HEADER TRANSCRIPTION REGULATION 03-FEB-06 2CE8
TITLE AN EH1 PEPTIDE BOUND TO THE GROUCHO-TLE WD40 DOMAIN.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSDUCIN-LIKE ENHANCER PROTEIN 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: PARTIAL SP AND WHOLE WD40 DOMAINS, RESIDUES 443-770;
COMPND 5 SYNONYM: ESG1, E(SP1) HOMOLOG;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: EH1 PEPTIDE;
COMPND 9 CHAIN: X, Y;
COMPND 10 ENGINEERED: 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: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS TRANSCRIPTIONAL CO-REPRESSOR, WD40 DOMAIN, WNT SIGNALING PATHWAY,
KEYWDS 2 NUCLEAR PROTEIN, PHOSPHORYLATION, REPRESSOR, TRANSCRIPTION,
KEYWDS 3 TRANSCRIPTION REGULATION, WD REPEAT
EXPDTA X-RAY DIFFRACTION
AUTHOR L.M.PICKLES,S.M.ROE,L.H.PEARL
REVDAT 6 13-DEC-23 2CE8 1 REMARK
REVDAT 5 08-MAY-19 2CE8 1 REMARK
REVDAT 4 05-JUL-17 2CE8 1 REMARK
REVDAT 3 13-JUL-11 2CE8 1 VERSN
REVDAT 2 24-FEB-09 2CE8 1 VERSN
REVDAT 1 14-JUN-06 2CE8 0
JRNL AUTH B.H.JENNINGS,L.M.PICKLES,S.M.WAINWRIGHT,S.M.ROE,L.H.PEARL,
JRNL AUTH 2 D.ISH-HOROWICZ
JRNL TITL MOLECULAR RECOGNITION OF TRANSCRIPTIONAL REPRESSOR MOTIFS BY
JRNL TITL 2 THE WD DOMAIN OF THE GROUCHO/TLE COREPRESSOR.
JRNL REF MOL.CELL V. 22 645 2006
JRNL REFN ISSN 1097-2765
JRNL PMID 16762837
JRNL DOI 10.1016/J.MOLCEL.2006.04.024
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.M.PICKLES,S.M.ROE,E.J.HEMINGWAY,S.STIFANI,L.H.PEARL
REMARK 1 TITL CRYSTAL STRUCTURE OF THE C-TERMINAL WD40 REPEAT DOMAIN OF
REMARK 1 TITL 2 THE HUMAN GROUCHO-TLE1 TRANSCRIPTIONAL COREPRESSOR.
REMARK 1 REF STRUCTURE V. 10 751 2002
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 12057191
REMARK 1 DOI 10.1016/S0969-2126(02)00768-2
REMARK 2
REMARK 2 RESOLUTION. 2.03 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.03
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 116.25
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 83258
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) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4380
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) : 2.02
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4628
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2130
REMARK 3 BIN FREE R VALUE SET COUNT : 251
REMARK 3 BIN FREE R VALUE : 0.3210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10488
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 1077
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) : 20.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.84000
REMARK 3 B22 (A**2) : -0.14000
REMARK 3 B33 (A**2) : 0.75000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.29000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.209
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.185
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.117
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.923
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10752 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14642 ; 1.804 ; 1.942
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1360 ; 8.240 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 458 ;35.469 ;24.454
