HEADER UNKNOWN FUNCTION 11-JUL-08 3DRY
TITLE X-RAY CRYSTAL STRUCTURE OF HUMAN KCTD5 PROTEIN CRYSTALLIZED IN LOW-
TITLE 2 SALT BUFFER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BTB/POZ DOMAIN-CONTAINING PROTEIN KCTD5;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 FRAGMENT: UNP RESIDUES 34-234;
COMPND 5 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: KCTD5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET28A;
SOURCE 10 OTHER_DETAILS: MODIFIED VECTOR, TEV PROTEASE CLEAVAGE SITE REPLACING
SOURCE 11 THROMBIN SITE
KEYWDS KCTD5, BTB/POZ, GOLGI, GRASP55, POTASSIUM CHANNEL DOMAIN T1,
KEYWDS 2 PENTAMERIC ASSEMBLY, HOST-VIRUS INTERACTION, NUCLEUS, UNKNOWN
KEYWDS 3 FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR V.TERESHKO,I.DEMENTIEVA,S.A.N.GOLDSTEIN
REVDAT 4 30-AUG-23 3DRY 1 SEQADV
REVDAT 3 13-JUL-11 3DRY 1 VERSN
REVDAT 2 05-MAY-09 3DRY 1 JRNL
REVDAT 1 17-FEB-09 3DRY 0
JRNL AUTH I.S.DEMENTIEVA,V.TERESHKO,Z.A.MCCROSSAN,E.SOLOMAHA,D.ARAKI,
JRNL AUTH 2 C.XU,N.GRIGORIEFF,S.A.GOLDSTEIN
JRNL TITL PENTAMERIC ASSEMBLY OF POTASSIUM CHANNEL TETRAMERIZATION
JRNL TITL 2 DOMAIN-CONTAINING PROTEIN 5.
JRNL REF J.MOL.BIOL. V. 387 175 2009
JRNL REFN ISSN 0022-2836
JRNL PMID 19361449
JRNL DOI 10.1016/J.JMB.2009.01.030
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 16774
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) : 0.260
REMARK 3 R VALUE (WORKING SET) : 0.253
REMARK 3 FREE R VALUE : 0.308
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1913
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) : 3.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.38
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1151
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.47
REMARK 3 BIN R VALUE (WORKING SET) : 0.3610
REMARK 3 BIN FREE R VALUE SET COUNT : 140
REMARK 3 BIN FREE R VALUE : 0.4150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6810
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 73.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.94000
REMARK 3 B22 (A**2) : -4.73000
REMARK 3 B33 (A**2) : 13.67000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.738
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.636
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 86.335
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.901
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.825
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6940 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4777 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9379 ; 1.276 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11638 ; 0.941 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 835 ; 6.843 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 338 ;36.470 ;24.497
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1277 ;19.233 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 47 ;17.817 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1052 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7619 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1374 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1839 ; 0.232 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5002 ; 0.190 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3279 ; 0.186 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 3687 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 196 ; 0.166 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 2 ; 0.070 ; 0.200
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): 24 ; 0.196 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 59 ; 0.213 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.210 ; 0.200
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): 5472 ; 0.373 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1700 ; 0.051 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6810 ; 0.428 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3191 ; 0.478 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2569 ; 0.743 ; 4.500
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 : 3
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 45 A 95 4
REMARK 3 1 B 45 B 95 4
REMARK 3 1 C 45 C 95 4
REMARK 3 1 D 45 D 95 4
REMARK 3 1 E 45 E 95 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 714 ; 0.33 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 714 ; 0.38 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 714 ; 0.51 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 D (A): 714 ; 0.44 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 E (A): 714 ; 0.43 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 714 ; 0.17 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 714 ; 0.22 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 714 ; 0.27 ; 2.00
