HEADER HYDROLASE 06-DEC-16 5MLA
TITLE CRYSTAL STRUCTURE OF HUMAN RAS IN COMPLEX WITH DARPIN K55
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GTPASE KRAS;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: K-RAS 2,KI-RAS,C-K-RAS,C-KI-RAS;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DARPIN K55;
COMPND 8 CHAIN: B;
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: KRAS, KRAS2, RASK2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 10 ORGANISM_TAXID: 32630;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS RAS, DARPIN, NUCLEOTIDE EXCHANGE, INHIBITION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.E.DEBRECZENI,S.GUILLARD,P.KOLASINSKA-ZWIERZ,J.BREED,J.ZHANG,N.BERY,
AUTHOR 2 R.MARWOOD,J.TART,R.OVERMAN,P.STOCKI,B.MISTRY,C.PHILLIPS,T.RABBITTS,
AUTHOR 3 R.JACKSON,R.MINTER
REVDAT 1 20-DEC-17 5MLA 0
JRNL AUTH S.GUILLARD,P.KOLASINSKA-ZWIERZ,J.DEBRECZENI,J.BREED,J.ZHANG,
JRNL AUTH 2 N.BERY,R.MARWOOD,J.TART,R.OVERMAN,P.STOCKI,B.MINSTRY,
JRNL AUTH 3 C.PHILLIPS,T.RABBITTS,R.JACKSON,R.MINTER
JRNL TITL INHIBITION OF RAS NUCLEOTIDE EXCHANGE BY A DARPIN:
JRNL TITL 2 STRUCTURAL CHARACTERISATION AND EFFECTS ON DOWNSTREAM
JRNL TITL 3 SIGNALLING BY ACTIVE RAS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.41
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 14863
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 766
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) : 2.19
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.25
REMARK 3 REFLECTION IN BIN (WORKING SET) : 868
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 74.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.3110
REMARK 3 BIN FREE R VALUE SET COUNT : 35
REMARK 3 BIN FREE R VALUE : 0.3140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2305
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 85
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.80000
REMARK 3 B22 (A**2) : -0.80000
REMARK 3 B33 (A**2) : 2.58000
REMARK 3 B12 (A**2) : -0.40000
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): 0.285
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.210
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.185
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.696
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2400 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2264 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3267 ; 1.612 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5170 ; 1.021 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 308 ; 6.386 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 107 ;35.890 ;24.393
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 385 ;15.032 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;19.229 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 382 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2753 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 544 ; 0.002 ; 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): 1232 ; 0.986 ; 2.448
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1231 ; 0.985 ; 2.447
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1540 ; 1.643 ; 3.665
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1541 ; 1.642 ; 3.666
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1168 ; 1.412 ; 2.676
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1148 ; 1.288 ; 2.645
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1696 ; 2.168 ; 3.904
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2654 ; 4.068 ;20.021
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2621 ; 3.955 ;19.801
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 : 2
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 1 A 164
REMARK 3 ORIGIN FOR THE GROUP (A): 76.4172 98.3311 6.1935
REMARK 3 T TENSOR
REMARK 3 T11: 0.0148 T22: 0.0069
REMARK 3 T33: 0.0551 T12: 0.0086