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1698 ;15.590 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;20.331 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1620 ; 0.130 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8218 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4780 ; 0.225 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 7034 ; 0.304 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1072 ; 0.182 ; 0.200
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): 101 ; 0.206 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 59 ; 0.233 ; 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): 6974 ; 1.126 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10968 ; 1.872 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4394 ; 2.627 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3674 ; 3.908 ; 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 : 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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 434 A 770
REMARK 3 RESIDUE RANGE : X 1 X 9
REMARK 3 ORIGIN FOR THE GROUP (A): -17.8817 1.5953 44.7312
REMARK 3 T TENSOR
REMARK 3 T11: -0.0039 T22: -0.0323
REMARK 3 T33: -0.0018 T12: 0.0027
REMARK 3 T13: 0.0005 T23: -0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 0.3859 L22: 0.1331
REMARK 3 L33: 0.2659 L12: 0.0558
REMARK 3 L13: 0.0427 L23: -0.0204
REMARK 3 S TENSOR
REMARK 3 S11: -0.0066 S12: 0.0071 S13: 0.0142
REMARK 3 S21: -0.0205 S22: 0.0058 S23: 0.0237
REMARK 3 S31: -0.0046 S32: 0.0034 S33: 0.0008
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 434 B 770
REMARK 3 ORIGIN FOR THE GROUP (A): 25.6969 -0.8173 71.3182
REMARK 3 T TENSOR
REMARK 3 T11: -0.0086 T22: -0.0257
REMARK 3 T33: -0.0068 T12: -0.0045
REMARK 3 T13: 0.0019 T23: -0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 0.3834 L22: 0.1730
REMARK 3 L33: 0.3146 L12: -0.0201
REMARK 3 L13: 0.0444 L23: 0.0250
REMARK 3 S TENSOR
REMARK 3 S11: 0.0134 S12: -0.0192 S13: 0.0183
REMARK 3 S21: 0.0266 S22: -0.0306 S23: -0.0200
REMARK 3 S31: 0.0128 S32: 0.0117 S33: 0.0172
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 434 C 770
REMARK 3 RESIDUE RANGE : Y 1 Y 9
REMARK 3 ORIGIN FOR THE GROUP (A): 5.9613 1.3550 -13.0493
REMARK 3 T TENSOR
REMARK 3 T11: -0.0074 T22: -0.0309
REMARK 3 T33: -0.0057 T12: 0.0006
REMARK 3 T13: -0.0091 T23: -0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 0.4740 L22: 0.1118
REMARK 3 L33: 0.3662 L12: -0.0324
REMARK 3 L13: 0.0325 L23: -0.0483
REMARK 3 S TENSOR
REMARK 3 S11: -0.0146 S12: -0.0099 S13: 0.0391
REMARK 3 S21: -0.0194 S22: 0.0066 S23: 0.0034
REMARK 3 S31: 0.0115 S32: -0.0100 S33: 0.0079
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 : D 434 D 770
REMARK 3 ORIGIN FOR THE GROUP (A): 49.4822 -1.8031 13.5743
REMARK 3 T TENSOR
REMARK 3 T11: -0.0091 T22: -0.0306
REMARK 3 T33: -0.0105 T12: -0.0057
REMARK 3 T13: -0.0019 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 0.5668 L22: 0.1413
REMARK 3 L33: 0.4109 L12: -0.1029
REMARK 3 L13: 0.1773 L23: -0.0008
REMARK 3 S TENSOR
REMARK 3 S11: -0.0199 S12: -0.0053 S13: 0.0530
REMARK 3 S21: 0.0199 S22: -0.0248 S23: 0.0040
REMARK 3 S31: 0.0187 S32: 0.0163 S33: 0.0447
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 2CE8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1290027568.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-SEP-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 87651
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.020
