HEADER PROTEIN BINDING 23-FEB-08 3CBY
TITLE THE DVL2 PDZ DOMAIN IN COMPLEX WITH THE N1 INHIBITORY PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DISHEVELLED-2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: PDZ DOMAIN (UNP RESIDUES 264-354);
COMPND 5 SYNONYM: SEGMENT POLARITY PROTEIN DISHEVELLED HOMOLOG DVL-2, DSH
COMPND 6 HOMOLOG 2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DVL2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS PDZ DOMAIN, PHAGE DERIVED HIGH AFFINITY LIGAND, CYTOPLASM,
KEYWDS 2 DEVELOPMENTAL PROTEIN, PHOSPHOPROTEIN, WNT SIGNALING PATHWAY,
KEYWDS 3 PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR B.A.APPLETON,C.WIESMANN
REVDAT 6 30-AUG-23 3CBY 1 REMARK
REVDAT 5 20-OCT-21 3CBY 1 SEQADV
REVDAT 4 25-OCT-17 3CBY 1 REMARK
REVDAT 3 31-MAR-09 3CBY 1 JRNL
REVDAT 2 17-MAR-09 3CBY 1 JRNL
REVDAT 1 03-MAR-09 3CBY 0
JRNL AUTH Y.ZHANG,B.A.APPLETON,C.WIESMANN,T.LAU,M.COSTA,R.N.HANNOUSH,
JRNL AUTH 2 S.S.SIDHU
JRNL TITL INHIBITION OF WNT SIGNALING BY DISHEVELLED PDZ PEPTIDES
JRNL REF NAT.CHEM.BIOL. V. 5 217 2009
JRNL REFN ISSN 1552-4450
JRNL PMID 19252499
JRNL DOI 10.1038/NCHEMBIO.152
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 33035
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) : 0.136
REMARK 3 R VALUE (WORKING SET) : 0.134
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1743
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 25
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.53
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1940
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.1370
REMARK 3 BIN FREE R VALUE SET COUNT : 92
REMARK 3 BIN FREE R VALUE : 0.2320
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1500
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 198
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.49000
REMARK 3 B22 (A**2) : 0.32000
REMARK 3 B33 (A**2) : 0.39000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.61000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.066
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.064
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.040
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.344
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.977
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1599 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1059 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2175 ; 1.513 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2614 ; 0.915 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 218 ; 5.558 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 67 ;39.227 ;25.373
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 281 ;11.923 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;10.478 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 249 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1797 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 298 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 279 ; 0.216 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1104 ; 0.195 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 775 ; 0.181 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 872 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 138 ; 0.199 ; 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): 11 ; 0.136 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 25 ; 0.252 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.110 ; 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): 1074 ; 5.219 ; 2.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 430 ; 2.601 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1627 ; 6.340 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 652 ; 5.941 ; 2.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 536 ; 7.804 ; 5.000
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): 2989 ; 3.252 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 198 ;14.781 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2626 ; 7.246 ; 3.000
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 3CBY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-FEB-08.