REMARK 3 MEDIUM THERMAL 1 D (A**2): 714 ; 0.31 ; 2.00
REMARK 3 MEDIUM THERMAL 1 E (A**2): 714 ; 0.20 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B C D E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 96 A 145 4
REMARK 3 1 B 96 B 145 4
REMARK 3 1 C 96 C 145 4
REMARK 3 1 D 96 D 145 4
REMARK 3 1 E 96 E 145 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 709 ; 0.32 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 B (A): 709 ; 0.31 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 C (A): 709 ; 0.32 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 D (A): 709 ; 0.37 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 E (A): 709 ; 0.33 ; 0.50
REMARK 3 MEDIUM THERMAL 2 A (A**2): 709 ; 0.15 ; 2.00
REMARK 3 MEDIUM THERMAL 2 B (A**2): 709 ; 0.15 ; 2.00
REMARK 3 MEDIUM THERMAL 2 C (A**2): 709 ; 0.18 ; 2.00
REMARK 3 MEDIUM THERMAL 2 D (A**2): 709 ; 0.22 ; 2.00
REMARK 3 MEDIUM THERMAL 2 E (A**2): 709 ; 0.16 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B C D E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 155 A 187 4
REMARK 3 1 B 155 B 187 4
REMARK 3 1 C 155 C 187 4
REMARK 3 1 D 155 D 187 4
REMARK 3 1 E 155 E 187 4
REMARK 3 2 A 200 A 210 4
REMARK 3 2 B 200 B 210 4
REMARK 3 2 C 200 C 210 4
REMARK 3 2 D 200 D 210 4
REMARK 3 2 E 200 E 210 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 A (A): 598 ; 0.55 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 B (A): 598 ; 0.47 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 C (A): 598 ; 0.48 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 D (A): 598 ; 0.49 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 E (A): 598 ; 0.47 ; 0.50
REMARK 3 MEDIUM THERMAL 3 A (A**2): 598 ; 0.26 ; 2.00
REMARK 3 MEDIUM THERMAL 3 B (A**2): 598 ; 0.22 ; 2.00
REMARK 3 MEDIUM THERMAL 3 C (A**2): 598 ; 0.25 ; 2.00
REMARK 3 MEDIUM THERMAL 3 D (A**2): 598 ; 0.18 ; 2.00
REMARK 3 MEDIUM THERMAL 3 E (A**2): 598 ; 0.18 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 5
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 40 A 95
REMARK 3 RESIDUE RANGE : B 42 B 95
REMARK 3 RESIDUE RANGE : C 33 C 95
REMARK 3 RESIDUE RANGE : D 34 D 95
REMARK 3 RESIDUE RANGE : E 42 E 95
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0071 12.0171 26.7950
REMARK 3 T TENSOR
REMARK 3 T11: -0.2308 T22: -0.2114
REMARK 3 T33: -0.8865 T12: -0.0161
REMARK 3 T13: 0.1036 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 4.2319 L22: 3.5736
REMARK 3 L33: 0.8118 L12: -0.2036
REMARK 3 L13: -0.1425 L23: 0.1552
REMARK 3 S TENSOR
REMARK 3 S11: -0.0382 S12: -0.6276 S13: -0.2981
REMARK 3 S21: 0.4279 S22: 0.0365 S23: 0.5241
REMARK 3 S31: 0.0643 S32: 0.0164 S33: 0.0017
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 5
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 96 A 150
REMARK 3 RESIDUE RANGE : B 96 B 150
REMARK 3 RESIDUE RANGE : C 96 C 150
REMARK 3 RESIDUE RANGE : D 96 D 150
REMARK 3 RESIDUE RANGE : E 96 E 150
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9964 10.7935 7.7206
REMARK 3 T TENSOR
REMARK 3 T11: 0.0020 T22: -0.0353
REMARK 3 T33: -0.6647 T12: 0.0210
REMARK 3 T13: -0.1112 T23: -0.0566
REMARK 3 L TENSOR
REMARK 3 L11: 3.4602 L22: 4.0712
REMARK 3 L33: 0.5133 L12: -0.9100
REMARK 3 L13: 0.0222 L23: -0.0755
REMARK 3 S TENSOR
REMARK 3 S11: 0.0993 S12: 0.7390 S13: -0.4566
REMARK 3 S21: -0.8648 S22: -0.3136 S23: 0.7033
REMARK 3 S31: -0.0479 S32: -0.1714 S33: 0.2143
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 5
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 151 A 210
REMARK 3 RESIDUE RANGE : B 151 B 210
REMARK 3 RESIDUE RANGE : C 151 C 210
REMARK 3 RESIDUE RANGE : D 151 D 210
REMARK 3 RESIDUE RANGE : E 151 E 210
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6996 9.5422 -36.7865
REMARK 3 T TENSOR
REMARK 3 T11: -0.1096 T22: -0.0261
REMARK 3 T33: -0.8354 T12: 0.0462
REMARK 3 T13: -0.1050 T23: -0.1814
REMARK 3 L TENSOR
REMARK 3 L11: 6.3021 L22: 5.8687
REMARK 3 L33: 2.3121 L12: -2.2750
REMARK 3 L13: -1.8384 L23: 1.0636
REMARK 3 S TENSOR
REMARK 3 S11: 0.1710 S12: 0.3340 S13: -0.2374
REMARK 3 S21: -0.1128 S22: -0.0193 S23: -0.0870
REMARK 3 S31: 0.2033 S32: 0.0300 S33: -0.1517
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
REMARK 4
REMARK 4 3DRY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUL-08.