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.19000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.200
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 1GXR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6MG/ML PROTEIN WAS MIXED 1:1 WITH 12%
REMARK 280 PEG8000 100MM NACACODYLATE, 100MM CAACETATE AT 14C IN
REMARK 280 MICROBATCH. PEPTIDES WERE ADDED TO THE PROTEIN CRYSTALS IN 125
REMARK 280 MM NACL, 25 MM TRIS PH8.0, 0.5 MM EDTA TO A FINAL CONCENTRATION
REMARK 280 OF 0.76 MM, AND INCUBATED FOR 16 H BEFORE HARVESTING AND WASHING
REMARK 280 IN 50MM NA CACODYLATE PH6.5, 12 % PEG 8K, AND CRYO-PROTECTED IN
REMARK 280 30% ETHYLENE GLYCOL 50MM NA CACODYLATE PH6.5, 12 % PEG 8K, PH
REMARK 280 6.50, TEMPERATURE 287K
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 28.17600
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, X
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, Y
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 TRANSCRIPTIONAL COREPRESSOR THAT BINDS TO A NUMBER OF
REMARK 400 TRANSCRIPTION FACTORS
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 A 2183 O HOH A 2232 1.92
REMARK 500 O HOH A 2006 O HOH B 2123 1.98
REMARK 500 O PRO B 515 ND2 ASN B 517 2.00
REMARK 500 O HOH B 2006 O HOH B 2137 2.04
REMARK 500 N SER D 519 O HOH D 2055 2.08
REMARK 500 O HOH D 2111 O HOH D 2113 2.13
REMARK 500 O HOH C 2004 O HOH D 2010 2.17
REMARK 500 O HOH B 2039 O HOH B 2245 2.17
REMARK 500 ND2 ASN A 479 O HOH A 2043 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH D 2052 O HOH D 2220 2645 1.84
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 LEU A 663 CA - CB - CG ANGL. DEV. = 15.4 DEGREES
REMARK 500 LEU B 663 CA - CB - CG ANGL. DEV. = 17.0 DEGREES
REMARK 500 SER B 678 CA - CB - OG ANGL. DEV. = -16.2 DEGREES
REMARK 500 LEU B 704 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 LEU C 704 CA - CB - CG ANGL. DEV. = 15.8 DEGREES
REMARK 500 PRO D 520 C - N - CA ANGL. DEV. = 15.2 DEGREES
REMARK 500 PRO D 520 C - N - CD ANGL. DEV. = -14.2 DEGREES
REMARK 500 THR D 563 C - N - CA ANGL. DEV. = 15.3 DEGREES
REMARK 500 LEU D 663 CA - CB - CG ANGL. DEV. = 21.1 DEGREES
REMARK 500 LEU D 704 CA - CB - CG ANGL. DEV. = 17.4 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 TYR A 435 -56.48 79.70
REMARK 500 ASP A 453 -167.84 -71.12
REMARK 500 ARG A 497 -25.90 -157.44
REMARK 500 PRO A 562 -99.12 -56.25
REMARK 500 THR A 563 78.12 70.17
REMARK 500 GLU A 670 -30.13 83.00
REMARK 500 SER A 679 -8.64 95.55
REMARK 500 ASN A 687 -1.89 76.63
REMARK 500 ASN A 720 -0.01 89.00
REMARK 500 LYS A 761 39.72 70.90
REMARK 500 ALA B 445 126.43 -37.59
REMARK 500 ARG B 497 -57.23 -165.86
REMARK 500 SER B 513 46.66 -91.15
REMARK 500 HIS B 514 14.54 -165.04
REMARK 500 PRO B 515 -107.80 26.85
REMARK 500 ASN B 517 -175.82 41.78
REMARK 500 LYS B 518 5.16 153.60
REMARK 500 ALA B 561 -45.36 -153.32
REMARK 500 LEU B 651 -68.68 -106.41
REMARK 500 GLU B 670 -28.77 81.38
REMARK 500 SER B 678 -74.50 -56.53
REMARK 500 SER B 679 -12.52 168.88
REMARK 500 ASN B 720 -0.45 84.87
REMARK 500 ASP B 751 15.92 55.56
REMARK 500 ASP C 453 -167.37 -78.04
REMARK 500 HIS C 474 -177.52 -171.86
REMARK 500 ARG C 497 -29.35 -143.39
REMARK 500 ALA C 561 90.67 42.06
REMARK 500 THR C 563 127.05 -32.66
REMARK 500 LEU C 651 -60.88 -107.81
REMARK 500 GLU C 670 -30.84 83.89
