HEADER SIGNALING PROTEIN 27-OCT-08 3F0W
TITLE HUMAN NUMB-LIKE PROTEIN, PHOSPHOTYROSINE INTERACTION DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUMB-LIKE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PHOSPHOTYROSINE INTERACTION DOMAIN, UNP RESIDUES 60-204;
COMPND 5 SYNONYM: NUMB-R;
COMPND 6 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: NUMBL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) R3 PRARE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4
KEYWDS PH DOMAIN-LIKE, PID DOMAIN, PHOSPHOPROTEIN, SIGNALING PROTEIN,
KEYWDS 2 STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC
EXPDTA X-RAY DIFFRACTION
AUTHOR L.LEHTIO,M.MOCHE,J.ANDERSSON,C.H.ARROWSMITH,H.BERGLUND,C.BOUNTRA,R.D
AUTHOR 2 BUSAM,R.COLLINS,L.G.DAHLGREN,A.M.EDWARDS,S.FLODIN,A.FLORES,
AUTHOR 3 S.GRASLUND,M.HAMMARSTROM,A.JOHANSSON,I.JOHANSSON,T.KARLBERG,
AUTHOR 4 T.KOTENYOVA,M.E.NILSSON,T.NYMAN,C.PERSSON,J.SAGEMARK,H.SCHUELER,
AUTHOR 5 A.G.THORSELL,L.TRESAUGUES,S.VAN DEN BERG,J.WEIGELT,M.WELIN,
AUTHOR 6 M.WIKSTROM,M.WISNIEWSKA,P.NORDLUND,STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 7 (SGC)
REVDAT 4 01-NOV-23 3F0W 1 REMARK SEQADV
REVDAT 3 13-JUL-11 3F0W 1 VERSN
REVDAT 2 24-FEB-09 3F0W 1 VERSN
REVDAT 1 04-NOV-08 3F0W 0
JRNL AUTH L.LEHTIO,M.MOCHE,J.ANDERSSON,C.H.ARROWSMITH,H.BERGLUND,
JRNL AUTH 2 C.BOUNTRA,R.D BUSAM,R.COLLINS,L.G.DAHLGREN,A.M.EDWARDS,
JRNL AUTH 3 S.FLODIN,A.FLORES,S.GRASLUND,M.HAMMARSTROM,A.JOHANSSON,
JRNL AUTH 4 I.JOHANSSON,T.KARLBERG,T.KOTENYOVA,M.E.NILSSON,T.NYMAN,
JRNL AUTH 5 C.PERSSON,J.SAGEMARK,H.SCHUELER,A.G.THORSELL,L.TRESAUGUES,
JRNL AUTH 6 S.VAN DEN BERG,J.WEIGELT,M.WELIN,M.WIKSTROM,M.WISNIEWSKA,
JRNL AUTH 7 P.NORDLUND
JRNL TITL HUMAN NUMB-LIKE PROTEIN, PHOSPHOTYROSINE INTERACTION DOMAIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0044
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 4591
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) : 0.242
REMARK 3 R VALUE (WORKING SET) : 0.238
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 510
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 334
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3460
REMARK 3 BIN FREE R VALUE SET COUNT : 37
REMARK 3 BIN FREE R VALUE : 0.3740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1188
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
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) : 16.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.45000
REMARK 3 B22 (A**2) : -0.45000
REMARK 3 B33 (A**2) : 0.67000
REMARK 3 B12 (A**2) : -0.22000
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): 0.401
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.345
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 38.630
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.903
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1213 ; 0.006 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 833 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1634 ; 0.923 ; 1.943
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2012 ; 0.773 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 151 ; 5.479 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 56 ;30.663 ;23.036