REMARK 3 T13: 0.0185 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 3.7416 L22: 1.9962
REMARK 3 L33: 2.2196 L12: -0.6032
REMARK 3 L13: 0.4357 L23: 0.5181
REMARK 3 S TENSOR
REMARK 3 S11: -0.0488 S12: -0.0498 S13: 0.1052
REMARK 3 S21: 0.0203 S22: -0.0129 S23: -0.0163
REMARK 3 S31: -0.0961 S32: -0.1095 S33: 0.0617
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 19 B 160
REMARK 3 ORIGIN FOR THE GROUP (A): 77.2138 93.2809 31.6911
REMARK 3 T TENSOR
REMARK 3 T11: 0.0684 T22: 0.2342
REMARK 3 T33: 0.1916 T12: -0.0735
REMARK 3 T13: 0.0031 T23: 0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 2.2956 L22: 3.8391
REMARK 3 L33: 2.8346 L12: 0.2651
REMARK 3 L13: -0.2109 L23: -0.6755
REMARK 3 S TENSOR
REMARK 3 S11: 0.1040 S12: -0.4095 S13: -0.4022
REMARK 3 S21: 0.2586 S22: -0.0762 S23: 0.4526
REMARK 3 S31: 0.2811 S32: -0.3183 S33: -0.0278
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 5MLA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1200002639.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15629
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 56.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.71600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG8000, 200MM CALCIUM ACETATE,
REMARK 280 100MM SODIUM CACODYLATE PH6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 56.41500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.57122
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 22.25667
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 56.41500
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 32.57122
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 22.25667
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 56.41500
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 32.57122
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 22.25667
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 65.14243
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 44.51333
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 65.14243
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 44.51333
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 65.14243
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 44.51333
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: 3190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 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 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 HOH A 361 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 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 LYS A 165
REMARK 465 HIS A 166
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 HIS B 11
REMARK 465 HIS B 12
REMARK 465 SER B 13
REMARK 465 SER B 14
REMARK 465 GLY B 15
REMARK 465 HIS B 16
REMARK 465 ILE B 17
REMARK 465 GLU B 18
REMARK 465 ASP B 161
REMARK 465 ILE B 162
REMARK 465 SER B 163
REMARK 465 ILE B 164
REMARK 465 ASP B 165
REMARK 465 ASN B 166
REMARK 465 GLY B 167
REMARK 465 ASN B 168
REMARK 465 GLU B 169
REMARK 465 ASP B 170
REMARK 465 LEU B 171
REMARK 465 ALA B 172
REMARK 465 GLU B 173
REMARK 465 ILE B 174
REMARK 465 LEU B 175
REMARK 465 GLN B 176
REMARK 465 LYS B 177
REMARK 465 LEU B 178
REMARK 465 TYR B 179
REMARK 465 PRO B 180
REMARK 465 TYR B 181
REMARK 465 ASP B 182
REMARK 465 VAL B 183
REMARK 465 PRO B 184
REMARK 465 ASP B 185
REMARK 465 TYR B 186
REMARK 465 ALA B 187
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 GLU A 3 CG CD OE1 OE2
REMARK 470 ASP A 30 CG OD1 OD2
REMARK 470 GLU A 63 CG CD OE1 OE2
REMARK 470 LYS A 128 CG CD CE NZ
REMARK 470 ARG A 164 CD NE CZ NH1 NH2
REMARK 470 ARG B 20 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 26 CD CE NZ
REMARK 470 LYS B 27 CD CE NZ
REMARK 470 GLN B 36 CG CD OE1 NE2
REMARK 470 GLU B 39 CG CD OE1 OE2
REMARK 470 GLU B 71 CG CD OE1 OE2
REMARK 470 LYS B 78 CG CD CE NZ
REMARK 470 GLU B 104 CG CD OE1 OE2