REMARK 100 THE DEPOSITION ID IS D_1000048412.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI (111)
REMARK 200 OPTICS : ADJUSTABLE FOCUSING MIRRORS K-B
REMARK 200 GEOMETRY
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20180
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.1400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.51000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3DRX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M PROLINE, 100 MM HEPES, 7% (W/V)
REMARK 280 PEG 3350, PH 7.5, VAPOR DIFFUSION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 51.49500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.08700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.39550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.08700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 51.49500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.39550
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 33
REMARK 465 ALA A 34
REMARK 465 LEU A 35
REMARK 465 ALA A 36
REMARK 465 GLN A 37
REMARK 465 ARG A 38
REMARK 465 PRO A 39
REMARK 465 TYR A 191
REMARK 465 ASN A 192
REMARK 465 TYR A 193
REMARK 465 GLY A 194
REMARK 465 ASN A 195
REMARK 465 ASN A 211
REMARK 465 THR A 212
REMARK 465 PRO A 213
REMARK 465 TYR A 214
REMARK 465 GLY A 215
REMARK 465 THR A 216
REMARK 465 ALA A 217
REMARK 465 SER A 218
REMARK 465 GLU A 219
REMARK 465 PRO A 220
REMARK 465 SER A 221
REMARK 465 GLU A 222
REMARK 465 LYS A 223
REMARK 465 ALA A 224
REMARK 465 LYS A 225
REMARK 465 ILE A 226
REMARK 465 LEU A 227
REMARK 465 GLN A 228
REMARK 465 GLU A 229
REMARK 465 ARG A 230
REMARK 465 GLY A 231
REMARK 465 SER A 232
REMARK 465 ARG A 233
REMARK 465 MET A 234
REMARK 465 SER B 33
REMARK 465 ALA B 34
REMARK 465 LEU B 35
REMARK 465 ALA B 36
REMARK 465 GLN B 37
REMARK 465 ARG B 38
REMARK 465 PRO B 39
REMARK 465 GLY B 40
REMARK 465 SER B 41
REMARK 465 TYR B 191
REMARK 465 ASN B 192
REMARK 465 TYR B 193
REMARK 465 GLY B 194
REMARK 465 ASN B 195
REMARK 465 ASN B 211
REMARK 465 THR B 212
REMARK 465 PRO B 213
REMARK 465 TYR B 214
REMARK 465 GLY B 215
REMARK 465 THR B 216
REMARK 465 ALA B 217
REMARK 465 SER B 218
REMARK 465 GLU B 219
REMARK 465 PRO B 220
REMARK 465 SER B 221
REMARK 465 GLU B 222
REMARK 465 LYS B 223
REMARK 465 ALA B 224
REMARK 465 LYS B 225
REMARK 465 ILE B 226
REMARK 465 LEU B 227
REMARK 465 GLN B 228
REMARK 465 GLU B 229
REMARK 465 ARG B 230
REMARK 465 GLY B 231
REMARK 465 SER B 232
REMARK 465 ARG B 233
REMARK 465 MET B 234
REMARK 465 ASN C 211
REMARK 465 THR C 212
REMARK 465 PRO C 213
REMARK 465 TYR C 214
REMARK 465 GLY C 215
REMARK 465 THR C 216
REMARK 465 ALA C 217