REMARK 500 SER C 679 -12.78 94.95
REMARK 500 ASN C 687 -8.54 77.24
REMARK 500 ASN C 720 1.51 83.83
REMARK 500 ARG D 497 -54.88 -160.49
REMARK 500 SER D 513 76.83 -67.47
REMARK 500 HIS D 514 134.23 130.84
REMARK 500 PRO D 515 -169.85 -74.34
REMARK 500 SER D 519 -158.87 100.93
REMARK 500 PRO D 540 -37.03 -37.76
REMARK 500 ALA D 560 -52.76 -132.49
REMARK 500 ALA D 561 78.45 79.94
REMARK 500 PRO D 562 -93.49 6.77
REMARK 500 THR D 563 57.93 89.95
REMARK 500 ASP D 617 -155.17 -101.97
REMARK 500 ASP D 637 7.02 -69.10
REMARK 500 ARG D 646 -64.05 -100.16
REMARK 500 LEU D 651 -66.88 -97.21
REMARK 500 GLU D 670 -27.85 79.85
REMARK 500 SER D 679 -16.78 103.14
REMARK 500
REMARK 500 THIS ENTRY HAS 51 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 PRO A 562 THR A 563 43.82
REMARK 500 HIS B 514 PRO B 515 -116.96
REMARK 500 GLY B 516 ASN B 517 31.61
REMARK 500 LYS D 518 SER D 519 37.05
REMARK 500 LEU D 559 ALA D 560 -41.30
REMARK 500 PRO D 562 THR D 563 30.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B2159 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH B2178 DISTANCE = 7.18 ANGSTROMS
REMARK 525 HOH B2184 DISTANCE = 6.00 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GXR RELATED DB: PDB
REMARK 900 WD40 REGION OF HUMAN GROUCHO/TLE1
REMARK 900 RELATED ID: 2CE9 RELATED DB: PDB
REMARK 900 A WRPW PEPTIDE BOUND TO THE GROUCHO-TLE WD40 DOMAIN.
DBREF 2CE8 A 434 442 PDB 2CE8 2CE8 434 442
DBREF 2CE8 A 443 770 UNP Q04724 TLE1_HUMAN 443 770
DBREF 2CE8 B 434 442 PDB 2CE8 2CE8 434 442
DBREF 2CE8 B 443 770 UNP Q04724 TLE1_HUMAN 443 770
DBREF 2CE8 C 434 442 PDB 2CE8 2CE8 434 442
DBREF 2CE8 C 443 770 UNP Q04724 TLE1_HUMAN 443 770
DBREF 2CE8 D 434 442 PDB 2CE8 2CE8 434 442
DBREF 2CE8 D 443 770 UNP Q04724 TLE1_HUMAN 443 770
DBREF 2CE8 X 1 9 PDB 2CE8 2CE8 1 9
DBREF 2CE8 Y 1 9 PDB 2CE8 2CE8 1 9
SEQRES 1 A 337 ASP TYR PHE GLN GLY ALA MET GLY SER LYS PRO ALA TYR
SEQRES 2 A 337 SER PHE HIS VAL THR ALA ASP GLY GLN MET GLN PRO VAL
SEQRES 3 A 337 PRO PHE PRO PRO ASP ALA LEU ILE GLY PRO GLY ILE PRO
SEQRES 4 A 337 ARG HIS ALA ARG GLN ILE ASN THR LEU ASN HIS GLY GLU
SEQRES 5 A 337 VAL VAL CYS ALA VAL THR ILE SER ASN PRO THR ARG HIS
SEQRES 6 A 337 VAL TYR THR GLY GLY LYS GLY CYS VAL LYS VAL TRP ASP
SEQRES 7 A 337 ILE SER HIS PRO GLY ASN LYS SER PRO VAL SER GLN LEU
SEQRES 8 A 337 ASP CYS LEU ASN ARG ASP ASN TYR ILE ARG SER CYS LYS
SEQRES 9 A 337 LEU LEU PRO ASP GLY CYS THR LEU ILE VAL GLY GLY GLU
SEQRES 10 A 337 ALA SER THR LEU SER ILE TRP ASP LEU ALA ALA PRO THR
SEQRES 11 A 337 PRO ARG ILE LYS ALA GLU LEU THR SER SER ALA PRO ALA
SEQRES 12 A 337 CYS TYR ALA LEU ALA ILE SER PRO ASP SER LYS VAL CYS
SEQRES 13 A 337 PHE SER CYS CYS SER ASP GLY ASN ILE ALA VAL TRP ASP
SEQRES 14 A 337 LEU HIS ASN GLN THR LEU VAL ARG GLN PHE GLN GLY HIS
SEQRES 15 A 337 THR ASP GLY ALA SER CYS ILE ASP ILE SER ASN ASP GLY
SEQRES 16 A 337 THR LYS LEU TRP THR GLY GLY LEU ASP ASN THR VAL ARG
SEQRES 17 A 337 SER TRP ASP LEU ARG GLU GLY ARG GLN LEU GLN GLN HIS
SEQRES 18 A 337 ASP PHE THR SER GLN ILE PHE SER LEU GLY TYR CYS PRO
SEQRES 19 A 337 THR GLY GLU TRP LEU ALA VAL GLY MET GLU SER SER ASN
SEQRES 20 A 337 VAL GLU VAL LEU HIS VAL ASN LYS PRO ASP LYS TYR GLN
SEQRES 21 A 337 LEU HIS LEU HIS GLU SER CYS VAL LEU SER LEU LYS PHE
SEQRES 22 A 337 ALA TYR CYS GLY LYS TRP PHE VAL SER THR GLY LYS ASP