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 210 ;13.961 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;14.151 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 179 ; 0.055 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1353 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 259 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 757 ; 0.230 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 311 ; 0.029 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1205 ; 0.445 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 456 ; 0.591 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 429 ; 1.034 ; 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 : 3
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 48 A 81
REMARK 3 ORIGIN FOR THE GROUP (A): -31.8420 -6.4480 -23.5320
REMARK 3 T TENSOR
REMARK 3 T11: 0.9563 T22: 0.6453
REMARK 3 T33: 0.4457 T12: 0.0621
REMARK 3 T13: 0.1518 T23: 0.0321
REMARK 3 L TENSOR
REMARK 3 L11: 2.1384 L22: 3.3581
REMARK 3 L33: 8.2106 L12: -0.2727
REMARK 3 L13: 3.2853 L23: 2.7856
REMARK 3 S TENSOR
REMARK 3 S11: -0.0631 S12: -0.3405 S13: -0.1138
REMARK 3 S21: 0.7393 S22: 0.0613 S23: 0.2286
REMARK 3 S31: 0.8699 S32: -0.5646 S33: 0.0019
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 82 A 109
REMARK 3 ORIGIN FOR THE GROUP (A): -14.2200 6.4810 -20.2850
REMARK 3 T TENSOR
REMARK 3 T11: 0.4745 T22: 1.1277
REMARK 3 T33: 0.2204 T12: -0.0721
REMARK 3 T13: -0.1162 T23: -0.2123
REMARK 3 L TENSOR
REMARK 3 L11: 11.2080 L22: 9.1133
REMARK 3 L33: 7.4993 L12: 1.6942
REMARK 3 L13: 2.1778 L23: -3.5238
REMARK 3 S TENSOR
REMARK 3 S11: -0.4591 S12: 0.1831 S13: -0.0602
REMARK 3 S21: 0.1696 S22: 0.6222 S23: -0.8137
REMARK 3 S31: -0.5842 S32: 1.7595 S33: -0.1631
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 : A 110 A 202
REMARK 3 ORIGIN FOR THE GROUP (A): -26.5980 5.3220 -19.4180
REMARK 3 T TENSOR
REMARK 3 T11: 0.5069 T22: 0.4089
REMARK 3 T33: 0.2577 T12: 0.1261
REMARK 3 T13: -0.0569 T23: -0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 2.5064 L22: 5.5687
REMARK 3 L33: 8.8635 L12: 0.3693
REMARK 3 L13: 0.3556 L23: 3.5567
REMARK 3 S TENSOR
REMARK 3 S11: -0.5163 S12: 0.0536 S13: 0.0605
REMARK 3 S21: 0.1575 S22: 0.4102 S23: 0.2142
REMARK 3 S31: -0.3526 S32: 0.7617 S33: 0.1060
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 3F0W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1000050006.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-APR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 5126
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.2800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.77
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.56500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.030
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 1WJ1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24 % PEG 8000, 0.1M LITHIUM SULPHATE,
REMARK 280 0.1M SODIUM ACETATE, PH 4.7, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.23333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 33.11667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 33.11667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 66.23333
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 300 REMARK: ASYMMETRIC UNIT CONTAINS A BIOLOGICAL MONOMER. STRONG
REMARK 300 INTERACTIONS GENERATED BY SYMMETRY ARE FORMED BY THE EXPRESSION TAG.
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -66.23333
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CL CL A 2 LIES ON A SPECIAL POSITION.