REMARK 465 SER C 218
REMARK 465 GLU C 219
REMARK 465 PRO C 220
REMARK 465 SER C 221
REMARK 465 GLU C 222
REMARK 465 LYS C 223
REMARK 465 ALA C 224
REMARK 465 LYS C 225
REMARK 465 ILE C 226
REMARK 465 LEU C 227
REMARK 465 GLN C 228
REMARK 465 GLU C 229
REMARK 465 ARG C 230
REMARK 465 GLY C 231
REMARK 465 SER C 232
REMARK 465 ARG C 233
REMARK 465 MET C 234
REMARK 465 SER D 33
REMARK 465 TYR D 191
REMARK 465 ASN D 192
REMARK 465 TYR D 193
REMARK 465 GLY D 194
REMARK 465 ASN D 195
REMARK 465 ASN D 211
REMARK 465 THR D 212
REMARK 465 PRO D 213
REMARK 465 TYR D 214
REMARK 465 GLY D 215
REMARK 465 THR D 216
REMARK 465 ALA D 217
REMARK 465 SER D 218
REMARK 465 GLU D 219
REMARK 465 PRO D 220
REMARK 465 SER D 221
REMARK 465 GLU D 222
REMARK 465 LYS D 223
REMARK 465 ALA D 224
REMARK 465 LYS D 225
REMARK 465 ILE D 226
REMARK 465 LEU D 227
REMARK 465 GLN D 228
REMARK 465 GLU D 229
REMARK 465 ARG D 230
REMARK 465 GLY D 231
REMARK 465 SER D 232
REMARK 465 ARG D 233
REMARK 465 MET D 234
REMARK 465 SER E 33
REMARK 465 ALA E 34
REMARK 465 LEU E 35
REMARK 465 ALA E 36
REMARK 465 GLN E 37
REMARK 465 ARG E 38
REMARK 465 PRO E 39
REMARK 465 GLY E 40
REMARK 465 SER E 41
REMARK 465 TYR E 191
REMARK 465 ASN E 192
REMARK 465 TYR E 193
REMARK 465 GLY E 194
REMARK 465 ASN E 195
REMARK 465 ASN E 211
REMARK 465 THR E 212
REMARK 465 PRO E 213
REMARK 465 TYR E 214
REMARK 465 GLY E 215
REMARK 465 THR E 216
REMARK 465 ALA E 217
REMARK 465 SER E 218
REMARK 465 GLU E 219
REMARK 465 PRO E 220
REMARK 465 SER E 221
REMARK 465 GLU E 222
REMARK 465 LYS E 223
REMARK 465 ALA E 224
REMARK 465 LYS E 225
REMARK 465 ILE E 226
REMARK 465 LEU E 227
REMARK 465 GLN E 228
REMARK 465 GLU E 229
REMARK 465 ARG E 230
REMARK 465 GLY E 231
REMARK 465 SER E 232
REMARK 465 ARG E 233
REMARK 465 MET E 234
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 SER A 190 C SER A 190 O 0.219
REMARK 500 ASN C 192 CG ASN C 192 OD1 0.157
REMARK 500 ASN C 192 C ASN C 192 O 0.134
REMARK 500 GLU C 208 CD GLU C 208 OE1 0.070
REMARK 500 GLU C 208 CD GLU C 208 OE2 0.093
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 SER A 43 85.24 -67.22
REMARK 500 ASN A 49 50.64 -99.22
REMARK 500 ALA A 76 60.04 62.05
REMARK 500 THR A 87 -3.43 -58.56
REMARK 500 ASP A 93 48.61 -87.75
REMARK 500 ASN A 130 79.35 71.71
REMARK 500 GLN A 162 113.20 -162.35
REMARK 500 MET A 175 140.51 -29.32
REMARK 500 GLU A 182 -61.92 -131.92
REMARK 500 ILE A 187 69.15 -105.09
REMARK 500 SER A 189 71.79 26.72
REMARK 500 ASP A 197 -67.17 -166.72
REMARK 500 GLN A 198 -155.30 49.22
REMARK 500 CYS A 203 131.91 -176.89
REMARK 500 CYS B 63 16.47 -142.53
REMARK 500 CYS B 74 -43.14 -26.41