SEQRES 23 A 337 ASN LEU LEU ASN ALA TRP ARG THR PRO TYR GLY ALA SER
SEQRES 24 A 337 ILE PHE GLN SER LYS GLU SER SER SER VAL LEU SER CYS
SEQRES 25 A 337 ASP ILE SER VAL ASP ASP LYS TYR ILE VAL THR GLY SER
SEQRES 26 A 337 GLY ASP LYS LYS ALA THR VAL TYR GLU VAL ILE TYR
SEQRES 1 B 337 ASP TYR PHE GLN GLY ALA MET GLY SER LYS PRO ALA TYR
SEQRES 2 B 337 SER PHE HIS VAL THR ALA ASP GLY GLN MET GLN PRO VAL
SEQRES 3 B 337 PRO PHE PRO PRO ASP ALA LEU ILE GLY PRO GLY ILE PRO
SEQRES 4 B 337 ARG HIS ALA ARG GLN ILE ASN THR LEU ASN HIS GLY GLU
SEQRES 5 B 337 VAL VAL CYS ALA VAL THR ILE SER ASN PRO THR ARG HIS
SEQRES 6 B 337 VAL TYR THR GLY GLY LYS GLY CYS VAL LYS VAL TRP ASP
SEQRES 7 B 337 ILE SER HIS PRO GLY ASN LYS SER PRO VAL SER GLN LEU
SEQRES 8 B 337 ASP CYS LEU ASN ARG ASP ASN TYR ILE ARG SER CYS LYS
SEQRES 9 B 337 LEU LEU PRO ASP GLY CYS THR LEU ILE VAL GLY GLY GLU
SEQRES 10 B 337 ALA SER THR LEU SER ILE TRP ASP LEU ALA ALA PRO THR
SEQRES 11 B 337 PRO ARG ILE LYS ALA GLU LEU THR SER SER ALA PRO ALA
SEQRES 12 B 337 CYS TYR ALA LEU ALA ILE SER PRO ASP SER LYS VAL CYS
SEQRES 13 B 337 PHE SER CYS CYS SER ASP GLY ASN ILE ALA VAL TRP ASP
SEQRES 14 B 337 LEU HIS ASN GLN THR LEU VAL ARG GLN PHE GLN GLY HIS
SEQRES 15 B 337 THR ASP GLY ALA SER CYS ILE ASP ILE SER ASN ASP GLY
SEQRES 16 B 337 THR LYS LEU TRP THR GLY GLY LEU ASP ASN THR VAL ARG
SEQRES 17 B 337 SER TRP ASP LEU ARG GLU GLY ARG GLN LEU GLN GLN HIS
SEQRES 18 B 337 ASP PHE THR SER GLN ILE PHE SER LEU GLY TYR CYS PRO
SEQRES 19 B 337 THR GLY GLU TRP LEU ALA VAL GLY MET GLU SER SER ASN
SEQRES 20 B 337 VAL GLU VAL LEU HIS VAL ASN LYS PRO ASP LYS TYR GLN
SEQRES 21 B 337 LEU HIS LEU HIS GLU SER CYS VAL LEU SER LEU LYS PHE
SEQRES 22 B 337 ALA TYR CYS GLY LYS TRP PHE VAL SER THR GLY LYS ASP
SEQRES 23 B 337 ASN LEU LEU ASN ALA TRP ARG THR PRO TYR GLY ALA SER
SEQRES 24 B 337 ILE PHE GLN SER LYS GLU SER SER SER VAL LEU SER CYS
SEQRES 25 B 337 ASP ILE SER VAL ASP ASP LYS TYR ILE VAL THR GLY SER
SEQRES 26 B 337 GLY ASP LYS LYS ALA THR VAL TYR GLU VAL ILE TYR
SEQRES 1 C 337 ASP TYR PHE GLN GLY ALA MET GLY SER LYS PRO ALA TYR
SEQRES 2 C 337 SER PHE HIS VAL THR ALA ASP GLY GLN MET GLN PRO VAL
SEQRES 3 C 337 PRO PHE PRO PRO ASP ALA LEU ILE GLY PRO GLY ILE PRO
SEQRES 4 C 337 ARG HIS ALA ARG GLN ILE ASN THR LEU ASN HIS GLY GLU
SEQRES 5 C 337 VAL VAL CYS ALA VAL THR ILE SER ASN PRO THR ARG HIS
SEQRES 6 C 337 VAL TYR THR GLY GLY LYS GLY CYS VAL LYS VAL TRP ASP
SEQRES 7 C 337 ILE SER HIS PRO GLY ASN LYS SER PRO VAL SER GLN LEU
SEQRES 8 C 337 ASP CYS LEU ASN ARG ASP ASN TYR ILE ARG SER CYS LYS
SEQRES 9 C 337 LEU LEU PRO ASP GLY CYS THR LEU ILE VAL GLY GLY GLU
SEQRES 10 C 337 ALA SER THR LEU SER ILE TRP ASP LEU ALA ALA PRO THR
SEQRES 11 C 337 PRO ARG ILE LYS ALA GLU LEU THR SER SER ALA PRO ALA
SEQRES 12 C 337 CYS TYR ALA LEU ALA ILE SER PRO ASP SER LYS VAL CYS
SEQRES 13 C 337 PHE SER CYS CYS SER ASP GLY ASN ILE ALA VAL TRP ASP
SEQRES 14 C 337 LEU HIS ASN GLN THR LEU VAL ARG GLN PHE GLN GLY HIS
SEQRES 15 C 337 THR ASP GLY ALA SER CYS ILE ASP ILE SER ASN ASP GLY
SEQRES 16 C 337 THR LYS LEU TRP THR GLY GLY LEU ASP ASN THR VAL ARG
SEQRES 17 C 337 SER TRP ASP LEU ARG GLU GLY ARG GLN LEU GLN GLN HIS
SEQRES 18 C 337 ASP PHE THR SER GLN ILE PHE SER LEU GLY TYR CYS PRO
SEQRES 19 C 337 THR GLY GLU TRP LEU ALA VAL GLY MET GLU SER SER ASN
