GLN GLN TRP ILE GLU TYR ILE LYS ALA PHE GLY
SEQRES 24 B 354 SER THR ILE VAL ILE ASN PRO GLU LYS ASP LYS THR MET
SEQRES 25 B 354 ARG GLN GLU LEU ASP ASP PHE LYS ASP LYS VAL ASP HIS
SEQRES 26 B 354 ILE ILE ASP ILE CYS PHE LEU LYS ASN GLU LYS PHE ILE
SEQRES 27 B 354 ASN ALA MET LYS GLU ALA PHE GLU THR PHE ILE ASN LYS
SEQRES 28 B 354 ARG PRO ASN
SEQRES 1 C 354 SER MET PRO LYS LEU PRO GLU ASN TYR THR ASP GLU THR
SEQRES 2 C 354 TRP GLN LYS LEU LYS GLU ALA VAL GLU ALA ILE GLN ASN
SEQRES 3 C 354 SER THR SER ILE LYS TYR ASN LEU GLU GLU LEU TYR GLN
SEQRES 4 C 354 ALA VAL GLU ASN LEU CYS SER TYR LYS ILE SER ALA ASN
SEQRES 5 C 354 LEU TYR LYS GLN LEU ARG GLN ILE CYS GLU ASP HIS ILE
SEQRES 6 C 354 LYS ALA GLN ILE HIS GLN PHE ARG GLU ASP SER LEU ASP
SEQRES 7 C 354 SER VAL LEU PHE LEU LYS LYS ILE ASP ARG CYS TRP GLN
SEQRES 8 C 354 ASN HIS CYS ARG GLN MET ILE MET ILE ARG SER ILE PHE
SEQRES 9 C 354 LEU PHE LEU ASP ARG THR TYR VAL LEU GLN ASN SER MET
SEQRES 10 C 354 LEU PRO SER ILE TRP ASP MET GLY LEU GLU LEU PHE ARG
SEQRES 11 C 354 ALA HIS ILE ILE SER ASP GLN LYS VAL GLN ASN LYS THR
SEQRES 12 C 354 ILE ASP GLY ILE LEU LEU LEU ILE GLU ARG GLU ARG ASN
SEQRES 13 C 354 GLY GLU ALA ILE ASP ARG SER LEU LEU ARG SER LEU LEU
SEQRES 14 C 354 SER MET LEU SER ASP LEU GLN ILE TYR GLN ASP SER PHE
SEQRES 15 C 354 GLU GLN ARG PHE LEU GLU GLU THR ASN ARG LEU TYR ALA
SEQRES 16 C 354 ALA GLU GLY GLN LYS LEU MET GLN GLU ARG GLU VAL PRO
SEQRES 17 C 354 GLU TYR LEU HIS HIS VAL ASN LYS ARG LEU GLU GLU GLU
SEQRES 18 C 354 ALA ASP ARG LEU ILE THR TYR LEU ASP GLN THR THR GLN
SEQRES 19 C 354 LYS SER LEU ILE ALA THR VAL GLU LYS GLN LEU LEU GLY
SEQRES 20 C 354 GLU HIS LEU THR ALA ILE LEU GLN LYS GLY LEU ASN ASN
SEQRES 21 C 354 LEU LEU ASP GLU ASN ARG ILE GLN ASP LEU SER LEU LEU
SEQRES 22 C 354 TYR GLN LEU PHE SER ARG VAL ARG GLY GLY VAL GLN VAL
SEQRES 23 C 354 LEU LEU GLN GLN TRP ILE GLU TYR ILE LYS ALA PHE GLY
SEQRES 24 C 354 SER THR ILE VAL ILE ASN PRO GLU LYS ASP LYS THR MET
SEQRES 25 C 354 ARG GLN GLU LEU ASP ASP PHE LYS ASP LYS VAL ASP HIS
SEQRES 26 C 354 ILE ILE ASP ILE CYS PHE LEU LYS ASN GLU LYS PHE ILE
SEQRES 27 C 354 ASN ALA MET LYS GLU ALA PHE GLU THR PHE ILE ASN LYS
SEQRES 28 C 354 ARG PRO ASN
SEQRES 1 D 354 SER MET PRO LYS LEU PRO GLU ASN TYR THR ASP GLU THR
SEQRES 2 D 354 TRP GLN LYS LEU LYS GLU ALA VAL GLU ALA ILE GLN ASN
SEQRES 3 D 354 SER THR SER ILE LYS TYR ASN LEU GLU GLU LEU TYR GLN
SEQRES 4 D 354 ALA VAL GLU ASN LEU CYS SER TYR LYS ILE SER ALA ASN
SEQRES 5 D 354 LEU TYR LYS GLN LEU ARG GLN ILE CYS GLU ASP HIS ILE
SEQRES 6 D 354 LYS ALA GLN ILE HIS GLN PHE ARG GLU ASP SER LEU ASP