REMARK 500 ASP B 83 25.35 -77.62
REMARK 500 ASP B 93 61.68 -66.57
REMARK 500 LEU B 106 -4.72 -58.82
REMARK 500 ASN B 130 76.97 70.70
REMARK 500 SER B 147 1.49 -64.38
REMARK 500 SER B 150 114.51 -32.93
REMARK 500 MET B 175 127.79 -33.47
REMARK 500 SER B 176 -179.66 -57.86
REMARK 500 SER B 189 72.08 -106.73
REMARK 500 GLN B 198 -153.96 37.98
REMARK 500 CYS B 203 120.36 175.45
REMARK 500 LEU B 209 55.61 -140.91
REMARK 500 ALA C 34 98.74 4.65
REMARK 500 GLN C 37 -166.72 -72.37
REMARK 500 PRO C 39 -26.27 -39.44
REMARK 500 SER C 43 151.45 -20.91
REMARK 500 ASN C 49 58.74 -118.65
REMARK 500 VAL C 50 84.88 -65.82
REMARK 500 ARG C 59 -39.76 -38.61
REMARK 500 CYS C 63 30.90 -89.66
REMARK 500 ASP C 85 -124.58 -106.07
REMARK 500 ASN C 130 82.81 71.28
REMARK 500 VAL C 154 88.34 39.49
REMARK 500 LYS C 155 79.49 -68.18
REMARK 500 GLU C 166 -19.78 -44.83
REMARK 500 THR C 174 44.93 -100.57
REMARK 500 SER C 190 61.75 153.90
REMARK 500 TYR C 191 -163.96 65.88
REMARK 500 ASN C 192 -138.61 -102.06
REMARK 500 TYR C 193 -81.65 -130.72
REMARK 500 ASN C 195 24.21 -75.75
REMARK 500 GLU C 196 -149.58 -162.16
REMARK 500 ASP C 197 166.25 128.61
REMARK 500 ALA C 199 -92.39 -42.58
REMARK 500
REMARK 500 THIS ENTRY HAS 93 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN C 151 VAL C 152 147.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DRX RELATED DB: PDB
REMARK 900 KCTD5 PROTEIN CRYSTALLIZED IN HIGH-SALT BUFFER
REMARK 900 RELATED ID: 3DRZ RELATED DB: PDB
REMARK 900 N-TERMINAL BTB DOMAIN OF HUMAN KCTD5 PROTEIN
DBREF 3DRY A 34 234 UNP Q9NXV2 KCTD5_HUMAN 34 234
DBREF 3DRY B 34 234 UNP Q9NXV2 KCTD5_HUMAN 34 234
DBREF 3DRY C 34 234 UNP Q9NXV2 KCTD5_HUMAN 34 234
DBREF 3DRY D 34 234 UNP Q9NXV2 KCTD5_HUMAN 34 234
DBREF 3DRY E 34 234 UNP Q9NXV2 KCTD5_HUMAN 34 234
SEQADV 3DRY SER A 33 UNP Q9NXV2 EXPRESSION TAG
SEQADV 3DRY SER B 33 UNP Q9NXV2 EXPRESSION TAG
SEQADV 3DRY SER C 33 UNP Q9NXV2 EXPRESSION TAG
SEQADV 3DRY SER D 33 UNP Q9NXV2 EXPRESSION TAG
SEQADV 3DRY SER E 33 UNP Q9NXV2 EXPRESSION TAG
SEQRES 1 A 202 SER ALA LEU ALA GLN ARG PRO GLY SER VAL SER LYS TRP
SEQRES 2 A 202 VAL ARG LEU ASN VAL GLY GLY THR TYR PHE LEU THR THR
SEQRES 3 A 202 ARG GLN THR LEU CYS ARG ASP PRO LYS SER PHE LEU TYR
SEQRES 4 A 202 ARG LEU CYS GLN ALA ASP PRO ASP LEU ASP SER ASP LYS
SEQRES 5 A 202 ASP GLU THR GLY ALA TYR LEU ILE ASP ARG ASP PRO THR
SEQRES 6 A 202 TYR PHE GLY PRO VAL LEU ASN TYR LEU ARG HIS GLY LYS
SEQRES 7 A 202 LEU VAL ILE ASN LYS ASP LEU ALA GLU GLU GLY VAL LEU
SEQRES 8 A 202 GLU GLU ALA GLU PHE TYR ASN ILE THR SER LEU ILE LYS
SEQRES 9 A 202 LEU VAL LYS ASP LYS ILE ARG GLU ARG ASP SER LYS THR