SEQRES 20 C 337 VAL GLU VAL LEU HIS VAL ASN LYS PRO ASP LYS TYR GLN
SEQRES 21 C 337 LEU HIS LEU HIS GLU SER CYS VAL LEU SER LEU LYS PHE
SEQRES 22 C 337 ALA TYR CYS GLY LYS TRP PHE VAL SER THR GLY LYS ASP
SEQRES 23 C 337 ASN LEU LEU ASN ALA TRP ARG THR PRO TYR GLY ALA SER
SEQRES 24 C 337 ILE PHE GLN SER LYS GLU SER SER SER VAL LEU SER CYS
SEQRES 25 C 337 ASP ILE SER VAL ASP ASP LYS TYR ILE VAL THR GLY SER
SEQRES 26 C 337 GLY ASP LYS LYS ALA THR VAL TYR GLU VAL ILE TYR
SEQRES 1 D 337 ASP TYR PHE GLN GLY ALA MET GLY SER LYS PRO ALA TYR
SEQRES 2 D 337 SER PHE HIS VAL THR ALA ASP GLY GLN MET GLN PRO VAL
SEQRES 3 D 337 PRO PHE PRO PRO ASP ALA LEU ILE GLY PRO GLY ILE PRO
SEQRES 4 D 337 ARG HIS ALA ARG GLN ILE ASN THR LEU ASN HIS GLY GLU
SEQRES 5 D 337 VAL VAL CYS ALA VAL THR ILE SER ASN PRO THR ARG HIS
SEQRES 6 D 337 VAL TYR THR GLY GLY LYS GLY CYS VAL LYS VAL TRP ASP
SEQRES 7 D 337 ILE SER HIS PRO GLY ASN LYS SER PRO VAL SER GLN LEU
SEQRES 8 D 337 ASP CYS LEU ASN ARG ASP ASN TYR ILE ARG SER CYS LYS
SEQRES 9 D 337 LEU LEU PRO ASP GLY CYS THR LEU ILE VAL GLY GLY GLU
SEQRES 10 D 337 ALA SER THR LEU SER ILE TRP ASP LEU ALA ALA PRO THR
SEQRES 11 D 337 PRO ARG ILE LYS ALA GLU LEU THR SER SER ALA PRO ALA
SEQRES 12 D 337 CYS TYR ALA LEU ALA ILE SER PRO ASP SER LYS VAL CYS
SEQRES 13 D 337 PHE SER CYS CYS SER ASP GLY ASN ILE ALA VAL TRP ASP
SEQRES 14 D 337 LEU HIS ASN GLN THR LEU VAL ARG GLN PHE GLN GLY HIS
SEQRES 15 D 337 THR ASP GLY ALA SER CYS ILE ASP ILE SER ASN ASP GLY
SEQRES 16 D 337 THR LYS LEU TRP THR GLY GLY LEU ASP ASN THR VAL ARG
SEQRES 17 D 337 SER TRP ASP LEU ARG GLU GLY ARG GLN LEU GLN GLN HIS
SEQRES 18 D 337 ASP PHE THR SER GLN ILE PHE SER LEU GLY TYR CYS PRO
SEQRES 19 D 337 THR GLY GLU TRP LEU ALA VAL GLY MET GLU SER SER ASN
SEQRES 20 D 337 VAL GLU VAL LEU HIS VAL ASN LYS PRO ASP LYS TYR GLN
SEQRES 21 D 337 LEU HIS LEU HIS GLU SER CYS VAL LEU SER LEU LYS PHE
SEQRES 22 D 337 ALA TYR CYS GLY LYS TRP PHE VAL SER THR GLY LYS ASP
SEQRES 23 D 337 ASN LEU LEU ASN ALA TRP ARG THR PRO TYR GLY ALA SER
SEQRES 24 D 337 ILE PHE GLN SER LYS GLU SER SER SER VAL LEU SER CYS
SEQRES 25 D 337 ASP ILE SER VAL ASP ASP LYS TYR ILE VAL THR GLY SER
SEQRES 26 D 337 GLY ASP LYS LYS ALA THR VAL TYR GLU VAL ILE TYR
SEQRES 1 X 9 MET PHE SER ILE ASP ASN ILE LEU ALA
SEQRES 1 Y 9 MET PHE SER ILE ASP ASN ILE LEU ALA
FORMUL 7 HOH *1077(H2 O)
HELIX 1 1 SER X 3 ALA X 9 1 7
HELIX 2 2 SER Y 3 ALA Y 9 1 7
SHEET 1 AA 2 PHE A 436 PRO A 444 0
SHEET 2 AA 2 PHE B 436 PRO B 444 -1 O GLN B 437 N LYS A 443
SHEET 1 AB 6 MET A 456 PRO A 458 0
SHEET 2 AB 6 SER A 447 VAL A 450 -1 O HIS A 449 N GLN A 457
SHEET 3 AB 6 LYS A 691 LEU A 694 -1 O LYS A 691 N VAL A 450
SHEET 4 AB 6 VAL A 681 HIS A 685 -1 O VAL A 681 N LEU A 694
SHEET 5 AB 6 TRP A 671 MET A 676 -1 O LEU A 672 N LEU A 684
SHEET 6 AB 6 ILE A 660 TYR A 665 -1 N PHE A 661 O GLY A 675
SHEET 1 AC 4 HIS A 474 LEU A 481 0
SHEET 2 AC 4 ALA A 763 ILE A 769 -1 O ALA A 763 N LEU A 481
SHEET 3 AC 4 TYR A 753 SER A 758 -1 O ILE A 754 N TYR A 766
SHEET 4 AC 4 VAL A 742 ILE A 747 -1 N LEU A 743 O GLY A 757
SHEET 1 AD 4 ALA A 489 ILE A 492 0
SHEET 2 AD 4 HIS A 498 GLY A 502 -1 O TYR A 500 N THR A 491
SHEET 3 AD 4 CYS A 506 ASP A 511 -1 O LYS A 508 N THR A 501
SHEET 4 AD 4 SER A 522 ASP A 525 -1 O SER A 522 N VAL A 509
SHEET 1 AE 4 ILE A 533 LEU A 538 0