REMARK 100 THE DEPOSITION ID IS D_1000046590.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUN-06
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 : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34942
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.63600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
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: 3CBX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M TRI-SODIUM CITRATE, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 68.15150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.09350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 68.15150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.09350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 260
REMARK 465 SER A 286
REMARK 465 ASN A 287
REMARK 465 GLU A 288
REMARK 465 ARG A 289
REMARK 465 GLY A 290
REMARK 465 ASP A 291
REMARK 465 GLY B 260
REMARK 465 SER B 261
REMARK 465 HIS B 262
REMARK 465 MET B 263
REMARK 465 ASN B 287
REMARK 465 GLU B 288
REMARK 465 ARG B 289
REMARK 465 GLY B 290
REMARK 465 GLY B 355
REMARK 465 GLY B 356
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 367 CG CD CE NZ
REMARK 470 LYS B 367 CG CD CE NZ
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 MET A 272 O TYR A 275 2.15
REMARK 500 O HOH B 1096 O HOH B 1100 2.17
REMARK 500 O HOH B 1066 O HOH B 1096 2.18
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 ASN A 321 -125.24 52.49
REMARK 500 ASN B 321 -125.13 50.48
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 A2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B2001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CBX RELATED DB: PDB
REMARK 900 RELATED ID: 3CBZ RELATED DB: PDB
REMARK 900 RELATED ID: 3CC0 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE PEPTIDE LIGAND WAS FUSED TO THE C TERMINUS OF THE LINKER
DBREF 3CBY A 264 354 UNP O14641 DVL2_HUMAN 264 354
DBREF 3CBY B 264 354 UNP O14641 DVL2_HUMAN 264 354
SEQADV 3CBY GLY A 260 UNP O14641 EXPRESSION TAG
SEQADV 3CBY SER A 261 UNP O14641 EXPRESSION TAG
SEQADV 3CBY HIS A 262 UNP O14641 EXPRESSION TAG
SEQADV 3CBY MET A 263 UNP O14641 EXPRESSION TAG
SEQADV 3CBY SER A 354 UNP O14641 CYS 354 ENGINEERED MUTATION
SEQADV 3CBY GLY A 355 UNP O14641 LINKER
SEQADV 3CBY GLY A 356 UNP O14641 LINKER
SEQADV 3CBY GLY A 357 UNP O14641 LINKER
SEQADV 3CBY TRP A 358 UNP O14641 SEE REMARK 999
SEQADV 3CBY LYS A 359 UNP O14641 SEE REMARK 999
SEQADV 3CBY ASP A 360 UNP O14641 SEE REMARK 999
SEQADV 3CBY TYR A 361 UNP O14641 SEE REMARK 999
SEQADV 3CBY GLY A 362 UNP O14641 SEE REMARK 999
SEQADV 3CBY TRP A 363 UNP O14641 SEE REMARK 999
SEQADV 3CBY ILE A 364 UNP O14641 SEE REMARK 999
SEQADV 3CBY ASP A 365 UNP O14641 SEE REMARK 999
SEQADV 3CBY GLY A 366 UNP O14641 SEE REMARK 999
SEQADV 3CBY LYS A 367 UNP O14641 SEE REMARK 999
SEQADV 3CBY GLY B 260 UNP O14641 EXPRESSION TAG
SEQADV 3CBY SER B 261 UNP O14641 EXPRESSION TAG
SEQADV 3CBY HIS B 262 UNP O14641 EXPRESSION TAG
SEQADV 3CBY MET B 263 UNP O14641 EXPRESSION TAG
SEQADV 3CBY SER B 354 UNP O14641 CYS 354 ENGINEERED MUTATION
SEQADV 3CBY GLY B 355 UNP O14641 LINKER