SEQRES 10 A 202 SER GLN VAL PRO VAL LYS HIS VAL TYR ARG VAL LEU GLN
SEQRES 11 A 202 CYS GLN GLU GLU GLU LEU THR GLN MET VAL SER THR MET
SEQRES 12 A 202 SER ASP GLY TRP LYS PHE GLU GLN LEU VAL SER ILE GLY
SEQRES 13 A 202 SER SER TYR ASN TYR GLY ASN GLU ASP GLN ALA GLU PHE
SEQRES 14 A 202 LEU CYS VAL VAL SER LYS GLU LEU HIS ASN THR PRO TYR
SEQRES 15 A 202 GLY THR ALA SER GLU PRO SER GLU LYS ALA LYS ILE LEU
SEQRES 16 A 202 GLN GLU ARG GLY SER ARG MET
SEQRES 1 B 202 SER ALA LEU ALA GLN ARG PRO GLY SER VAL SER LYS TRP
SEQRES 2 B 202 VAL ARG LEU ASN VAL GLY GLY THR TYR PHE LEU THR THR
SEQRES 3 B 202 ARG GLN THR LEU CYS ARG ASP PRO LYS SER PHE LEU TYR
SEQRES 4 B 202 ARG LEU CYS GLN ALA ASP PRO ASP LEU ASP SER ASP LYS
SEQRES 5 B 202 ASP GLU THR GLY ALA TYR LEU ILE ASP ARG ASP PRO THR
SEQRES 6 B 202 TYR PHE GLY PRO VAL LEU ASN TYR LEU ARG HIS GLY LYS
SEQRES 7 B 202 LEU VAL ILE ASN LYS ASP LEU ALA GLU GLU GLY VAL LEU
SEQRES 8 B 202 GLU GLU ALA GLU PHE TYR ASN ILE THR SER LEU ILE LYS
SEQRES 9 B 202 LEU VAL LYS ASP LYS ILE ARG GLU ARG ASP SER LYS THR
SEQRES 10 B 202 SER GLN VAL PRO VAL LYS HIS VAL TYR ARG VAL LEU GLN
SEQRES 11 B 202 CYS GLN GLU GLU GLU LEU THR GLN MET VAL SER THR MET
SEQRES 12 B 202 SER ASP GLY TRP LYS PHE GLU GLN LEU VAL SER ILE GLY
SEQRES 13 B 202 SER SER TYR ASN TYR GLY ASN GLU ASP GLN ALA GLU PHE
SEQRES 14 B 202 LEU CYS VAL VAL SER LYS GLU LEU HIS ASN THR PRO TYR
SEQRES 15 B 202 GLY THR ALA SER GLU PRO SER GLU LYS ALA LYS ILE LEU
SEQRES 16 B 202 GLN GLU ARG GLY SER ARG MET
SEQRES 1 C 202 SER ALA LEU ALA GLN ARG PRO GLY SER VAL SER LYS TRP
SEQRES 2 C 202 VAL ARG LEU ASN VAL GLY GLY THR TYR PHE LEU THR THR
SEQRES 3 C 202 ARG GLN THR LEU CYS ARG ASP PRO LYS SER PHE LEU TYR
SEQRES 4 C 202 ARG LEU CYS GLN ALA ASP PRO ASP LEU ASP SER ASP LYS
SEQRES 5 C 202 ASP GLU THR GLY ALA TYR LEU ILE ASP ARG ASP PRO THR
SEQRES 6 C 202 TYR PHE GLY PRO VAL LEU ASN TYR LEU ARG HIS GLY LYS
SEQRES 7 C 202 LEU VAL ILE ASN LYS ASP LEU ALA GLU GLU GLY VAL LEU
SEQRES 8 C 202 GLU GLU ALA GLU PHE TYR ASN ILE THR SER LEU ILE LYS
SEQRES 9 C 202 LEU VAL LYS ASP LYS ILE ARG GLU ARG ASP SER LYS THR
SEQRES 10 C 202 SER GLN VAL PRO VAL LYS HIS VAL TYR ARG VAL LEU GLN
SEQRES 11 C 202 CYS GLN GLU GLU GLU LEU THR GLN MET VAL SER THR MET
SEQRES 12 C 202 SER ASP GLY TRP LYS PHE GLU GLN LEU VAL SER ILE GLY
SEQRES 13 C 202 SER SER TYR ASN TYR GLY ASN GLU ASP GLN ALA GLU PHE
SEQRES 14 C 202 LEU CYS VAL VAL SER LYS GLU LEU HIS ASN THR PRO TYR
SEQRES 15 C 202 GLY THR ALA SER GLU PRO SER GLU LYS ALA LYS ILE LEU
SEQRES 16 C 202 GLN GLU ARG GLY SER ARG MET
SEQRES 1 D 202 SER ALA LEU ALA GLN ARG PRO GLY SER VAL SER LYS TRP