SHEET 2 AE 4 THR A 544 GLY A 549 -1 O ILE A 546 N LYS A 537
SHEET 3 AE 4 THR A 553 ASP A 558 -1 O SER A 555 N VAL A 547
SHEET 4 AE 4 ARG A 565 THR A 571 -1 O ARG A 565 N ASP A 558
SHEET 1 AF 4 CYS A 577 ILE A 582 0
SHEET 2 AF 4 VAL A 588 CYS A 593 -1 O PHE A 590 N ALA A 581
SHEET 3 AF 4 ILE A 598 ASP A 602 -1 O ALA A 599 N SER A 591
SHEET 4 AF 4 THR A 607 PHE A 612 -1 O THR A 607 N ASP A 602
SHEET 1 AG 4 ALA A 619 ILE A 624 0
SHEET 2 AG 4 LYS A 630 GLY A 635 -1 O TRP A 632 N ASP A 623
SHEET 3 AG 4 THR A 639 ASP A 644 -1 O THR A 639 N GLY A 635
SHEET 4 AG 4 GLN A 650 ASP A 655 -1 N LEU A 651 O SER A 642
SHEET 1 AH 4 VAL A 701 PHE A 706 0
SHEET 2 AH 4 TRP A 712 GLY A 717 -1 O VAL A 714 N LYS A 705
SHEET 3 AH 4 LEU A 721 ARG A 726 -1 O LEU A 721 N GLY A 717
SHEET 4 AH 4 SER A 732 LYS A 737 -1 N ILE A 733 O ALA A 724
SHEET 1 BA 6 MET B 456 PRO B 458 0
SHEET 2 BA 6 SER B 447 VAL B 450 -1 O HIS B 449 N GLN B 457
SHEET 3 BA 6 LYS B 691 LEU B 694 -1 O LYS B 691 N VAL B 450
SHEET 4 BA 6 VAL B 681 HIS B 685 -1 O VAL B 681 N LEU B 694
SHEET 5 BA 6 TRP B 671 MET B 676 -1 O LEU B 672 N LEU B 684
SHEET 6 BA 6 ILE B 660 TYR B 665 -1 N PHE B 661 O GLY B 675
SHEET 1 BB 4 HIS B 474 LEU B 481 0
SHEET 2 BB 4 ALA B 763 ILE B 769 -1 O ALA B 763 N LEU B 481
SHEET 3 BB 4 TYR B 753 SER B 758 -1 O ILE B 754 N TYR B 766
SHEET 4 BB 4 VAL B 742 ILE B 747 -1 N LEU B 743 O GLY B 757
SHEET 1 BC 4 ALA B 489 ILE B 492 0
SHEET 2 BC 4 HIS B 498 GLY B 502 -1 O TYR B 500 N THR B 491
SHEET 3 BC 4 CYS B 506 ASP B 511 -1 O LYS B 508 N THR B 501
SHEET 4 BC 4 SER B 522 ASP B 525 -1 O SER B 522 N VAL B 509
SHEET 1 BD 4 ILE B 533 LEU B 538 0
SHEET 2 BD 4 THR B 544 GLY B 549 -1 O ILE B 546 N LYS B 537
SHEET 3 BD 4 THR B 553 ASP B 558 -1 O SER B 555 N VAL B 547
SHEET 4 BD 4 ARG B 565 THR B 571 -1 O ARG B 565 N ASP B 558
SHEET 1 BE 4 CYS B 577 ILE B 582 0
SHEET 2 BE 4 VAL B 588 CYS B 593 -1 O PHE B 590 N ALA B 581
SHEET 3 BE 4 ILE B 598 ASP B 602 -1 O ALA B 599 N SER B 591
SHEET 4 BE 4 THR B 607 PHE B 612 -1 O THR B 607 N ASP B 602
SHEET 1 BF 4 ALA B 619 ILE B 624 0
SHEET 2 BF 4 LYS B 630 GLY B 635 -1 O TRP B 632 N ASP B 623
SHEET 3 BF 4 THR B 639 ASP B 644 -1 O THR B 639 N GLY B 635
SHEET 4 BF 4 GLN B 650 ASP B 655 -1 N LEU B 651 O SER B 642
SHEET 1 BG 4 VAL B 701 PHE B 706 0
SHEET 2 BG 4 TRP B 712 GLY B 717 -1 O VAL B 714 N LYS B 705
SHEET 3 BG 4 LEU B 721 ARG B 726 -1 O LEU B 721 N GLY B 717
SHEET 4 BG 4 SER B 732 LYS B 737 -1 N ILE B 733 O ALA B 724
SHEET 1 CA 2 PHE C 436 PRO C 444 0
SHEET 2 CA 2 PHE D 436 PRO D 444 -1 O GLN D 437 N LYS C 443
SHEET 1 CB 6 MET C 456 PRO C 458 0
SHEET 2 CB 6 SER C 447 VAL C 450 -1 O HIS C 449 N GLN C 457
SHEET 3 CB 6 LYS C 691 LEU C 694 -1 O LYS C 691 N VAL C 450
SHEET 4 CB 6 VAL C 681 HIS C 685 -1 O VAL C 681 N LEU C 694
SHEET 5 CB 6 TRP C 671 MET C 676 -1 O LEU C 672 N LEU C 684
SHEET 6 CB 6 ILE C 660 TYR C 665 -1 N PHE C 661 O GLY C 675
SHEET 1 CC 4 HIS C 474 LEU C 481 0
SHEET 2 CC 4 ALA C 763 ILE C 769 -1 O ALA C 763 N LEU C 481
SHEET 3 CC 4 TYR C 753 SER C 758 -1 O ILE C 754 N TYR C 766
SHEET 4 CC 4 VAL C 742 ILE C 747 -1 N LEU C 743 O GLY C 757
SHEET 1 CD 4 ALA C 489 ILE C 492 0
SHEET 2 CD 4 HIS C 498 GLY C 502 -1 O TYR C 500 N THR C 491
SHEET 3 CD 4 CYS C 506 ASP C 511 -1 O LYS C 508 N THR C 501
SHEET 4 CD 4 SER C 522 ASP C 525 -1 O SER C 522 N VAL C 509