SEQRES 7 D 354 SER VAL LEU PHE LEU LYS LYS ILE ASP ARG CYS TRP GLN
SEQRES 8 D 354 ASN HIS CYS ARG GLN MET ILE MET ILE ARG SER ILE PHE
SEQRES 9 D 354 LEU PHE LEU ASP ARG THR TYR VAL LEU GLN ASN SER MET
SEQRES 10 D 354 LEU PRO SER ILE TRP ASP MET GLY LEU GLU LEU PHE ARG
SEQRES 11 D 354 ALA HIS ILE ILE SER ASP GLN LYS VAL GLN ASN LYS THR
SEQRES 12 D 354 ILE ASP GLY ILE LEU LEU LEU ILE GLU ARG GLU ARG ASN
SEQRES 13 D 354 GLY GLU ALA ILE ASP ARG SER LEU LEU ARG SER LEU LEU
SEQRES 14 D 354 SER MET LEU SER ASP LEU GLN ILE TYR GLN ASP SER PHE
SEQRES 15 D 354 GLU GLN ARG PHE LEU GLU GLU THR ASN ARG LEU TYR ALA
SEQRES 16 D 354 ALA GLU GLY GLN LYS LEU MET GLN GLU ARG GLU VAL PRO
SEQRES 17 D 354 GLU TYR LEU HIS HIS VAL ASN LYS ARG LEU GLU GLU GLU
SEQRES 18 D 354 ALA ASP ARG LEU ILE THR TYR LEU ASP GLN THR THR GLN
SEQRES 19 D 354 LYS SER LEU ILE ALA THR VAL GLU LYS GLN LEU LEU GLY
SEQRES 20 D 354 GLU HIS LEU THR ALA ILE LEU GLN LYS GLY LEU ASN ASN
SEQRES 21 D 354 LEU LEU ASP GLU ASN ARG ILE GLN ASP LEU SER LEU LEU
SEQRES 22 D 354 TYR GLN LEU PHE SER ARG VAL ARG GLY GLY VAL GLN VAL
SEQRES 23 D 354 LEU LEU GLN GLN TRP ILE GLU TYR ILE LYS ALA PHE GLY
SEQRES 24 D 354 SER THR ILE VAL ILE ASN PRO GLU LYS ASP LYS THR MET
SEQRES 25 D 354 ARG GLN GLU LEU ASP ASP PHE LYS ASP LYS VAL ASP HIS
SEQRES 26 D 354 ILE ILE ASP ILE CYS PHE LEU LYS ASN GLU LYS PHE ILE
SEQRES 27 D 354 ASN ALA MET LYS GLU ALA PHE GLU THR PHE ILE ASN LYS
SEQRES 28 D 354 ARG PRO ASN
HET EDO A1534 4
HET EDO A1535 4
HET EDO A1536 4
HET EDO A1537 4
HET EDO B1534 4
HET EDO C1535 4
HET EDO D1533 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 EDO 7(C2 H6 O2)
FORMUL 12 HOH *253(H2 O)
HELIX 1 1 ASP A 196 ASN A 211 1 16
HELIX 2 2 ASN A 218 LYS A 233 1 16
HELIX 3 3 ILE A 234 GLN A 253 1 20
HELIX 4 4 ILE A 254 GLU A 259 5 6
HELIX 5 5 ASP A 263 PHE A 289 1 27
HELIX 6 6 PHE A 289 THR A 295 1 7
HELIX 7 7 SER A 305 ILE A 318 1 14
HELIX 8 8 ASP A 321 ASN A 341 1 21
HELIX 9 9 ASP A 346 LEU A 360 1 15
HELIX 10 10 ILE A 362 PHE A 367 1 6
HELIX 11 11 PHE A 367 ARG A 390 1 24
HELIX 12 12 GLU A 391 TYR A 413 1 23
HELIX 13 13 ASP A 415 THR A 417 5 3
HELIX 14 14 THR A 418 LEU A 431 1 14
HELIX 15 15 HIS A 434 GLU A 449 1 16
HELIX 16 16 ARG A 451 SER A 463 1 13
HELIX 17 17 GLY A 467 ASN A 490 1 24
HELIX 18 18 THR A 496 PHE A 516 1 21
HELIX 19 19 ASN A 519 THR A 532 1 14
HELIX 20 20 ASP B 196 ASN B 211 1 16
HELIX 21 21 ASN B 218 LYS B 233 1 16
HELIX 22 22 ILE B 234 GLN B 253 1 20
HELIX 23 23 ILE B 254 GLU B 259 5 6
HELIX 24 24 ASP B 263 PHE B 289 1 27
HELIX 25 25 PHE B 289 THR B 295 1 7
HELIX 26 26 SER B 305 ILE B 318 1 14