SEQRES 2 D 202 VAL ARG LEU ASN VAL GLY GLY THR TYR PHE LEU THR THR
SEQRES 3 D 202 ARG GLN THR LEU CYS ARG ASP PRO LYS SER PHE LEU TYR
SEQRES 4 D 202 ARG LEU CYS GLN ALA ASP PRO ASP LEU ASP SER ASP LYS
SEQRES 5 D 202 ASP GLU THR GLY ALA TYR LEU ILE ASP ARG ASP PRO THR
SEQRES 6 D 202 TYR PHE GLY PRO VAL LEU ASN TYR LEU ARG HIS GLY LYS
SEQRES 7 D 202 LEU VAL ILE ASN LYS ASP LEU ALA GLU GLU GLY VAL LEU
SEQRES 8 D 202 GLU GLU ALA GLU PHE TYR ASN ILE THR SER LEU ILE LYS
SEQRES 9 D 202 LEU VAL LYS ASP LYS ILE ARG GLU ARG ASP SER LYS THR
SEQRES 10 D 202 SER GLN VAL PRO VAL LYS HIS VAL TYR ARG VAL LEU GLN
SEQRES 11 D 202 CYS GLN GLU GLU GLU LEU THR GLN MET VAL SER THR MET
SEQRES 12 D 202 SER ASP GLY TRP LYS PHE GLU GLN LEU VAL SER ILE GLY
SEQRES 13 D 202 SER SER TYR ASN TYR GLY ASN GLU ASP GLN ALA GLU PHE
SEQRES 14 D 202 LEU CYS VAL VAL SER LYS GLU LEU HIS ASN THR PRO TYR
SEQRES 15 D 202 GLY THR ALA SER GLU PRO SER GLU LYS ALA LYS ILE LEU
SEQRES 16 D 202 GLN GLU ARG GLY SER ARG MET
SEQRES 1 E 202 SER ALA LEU ALA GLN ARG PRO GLY SER VAL SER LYS TRP
SEQRES 2 E 202 VAL ARG LEU ASN VAL GLY GLY THR TYR PHE LEU THR THR
SEQRES 3 E 202 ARG GLN THR LEU CYS ARG ASP PRO LYS SER PHE LEU TYR
SEQRES 4 E 202 ARG LEU CYS GLN ALA ASP PRO ASP LEU ASP SER ASP LYS
SEQRES 5 E 202 ASP GLU THR GLY ALA TYR LEU ILE ASP ARG ASP PRO THR
SEQRES 6 E 202 TYR PHE GLY PRO VAL LEU ASN TYR LEU ARG HIS GLY LYS
SEQRES 7 E 202 LEU VAL ILE ASN LYS ASP LEU ALA GLU GLU GLY VAL LEU
SEQRES 8 E 202 GLU GLU ALA GLU PHE TYR ASN ILE THR SER LEU ILE LYS
SEQRES 9 E 202 LEU VAL LYS ASP LYS ILE ARG GLU ARG ASP SER LYS THR
SEQRES 10 E 202 SER GLN VAL PRO VAL LYS HIS VAL TYR ARG VAL LEU GLN
SEQRES 11 E 202 CYS GLN GLU GLU GLU LEU THR GLN MET VAL SER THR MET
SEQRES 12 E 202 SER ASP GLY TRP LYS PHE GLU GLN LEU VAL SER ILE GLY
SEQRES 13 E 202 SER SER TYR ASN TYR GLY ASN GLU ASP GLN ALA GLU PHE
SEQRES 14 E 202 LEU CYS VAL VAL SER LYS GLU LEU HIS ASN THR PRO TYR
SEQRES 15 E 202 GLY THR ALA SER GLU PRO SER GLU LYS ALA LYS ILE LEU
SEQRES 16 E 202 GLN GLU ARG GLY SER ARG MET
HELIX 1 1 GLN A 60 CYS A 63 5 4
HELIX 2 2 PHE A 69 GLN A 75 1 7
HELIX 3 3 ASP A 77 LYS A 84 5 8
HELIX 4 4 ASP A 95 GLY A 109 1 15
HELIX 5 5 ALA A 118 ASN A 130 1 13
HELIX 6 6 ILE A 131 ASP A 146 1 16
HELIX 7 7 GLN A 164 GLU A 166 5 3
HELIX 8 8 GLU A 167 MET A 175 1 9
HELIX 9 9 GLN B 60 ARG B 64 5 5
HELIX 10 10 PHE B 69 GLN B 75 1 7
HELIX 11 11 ASP B 95 GLY B 109 1 15
HELIX 12 12 ALA B 118 ASN B 130 1 13
HELIX 13 13 ILE B 131 SER B 147 1 17
HELIX 14 14 LYS B 148 SER B 150 5 3
HELIX 15 15 GLU B 167 MET B 175 1 9
HELIX 16 16 GLN C 60 ASP C 65 5 6
HELIX 17 17 LEU C 70 GLN C 75 1 6