SHEET 1 CE 4 ILE C 533 LEU C 538 0
SHEET 2 CE 4 THR C 544 GLY C 549 -1 O ILE C 546 N LYS C 537
SHEET 3 CE 4 THR C 553 ASP C 558 -1 O SER C 555 N VAL C 547
SHEET 4 CE 4 ARG C 565 THR C 571 -1 O ARG C 565 N ASP C 558
SHEET 1 CF 4 CYS C 577 ILE C 582 0
SHEET 2 CF 4 VAL C 588 CYS C 593 -1 O PHE C 590 N ALA C 581
SHEET 3 CF 4 ILE C 598 ASP C 602 -1 O ALA C 599 N SER C 591
SHEET 4 CF 4 THR C 607 PHE C 612 -1 O THR C 607 N ASP C 602
SHEET 1 CG 4 ALA C 619 ILE C 624 0
SHEET 2 CG 4 LYS C 630 GLY C 635 -1 O TRP C 632 N ASP C 623
SHEET 3 CG 4 THR C 639 ASP C 644 -1 O THR C 639 N GLY C 635
SHEET 4 CG 4 GLN C 650 ASP C 655 -1 N LEU C 651 O SER C 642
SHEET 1 CH 4 VAL C 701 PHE C 706 0
SHEET 2 CH 4 TRP C 712 GLY C 717 -1 O VAL C 714 N LYS C 705
SHEET 3 CH 4 LEU C 721 ARG C 726 -1 O LEU C 721 N GLY C 717
SHEET 4 CH 4 SER C 732 LYS C 737 -1 N ILE C 733 O ALA C 724
SHEET 1 DA 6 MET D 456 PRO D 458 0
SHEET 2 DA 6 SER D 447 VAL D 450 -1 O HIS D 449 N GLN D 457
SHEET 3 DA 6 LYS D 691 LEU D 694 -1 O LYS D 691 N VAL D 450
SHEET 4 DA 6 VAL D 681 HIS D 685 -1 O VAL D 681 N LEU D 694
SHEET 5 DA 6 TRP D 671 MET D 676 -1 O LEU D 672 N LEU D 684
SHEET 6 DA 6 ILE D 660 TYR D 665 -1 N PHE D 661 O GLY D 675
SHEET 1 DB 4 HIS D 474 LEU D 481 0
SHEET 2 DB 4 ALA D 763 ILE D 769 -1 O ALA D 763 N LEU D 481
SHEET 3 DB 4 TYR D 753 SER D 758 -1 O ILE D 754 N TYR D 766
SHEET 4 DB 4 VAL D 742 ILE D 747 -1 N LEU D 743 O GLY D 757
SHEET 1 DC 4 ALA D 489 ILE D 492 0
SHEET 2 DC 4 HIS D 498 GLY D 502 -1 O TYR D 500 N THR D 491
SHEET 3 DC 4 CYS D 506 ASP D 511 -1 O LYS D 508 N THR D 501
SHEET 4 DC 4 SER D 522 ASP D 525 -1 O SER D 522 N VAL D 509
SHEET 1 DD 4 ILE D 533 LEU D 538 0
SHEET 2 DD 4 THR D 544 GLY D 549 -1 O ILE D 546 N LYS D 537
SHEET 3 DD 4 THR D 553 ASP D 558 -1 O SER D 555 N VAL D 547
SHEET 4 DD 4 ARG D 565 THR D 571 -1 O ARG D 565 N ASP D 558
SHEET 1 DE 4 CYS D 577 ILE D 582 0
SHEET 2 DE 4 VAL D 588 CYS D 593 -1 O PHE D 590 N ALA D 581
SHEET 3 DE 4 ILE D 598 ASP D 602 -1 O ALA D 599 N SER D 591
SHEET 4 DE 4 THR D 607 PHE D 612 -1 O THR D 607 N ASP D 602
SHEET 1 DF 4 ALA D 619 ILE D 624 0
SHEET 2 DF 4 LYS D 630 GLY D 635 -1 O TRP D 632 N ASP D 623
SHEET 3 DF 4 THR D 639 ASP D 644 -1 O THR D 639 N GLY D 635
SHEET 4 DF 4 GLN D 650 ASP D 655 -1 N LEU D 651 O SER D 642
SHEET 1 DG 4 VAL D 701 PHE D 706 0
SHEET 2 DG 4 TRP D 712 GLY D 717 -1 O VAL D 714 N LYS D 705
SHEET 3 DG 4 LEU D 721 ARG D 726 -1 O LEU D 721 N GLY D 717
SHEET 4 DG 4 SER D 732 LYS D 737 -1 N ILE D 733 O ALA D 724
CISPEP 1 ASN A 494 PRO A 495 0 0.21
CISPEP 2 ALA A 561 PRO A 562 0 12.30
CISPEP 3 THR A 727 PRO A 728 0 -8.26
CISPEP 4 ASN B 494 PRO B 495 0 0.98
CISPEP 5 PRO B 515 GLY B 516 0 19.28
CISPEP 6 ALA B 560 ALA B 561 0 -14.76
CISPEP 7 ALA B 561 PRO B 562 0 -11.96
CISPEP 8 THR B 727 PRO B 728 0 -8.04
CISPEP 9 ASN C 494 PRO C 495 0 3.66
CISPEP 10 PRO C 562 THR C 563 0 1.66
CISPEP 11 THR C 727 PRO C 728 0 -12.90
CISPEP 12 ASN D 494 PRO D 495 0 -2.29
CISPEP 13 SER D 519 PRO D 520 0 -2.27
CISPEP 14 ALA D 560 ALA D 561 0 9.50
CISPEP 15 THR D 727 PRO D 728 0 -4.59
CRYST1 107.585 56.352 125.245 90.00 112.32 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 0.009295 0.000000 0.003816 0.00000
SCALE2 0.000000 0.017746 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008631 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
