HEADER TRANSFERASE 04-SEP-01 1JWO
TITLE CRYSTAL STRUCTURE ANALYSIS OF THE SH2 DOMAIN OF THE CSK HOMOLOGOUS
TITLE 2 KINASE CHK
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CSK HOMOLOGOUS KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH2 DOMAIN;
COMPND 5 SYNONYM: CHK, MEGAKARYOCYTE-ASSOCIATED TYROSINE-PROTEIN KINASE,
COMPND 6 TYROSINE-PROTEIN KINASE CTK, PROTEIN KINASE HYL, HEMATOPOIETIC
COMPND 7 CONSENSUS TYROSINE-LACKING KINASE;
COMPND 8 EC: 2.7.1.112;
COMPND 9 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: MATK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS ANTIPARALLEL BETA SHEET, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.V.S.MURTHY,G.D.WEBSTER
REVDAT 3 16-AUG-23 1JWO 1 REMARK
REVDAT 2 24-FEB-09 1JWO 1 VERSN
REVDAT 1 12-SEP-01 1JWO 0
JRNL AUTH T.V.S.MURTHY,G.D.WEBSTER
JRNL TITL RECOGNITION OF THE HER-2/NEU RECEPTOR BY THE SH2 DOMAIN OF
JRNL TITL 2 THE CSK HOMOLOGOUS KINASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 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 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 3 NUMBER OF REFLECTIONS : 3080
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.300
REMARK 3 FREE R VALUE TEST SET COUNT : 140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 785
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 48
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.79000
REMARK 3 B22 (A**2) : 0.23000
REMARK 3 B33 (A**2) : 0.80000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.28000
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): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.046 ; 1.690
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.016 ; 6.969
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.322 ; 4.552
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JWO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014271.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUN-01
REMARK 200 TEMPERATURE (KELVIN) : 298.0
REMARK 200 PH : 9.0
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 : NI MIRROR + NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 3237
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 41.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.900
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.10800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.30400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1SHA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 9.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 292.0K
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 32.07300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.34800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 32.07300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.34800
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: 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 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 GLU A 182
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ALA A 150 CB
REMARK 480 ARG A 164 CB CG CD
REMARK 480 ALA A 202 CB
REMARK 480 LYS A 206 CG CD