HELIX 18 18 ALA C 76 ASP C 81 5 6
HELIX 19 19 ASP C 95 GLY C 109 1 15
HELIX 20 20 ALA C 118 ASN C 130 1 13
HELIX 21 21 ILE C 131 SER C 150 1 20
HELIX 22 22 GLN C 164 GLU C 166 5 3
HELIX 23 23 GLU C 167 THR C 174 1 8
HELIX 24 24 ARG D 59 CYS D 63 1 5
HELIX 25 25 LEU D 70 GLN D 75 1 6
HELIX 26 26 ASP D 77 ASP D 81 5 5
HELIX 27 27 ASP D 95 GLY D 109 1 15
HELIX 28 28 ALA D 118 ASN D 130 1 13
HELIX 29 29 ILE D 131 SER D 147 1 17
HELIX 30 30 GLU D 167 THR D 174 1 8
HELIX 31 31 GLN E 60 LEU E 62 5 3
HELIX 32 32 LEU E 70 ALA E 76 1 7
HELIX 33 33 ASP E 77 ASP E 81 5 5
HELIX 34 34 ASP E 95 GLY E 109 1 15
HELIX 35 35 ALA E 118 ASN E 130 1 13
HELIX 36 36 ILE E 131 ASP E 146 1 16
HELIX 37 37 GLU E 167 THR E 174 1 8
SHEET 1 A 3 PHE A 55 THR A 58 0
SHEET 2 A 3 TRP A 45 VAL A 50 -1 N LEU A 48 O PHE A 55
SHEET 3 A 3 TYR A 90 ILE A 92 1 O TYR A 90 N ASN A 49
SHEET 1 B 3 HIS A 156 LEU A 161 0
SHEET 2 B 3 CYS A 203 GLU A 208 -1 O CYS A 203 N LEU A 161
SHEET 3 B 3 LYS A 180 GLN A 183 -1 N LYS A 180 O SER A 206
SHEET 1 C 3 THR B 53 THR B 58 0
SHEET 2 C 3 TRP B 45 VAL B 50 -1 N VAL B 46 O THR B 57
SHEET 3 C 3 TYR B 90 ILE B 92 1 O TYR B 90 N ASN B 49
SHEET 1 D 3 VAL B 157 CYS B 163 0
SHEET 2 D 3 PHE B 201 LYS B 207 -1 O CYS B 203 N LEU B 161
SHEET 3 D 3 LYS B 180 SER B 186 -1 N LYS B 180 O SER B 206
SHEET 1 E 3 PHE C 55 THR C 58 0
SHEET 2 E 3 TRP C 45 VAL C 50 -1 N VAL C 46 O THR C 57
SHEET 3 E 3 TYR C 90 ILE C 92 1 O TYR C 90 N ASN C 49
SHEET 1 F 3 VAL C 157 CYS C 163 0
SHEET 2 F 3 PHE C 201 LYS C 207 -1 O CYS C 203 N LEU C 161
SHEET 3 F 3 LYS C 180 SER C 186 -1 N LYS C 180 O SER C 206
SHEET 1 G 3 PHE D 55 THR D 58 0
SHEET 2 G 3 TRP D 45 VAL D 50 -1 N VAL D 46 O THR D 57
SHEET 3 G 3 TYR D 90 ILE D 92 1 O TYR D 90 N ASN D 49
SHEET 1 H 3 HIS D 156 CYS D 163 0
SHEET 2 H 3 PHE D 201 GLU D 208 -1 O CYS D 203 N LEU D 161
SHEET 3 H 3 LYS D 180 GLN D 183 -1 N GLN D 183 O VAL D 204
SHEET 1 I 2 TRP E 45 ARG E 47 0
SHEET 2 I 2 LEU E 56 THR E 58 -1 O THR E 57 N VAL E 46
SHEET 1 J 3 ARG E 159 CYS E 163 0
SHEET 2 J 3 PHE E 201 VAL E 205 -1 O PHE E 201 N CYS E 163
SHEET 3 J 3 PHE E 181 SER E 186 -1 N VAL E 185 O LEU E 202
SSBOND 1 CYS A 63 CYS A 74 1555 1555 2.03
SSBOND 2 CYS B 63 CYS B 74 1555 1555 2.05
SSBOND 3 CYS C 63 CYS C 74 1555 1555 2.04
SSBOND 4 CYS D 63 CYS D 74 1555 1555 2.02
SSBOND 5 CYS E 63 CYS E 74 1555 1555 2.03
CRYST1 102.990 106.791 110.174 90.00 90.00 90.00 P 21 21 21 20
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 0.009710 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009364 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009077 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