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 MET A 37
REMARK 465 HIS A 38
REMARK 465 HIS A 39
REMARK 465 HIS A 40
REMARK 465 HIS A 41
REMARK 465 HIS A 42
REMARK 465 HIS A 43
REMARK 465 SER A 44
REMARK 465 SER A 45
REMARK 465 GLY A 46
REMARK 465 VAL A 47
REMARK 465 ARG A 111
REMARK 465 LYS A 112
REMARK 465 GLU A 203
REMARK 465 LYS A 204
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 ASP A 48 CG OD1 OD2
REMARK 470 LEU A 49 CG CD1 CD2
REMARK 470 ARG A 168 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 178 CG CD CE NZ
REMARK 470 ARG A 202 CG CD NE CZ NH1 NH2
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 SER A 93 OG SER A 145 2.16
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 HIS A 64 42.95 -74.55
REMARK 500 MET A 109 -60.42 -109.02
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 SO4 A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 2
DBREF 3F0W A 60 204 UNP Q9Y6R0 NUMBL_HUMAN 60 204
SEQADV 3F0W MET A 37 UNP Q9Y6R0 INITIATING METHIONINE
SEQADV 3F0W HIS A 38 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W HIS A 39 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W HIS A 40 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W HIS A 41 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W HIS A 42 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W HIS A 43 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W SER A 44 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W SER A 45 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W GLY A 46 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W VAL A 47 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W ASP A 48 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W LEU A 49 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W GLY A 50 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W THR A 51 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W GLU A 52 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W ASN A 53 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W LEU A 54 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W TYR A 55 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W PHE A 56 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W GLN A 57 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W SER A 58 UNP Q9Y6R0 EXPRESSION TAG
SEQADV 3F0W MET A 59 UNP Q9Y6R0 EXPRESSION TAG
SEQRES 1 A 168 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 168 GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER ARG
SEQRES 3 A 168 PRO HIS GLN TRP GLN ALA ASP GLU ASP ALA VAL ARG LYS
SEQRES 4 A 168 GLY THR CYS SER PHE PRO VAL ARG TYR LEU GLY HIS VAL
SEQRES 5 A 168 GLU VAL GLU GLU SER ARG GLY MET HIS VAL CYS GLU ASP
SEQRES 6 A 168 ALA VAL LYS LYS LEU LYS ALA MET GLY ARG LYS SER VAL
SEQRES 7 A 168 LYS SER VAL LEU TRP VAL SER ALA ASP GLY LEU ARG VAL
SEQRES 8 A 168 VAL ASP ASP LYS THR LYS ASP LEU LEU VAL ASP GLN THR
SEQRES 9 A 168 ILE GLU LYS VAL SER PHE CYS ALA PRO ASP ARG ASN LEU
SEQRES 10 A 168 ASP LYS ALA PHE SER TYR ILE CYS ARG ASP GLY THR THR
SEQRES 11 A 168 ARG ARG TRP ILE CYS HIS CYS PHE LEU ALA LEU LYS ASP
SEQRES 12 A 168 SER GLY GLU ARG LEU SER HIS ALA VAL GLY CYS ALA PHE
SEQRES 13 A 168 ALA ALA CYS LEU GLU ARG LYS GLN ARG ARG GLU LYS
HET SO4 A 3 5
HET CL A 1 1
HET CL A 2 1
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
FORMUL 2 SO4 O4 S 2-
FORMUL 3 CL 2(CL 1-)
HELIX 1 1 ASN A 53 SER A 61 1 9
HELIX 2 2 TRP A 66 LYS A 75 1 10
HELIX 3 3 GLY A 95 ALA A 108 1 14
HELIX 4 4 SER A 180 ARG A 202 1 23
SHEET 1 A 7 LEU A 135 THR A 140 0
SHEET 2 A 7 GLY A 124 ASP A 129 -1 N LEU A 125 O GLN A 139
SHEET 3 A 7 VAL A 114 VAL A 120 -1 N TRP A 119 O ARG A 126
SHEET 4 A 7 CYS A 78 VAL A 90 -1 N CYS A 78 O VAL A 120
SHEET 5 A 7 ARG A 168 ALA A 176 -1 O CYS A 171 N VAL A 88
SHEET 6 A 7 ALA A 156 ASP A 163 -1 N CYS A 161 O ILE A 170
SHEET 7 A 7 VAL A 144 PRO A 149 -1 N PHE A 146 O ILE A 160
SITE 1 AC1 4 ARG A 94 GLY A 95 MET A 96 HIS A 97
SITE 1 AC2 3 ARG A 74 ARG A 198 ARG A 201
SITE 1 AC3 2 GLU A 52 ARG A 94
CRYST1 55.150 55.150 99.350 90.00 90.00 120.00 P 32 2 1 6
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 0.018132 0.010469 0.000000 0.00000
SCALE2 0.000000 0.020937 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010065 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