REMARK 480 ARG A 212 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 CG ARG A 164 O HOH A 305 0.71
REMARK 500 O ASP A 181 CA GLU A 182 0.73
REMARK 500 O ASP A 181 N GLU A 182 0.78
REMARK 500 O GLY A 201 CB ALA A 202 1.48
REMARK 500 O GLN A 130 O HOH A 317 1.54
REMARK 500 CD ARG A 164 O HOH A 305 1.55
REMARK 500 O ASP A 181 CB GLU A 182 1.72
REMARK 500 N GLY A 201 O HOH A 335 1.76
REMARK 500 C LYS A 200 O HOH A 335 1.81
REMARK 500 CG2 THR A 205 O HOH A 310 1.82
REMARK 500 CB ARG A 164 O HOH A 305 1.84
REMARK 500 CG HIS A 152 NH2 ARG A 170 1.86
REMARK 500 ND1 HIS A 152 NH2 ARG A 170 1.87
REMARK 500 CD2 HIS A 173 O HOH A 348 1.89
REMARK 500 NE2 HIS A 173 O HOH A 348 1.94
REMARK 500 C ASP A 181 N ALA A 183 1.97
REMARK 500 CE2 TYR A 169 CG2 ILE A 203 2.09
REMARK 500 O GLY A 154 O HOH A 348 2.10
REMARK 500 OE2 GLU A 140 NE ARG A 209 2.13
REMARK 500 O ILE A 180 N ALA A 183 2.14
REMARK 500 CA GLY A 176 O HOH A 322 2.14
REMARK 500 O HOH A 301 O HOH A 327 2.17
REMARK 500 CD1 TYR A 169 O HOH A 309 2.17
REMARK 500 O LYS A 200 O HOH A 335 2.19
REMARK 500 CB ALA A 202 O HOH A 304 2.19
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 CZ ARG A 164 CG GLU A 182 4546 0.80
REMARK 500 NH2 ARG A 164 CG GLU A 182 4546 1.00
REMARK 500 NH1 ARG A 164 CD GLU A 182 4546 1.04
REMARK 500 NH1 ARG A 164 OE1 GLU A 182 4546 1.18
REMARK 500 NH1 ARG A 164 CG GLU A 182 4546 1.36
REMARK 500 CZ ARG A 164 CD GLU A 182 4546 1.54
REMARK 500 NZ LYS A 211 O HOH A 340 1554 1.58
REMARK 500 NH2 ARG A 164 CB GLU A 182 4546 1.64
REMARK 500 O HOH A 311 O HOH A 340 1554 1.72
REMARK 500 O GLU A 182 SG CYS A 187 2656 2.06
REMARK 500 O HOH A 326 O HOH A 326 2555 2.07
REMARK 500 NE ARG A 164 CG GLU A 182 4546 2.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 122 CE3 TRP A 122 CZ3 -0.123
REMARK 500 PHE A 144 CE1 PHE A 144 CZ -0.140
REMARK 500 VAL A 146 CA VAL A 146 CB -0.128
REMARK 500 VAL A 146 CB VAL A 146 CG1 0.330
REMARK 500 ALA A 150 CA ALA A 150 CB -0.154
REMARK 500 VAL A 160 CB VAL A 160 CG2 -0.139
REMARK 500 ARG A 164 CD ARG A 164 NE 0.158
REMARK 500 HIS A 168 CB HIS A 168 CG -0.106
REMARK 500 TYR A 169 CB TYR A 169 CG 0.121
REMARK 500 TYR A 169 CD1 TYR A 169 CE1 0.099
REMARK 500 TYR A 169 CE1 TYR A 169 CZ -0.123
REMARK 500 ASP A 181 C GLU A 182 N -0.476
REMARK 500 VAL A 184 CA VAL A 184 CB -0.137
REMARK 500 ALA A 202 CA ALA A 202 CB 0.984
REMARK 500 LYS A 211 CD LYS A 211 CE 0.162
REMARK 500 ARG A 212 CG ARG A 212 CD 0.469
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 117 CA - CB - CG ANGL. DEV. = -15.7 DEGREES
REMARK 500 LEU A 119 CB - CG - CD1 ANGL. DEV. = -46.4 DEGREES
REMARK 500 LEU A 119 CB - CG - CD2 ANGL. DEV. = -10.9 DEGREES
REMARK 500 GLY A 129 CA - C - N ANGL. DEV. = -13.4 DEGREES
REMARK 500 GLN A 137 N - CA - C ANGL. DEV. = 17.5 DEGREES
REMARK 500 ASP A 141 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 147 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ALA A 150 CB - CA - C ANGL. DEV. = 14.1 DEGREES
REMARK 500 ALA A 150 N - CA - CB ANGL. DEV. = 10.7 DEGREES
REMARK 500 ARG A 164 NE - CZ - NH1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 TYR A 169 CB - CG - CD1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ASP A 175 CB - CG - OD2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 HIS A 177 N - CA - CB ANGL. DEV. = -14.6 DEGREES