HELIX 27 27 ASP B 321 ASN B 341 1 21
HELIX 28 28 ASP B 346 LEU B 360 1 15
HELIX 29 29 ILE B 362 PHE B 367 1 6
HELIX 30 30 PHE B 367 ARG B 390 1 24
HELIX 31 31 GLU B 391 LEU B 414 1 24
HELIX 32 32 ASP B 415 THR B 417 5 3
HELIX 33 33 THR B 418 LEU B 431 1 14
HELIX 34 34 HIS B 434 GLU B 449 1 16
HELIX 35 35 ARG B 451 SER B 463 1 13
HELIX 36 36 GLY B 467 ASN B 490 1 24
HELIX 37 37 THR B 496 PHE B 516 1 21
HELIX 38 38 ASN B 519 THR B 532 1 14
HELIX 39 39 ASP C 196 SER C 212 1 17
HELIX 40 40 ASN C 218 SER C 231 1 14
HELIX 41 41 ASN C 237 GLN C 253 1 17
HELIX 42 42 ILE C 254 GLU C 259 5 6
HELIX 43 43 ASP C 263 PHE C 289 1 27
HELIX 44 44 PHE C 289 LEU C 298 1 10
HELIX 45 45 SER C 305 ILE C 318 1 14
HELIX 46 46 ASP C 321 ASN C 341 1 21
HELIX 47 47 ASP C 346 LEU C 360 1 15
HELIX 48 48 ILE C 362 PHE C 367 1 6
HELIX 49 49 PHE C 367 ARG C 390 1 24
HELIX 50 50 GLU C 391 LEU C 414 1 24
HELIX 51 51 ASP C 415 THR C 417 5 3
HELIX 52 52 THR C 418 LEU C 431 1 14
HELIX 53 53 HIS C 434 GLU C 449 1 16
HELIX 54 54 ARG C 451 SER C 463 1 13
HELIX 55 55 GLY C 467 ASN C 490 1 24
HELIX 56 56 THR C 496 CYS C 515 1 20
HELIX 57 57 ASN C 519 GLU C 531 1 13
HELIX 58 58 ASP D 196 ASN D 211 1 16
HELIX 59 59 ASN D 218 CYS D 230 1 13
HELIX 60 60 ASN D 237 GLN D 253 1 17
HELIX 61 61 ILE D 254 GLU D 259 5 6
HELIX 62 62 ASP D 263 PHE D 289 1 27
HELIX 63 63 PHE D 289 GLN D 299 1 11
HELIX 64 64 SER D 305 ILE D 318 1 14
HELIX 65 65 ASP D 321 ASN D 341 1 21
HELIX 66 66 ASP D 346 LEU D 360 1 15
HELIX 67 67 ILE D 362 PHE D 367 1 6
HELIX 68 68 PHE D 367 ARG D 390 1 24
HELIX 69 69 GLU D 391 LEU D 414 1 24
HELIX 70 70 ASP D 415 THR D 417 5 3
HELIX 71 71 THR D 418 LEU D 431 1 14
HELIX 72 72 HIS D 434 GLU D 449 1 16
HELIX 73 73 ARG D 451 SER D 463 1 13
HELIX 74 74 GLY D 467 ILE D 489 1 23
HELIX 75 75 GLU D 500 CYS D 515 1 16
HELIX 76 76 ASN D 519 GLU D 531 1 13
CISPEP 1 ASP A 260 SER A 261 0 2.03
CISPEP 2 ASP B 260 SER B 261 0 2.91
SITE 1 AC1 3 ARG A 243 GLU A 312 ALA A 316
SITE 1 AC2 5 ILE A 345 ASP A 346 ARG A 347 GLN B 460
SITE 2 AC2 5 SER B 463
SITE 1 AC3 3 ASP A 272 GLN A 276 SER A 348
SITE 1 AC4 5 GLN A 210 ILE A 250 HIS A 278 GLN A 281
SITE 2 AC4 5 MET A 282
SITE 1 AC5 5 GLN B 210 ILE B 250 HIS B 278 GLN B 281
SITE 2 AC5 5 MET B 282
SITE 1 AC6 4 ARG C 243 GLU C 247 ALA C 316 LYS D 323
SITE 1 AC7 5 GLN C 460 ILE D 345 ASP D 346 ARG D 347
SITE 2 AC7 5 SER D 348
CRYST1 64.248 157.091 92.916 90.00 95.71 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015565 0.000000 0.001556 0.00000
SCALE2 0.000000 0.006366 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010816 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