SEQADV 3CBY GLY B 356 UNP O14641 LINKER
SEQADV 3CBY GLY B 357 UNP O14641 LINKER
SEQADV 3CBY TRP B 358 UNP O14641 SEE REMARK 999
SEQADV 3CBY LYS B 359 UNP O14641 SEE REMARK 999
SEQADV 3CBY ASP B 360 UNP O14641 SEE REMARK 999
SEQADV 3CBY TYR B 361 UNP O14641 SEE REMARK 999
SEQADV 3CBY GLY B 362 UNP O14641 SEE REMARK 999
SEQADV 3CBY TRP B 363 UNP O14641 SEE REMARK 999
SEQADV 3CBY ILE B 364 UNP O14641 SEE REMARK 999
SEQADV 3CBY ASP B 365 UNP O14641 SEE REMARK 999
SEQADV 3CBY GLY B 366 UNP O14641 SEE REMARK 999
SEQADV 3CBY LYS B 367 UNP O14641 SEE REMARK 999
SEQRES 1 A 108 GLY SER HIS MET ASN ILE ILE THR VAL THR LEU ASN MET
SEQRES 2 A 108 GLU LYS TYR ASN PHE LEU GLY ILE SER ILE VAL GLY GLN
SEQRES 3 A 108 SER ASN GLU ARG GLY ASP GLY GLY ILE TYR ILE GLY SER
SEQRES 4 A 108 ILE MET LYS GLY GLY ALA VAL ALA ALA ASP GLY ARG ILE
SEQRES 5 A 108 GLU PRO GLY ASP MET LEU LEU GLN VAL ASN ASP MET ASN
SEQRES 6 A 108 PHE GLU ASN MET SER ASN ASP ASP ALA VAL ARG VAL LEU
SEQRES 7 A 108 ARG ASP ILE VAL HIS LYS PRO GLY PRO ILE VAL LEU THR
SEQRES 8 A 108 VAL ALA LYS SER GLY GLY GLY TRP LYS ASP TYR GLY TRP
SEQRES 9 A 108 ILE ASP GLY LYS
SEQRES 1 B 108 GLY SER HIS MET ASN ILE ILE THR VAL THR LEU ASN MET
SEQRES 2 B 108 GLU LYS TYR ASN PHE LEU GLY ILE SER ILE VAL GLY GLN
SEQRES 3 B 108 SER ASN GLU ARG GLY ASP GLY GLY ILE TYR ILE GLY SER
SEQRES 4 B 108 ILE MET LYS GLY GLY ALA VAL ALA ALA ASP GLY ARG ILE
SEQRES 5 B 108 GLU PRO GLY ASP MET LEU LEU GLN VAL ASN ASP MET ASN
SEQRES 6 B 108 PHE GLU ASN MET SER ASN ASP ASP ALA VAL ARG VAL LEU
SEQRES 7 B 108 ARG ASP ILE VAL HIS LYS PRO GLY PRO ILE VAL LEU THR
SEQRES 8 B 108 VAL ALA LYS SER GLY GLY GLY TRP LYS ASP TYR GLY TRP
SEQRES 9 B 108 ILE ASP GLY LYS
HET EDO A2002 4
HET EDO B2001 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 2(C2 H6 O2)
FORMUL 5 HOH *198(H2 O)
HELIX 1 1 GLY A 303 GLY A 309 1 7
HELIX 2 2 SER A 329 HIS A 342 1 14
HELIX 3 3 SER A 354 GLY A 356 5 3
HELIX 4 4 GLY B 303 GLY B 309 1 7
HELIX 5 5 SER B 329 HIS B 342 1 14
SHEET 1 A 4 ILE A 265 LEU A 270 0
SHEET 2 A 4 ILE A 347 ALA A 352 -1 O ILE A 347 N LEU A 270
SHEET 3 A 4 MET A 316 VAL A 320 -1 N LEU A 318 O THR A 350
SHEET 4 A 4 MET A 323 ASN A 324 -1 O MET A 323 N VAL A 320
SHEET 1 B 3 ILE A 294 ILE A 299 0
SHEET 2 B 3 ILE A 280 GLY A 284 -1 N VAL A 283 O TYR A 295
SHEET 3 B 3 LYS B 359 TRP B 363 -1 O LYS B 359 N GLY A 284
SHEET 1 C 3 TRP A 358 TRP A 363 0
SHEET 2 C 3 ILE B 280 GLN B 285 -1 O GLY B 284 N LYS A 359
SHEET 3 C 3 GLY B 293 ILE B 299 -1 O TYR B 295 N VAL B 283
SHEET 1 D 4 ILE B 265 LEU B 270 0
SHEET 2 D 4 ILE B 347 ALA B 352 -1 O ILE B 347 N LEU B 270
SHEET 3 D 4 MET B 316 VAL B 320 -1 N LEU B 318 O THR B 350
SHEET 4 D 4 MET B 323 ASN B 324 -1 O MET B 323 N VAL B 320
SITE 1 AC1 4 SER A 298 ASP A 360 GLY A 362 HOH B1193
SITE 1 AC2 5 SER B 298 ASP B 360 GLY B 362 TRP B 363
SITE 2 AC2 5 HOH B1193
CRYST1 136.303 52.187 31.911 90.00 100.33 90.00 C 1 2 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 0.007337 0.000000 0.001337 0.00000
SCALE2 0.000000 0.019162 0.000000 0.00000
SCALE3 0.000000 0.000000 0.031853 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