REMARK 500 ASP A 181 CB - CG - OD2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ASP A 181 CA - C - N ANGL. DEV. = -19.5 DEGREES
REMARK 500 ASP A 181 O - C - N ANGL. DEV. = -86.5 DEGREES
REMARK 500 GLU A 182 C - N - CA ANGL. DEV. = -17.6 DEGREES
REMARK 500 GLU A 182 CA - C - N ANGL. DEV. = -21.3 DEGREES
REMARK 500 GLU A 182 O - C - N ANGL. DEV. = 20.1 DEGREES
REMARK 500 ALA A 183 C - N - CA ANGL. DEV. = -29.0 DEGREES
REMARK 500 ALA A 183 N - CA - C ANGL. DEV. = 17.2 DEGREES
REMARK 500 CYS A 187 CA - CB - SG ANGL. DEV. = -13.3 DEGREES
REMARK 500 ASP A 191 OD1 - CG - OD2 ANGL. DEV. = -14.5 DEGREES
REMARK 500 ASP A 191 CB - CG - OD2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 MET A 192 CB - CG - SD ANGL. DEV. = -22.4 DEGREES
REMARK 500 GLU A 194 CB - CA - C ANGL. DEV. = -14.6 DEGREES
REMARK 500 ALA A 202 N - CA - CB ANGL. DEV. = -23.2 DEGREES
REMARK 500 LYS A 206 CA - CB - CG ANGL. DEV. = 23.1 DEGREES
REMARK 500 ARG A 209 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A 212 CG - CD - NE ANGL. DEV. = 24.0 DEGREES
REMARK 500 LYS A 213 N - CA - CB ANGL. DEV. = 11.3 DEGREES
REMARK 500 LYS A 213 N - CA - C ANGL. DEV. = -24.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 139 152.85 -32.29
REMARK 500 GLU A 140 104.55 171.08
REMARK 500 ALA A 150 -63.38 -99.12
REMARK 500 ARG A 164 -18.85 83.29
REMARK 500 ASP A 175 -34.06 69.52
REMARK 500 LEU A 178 162.88 172.22
REMARK 500 ASP A 181 172.87 -31.35
REMARK 500 GLU A 182 -30.23 51.94
REMARK 500 ALA A 183 -88.60 -76.78
REMARK 500 MET A 190 62.34 -64.52
REMARK 500 ASP A 191 -48.48 165.01
REMARK 500 VAL A 193 -70.45 -47.46
REMARK 500 TYR A 196 1.78 -67.75
REMARK 500 ALA A 202 -42.46 136.02
REMARK 500 VAL A 208 -84.11 -128.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASP A 181 -68.77
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JWO A 117 213 UNP P42679 MATK_HUMAN 117 213
SEQRES 1 A 97 LEU SER LEU MET PRO TRP PHE HIS GLY LYS ILE SER GLY
SEQRES 2 A 97 GLN GLU ALA VAL GLN GLN LEU GLN PRO PRO GLU ASP GLY
SEQRES 3 A 97 LEU PHE LEU VAL ARG GLU SER ALA ARG HIS PRO GLY ASP
SEQRES 4 A 97 TYR VAL LEU CYS VAL SER PHE GLY ARG ASP VAL ILE HIS
SEQRES 5 A 97 TYR ARG VAL LEU HIS ARG ASP GLY HIS LEU THR ILE ASP
SEQRES 6 A 97 GLU ALA VAL PHE PHE CYS ASN LEU MET ASP MET VAL GLU
SEQRES 7 A 97 HIS TYR SER LYS ASP LYS GLY ALA ILE CYS THR LYS LEU
SEQRES 8 A 97 VAL ARG PRO LYS ARG LYS
FORMUL 2 HOH *48(H2 O)
HELIX 1 1 SER A 128 LEU A 136 1 9
HELIX 2 2 ASN A 188 ASP A 199 1 12
SHEET 1 A 5 PHE A 123 GLY A 125 0
SHEET 2 A 5 PHE A 144 GLU A 148 1 N GLU A 148 O GLY A 125
SHEET 3 A 5 TYR A 156 PHE A 162 -1 O VAL A 157 N ARG A 147
SHEET 4 A 5 ASP A 165 HIS A 173 -1 O VAL A 171 N TYR A 156
SHEET 5 A 5 HIS A 177 LEU A 178 -1 O LEU A 178 N LEU A 172
CRYST1 64.146 58.696 28.817 90.00 115.36 90.00 C 1 2 1 4
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 0.015589 0.000000 0.007387 0.00000
SCALE2 0.000000 0.017037 0.000000 0.00000
SCALE3 0.000000 0.000000 0.038401 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