REMARK 470 LYS B 111 CG CD CE NZ
REMARK 470 GLU B 137 CG CD OE1 OE2
REMARK 470 GLU B 140 CG CD OE1 OE2
REMARK 470 LYS B 144 CG CD CE NZ
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 ARG A 97 NE - CZ - NH2 ANGL. DEV. = 3.3 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 VAL A 12 131.13 -36.03
REMARK 500 ILE A 36 -72.91 -83.44
REMARK 500 GLU A 37 113.54 -162.99
REMARK 500 LYS A 117 42.24 72.57
REMARK 500 LYS A 117 40.72 72.57
REMARK 500 ARG A 149 -0.01 76.73
REMARK 500 ASP B 37 -39.16 -36.96
REMARK 500 ASN B 145 31.17 -96.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 17 OG
REMARK 620 2 THR A 35 OG1 84.0
REMARK 620 3 HOH A 311 O 95.1 94.5
REMARK 620 4 GSP A 202 O2B 99.7 175.7 87.3
REMARK 620 5 GSP A 202 O2G 165.8 82.4 81.9 94.0
REMARK 620 6 HOH A 318 O 90.3 84.8 174.4 93.1 92.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GSP A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 201
DBREF 5MLA A 1 166 UNP P01116 RASK_HUMAN 1 166
DBREF 5MLA B 1 187 PDB 5MLA 5MLA 1 187
SEQADV 5MLA GLY A -2 UNP P01116 EXPRESSION TAG
SEQADV 5MLA SER A -1 UNP P01116 EXPRESSION TAG
SEQADV 5MLA HIS A 0 UNP P01116 EXPRESSION TAG
SEQADV 5MLA VAL A 12 UNP P01116 GLY 12 VARIANT
SEQRES 1 A 169 GLY SER HIS MET THR GLU TYR LYS LEU VAL VAL VAL GLY
SEQRES 2 A 169 ALA VAL GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU
SEQRES 3 A 169 ILE GLN ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE
SEQRES 4 A 169 GLU ASP SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU
SEQRES 5 A 169 THR CYS LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU
SEQRES 6 A 169 GLU TYR SER ALA MET ARG ASP GLN TYR MET ARG THR GLY
SEQRES 7 A 169 GLU GLY PHE LEU CYS VAL PHE ALA ILE ASN ASN THR LYS
SEQRES 8 A 169 SER PHE GLU ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS
SEQRES 9 A 169 ARG VAL LYS ASP SER GLU ASP VAL PRO MET VAL LEU VAL
SEQRES 10 A 169 GLY ASN LYS CYS ASP LEU PRO SER ARG THR VAL ASP THR
SEQRES 11 A 169 LYS GLN ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO
SEQRES 12 A 169 PHE ILE GLU THR SER ALA LYS THR ARG GLN GLY VAL ASP
SEQRES 13 A 169 ASP ALA PHE TYR THR LEU VAL ARG GLU ILE ARG LYS HIS
SEQRES 1 B 187 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 B 187 SER GLY HIS ILE GLU GLY ARG HIS MET ASP LEU GLY LYS
SEQRES 3 B 187 LYS LEU LEU GLU ALA ALA ARG ALA GLY GLN ASP ASP GLU
SEQRES 4 B 187 VAL ARG ILE LEU MET ALA ASN GLY ALA ASP VAL ASN ALA
SEQRES 5 B 187 ASN ASP SER ALA GLY HIS THR PRO LEU HIS LEU ALA ALA
SEQRES 6 B 187 LYS ARG GLY HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS
SEQRES 7 B 187 HIS GLY ALA ASP VAL ASN ALA MET ASP ASN THR GLY PHE
SEQRES 8 B 187 THR PRO LEU HIS LEU ALA ALA LEU ARG GLY HIS LEU GLU
SEQRES 9 B 187 ILE VAL GLU VAL LEU LEU LYS ASN GLY ALA ASP VAL ASN
SEQRES 10 B 187 ALA GLN ASP ARG THR GLY ARG THR PRO LEU HIS LEU ALA
SEQRES 11 B 187 ALA LYS LEU GLY HIS LEU GLU ILE VAL GLU VAL LEU LEU
SEQRES 12 B 187 LYS ASN GLY ALA ASP VAL ASN ALA GLN ASP LYS PHE GLY
SEQRES 13 B 187 LYS THR ALA PHE ASP ILE SER ILE ASP ASN GLY ASN GLU
SEQRES 14 B 187 ASP LEU ALA GLU ILE LEU GLN LYS LEU TYR PRO TYR ASP
SEQRES 15 B 187 VAL PRO ASP TYR ALA
HET MG A 201 1
HET GSP A 202 32
HET SO4 A 203 5
HET SO4 B 201 5
HETNAM MG MAGNESIUM ION
HETNAM GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE
HETNAM SO4 SULFATE ION
FORMUL 3 MG MG 2+
FORMUL 4 GSP C10 H16 N5 O13 P3 S
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 HOH *85(H2 O)
HELIX 1 AA1 GLY A 15 ASN A 26 1 12
HELIX 2 AA2 GLN A 61 ALA A 66 5 6
HELIX 3 AA3 MET A 67 GLY A 75 1 9
HELIX 4 AA4 ASN A 86 ASP A 92 1 7
HELIX 5 AA5 ASP A 92 ASP A 105 1 14
HELIX 6 AA6 ASP A 126 GLY A 138 1 13
HELIX 7 AA7 GLY A 151 ARG A 164 1 14
HELIX 8 AA8 ARG B 20 ALA B 34 1 15
HELIX 9 AA9 GLN B 36 ASN B 46 1 11
HELIX 10 AB1 THR B 59 GLY B 68 1 10
HELIX 11 AB2 HIS B 69 HIS B 79 1 11
HELIX 12 AB3 THR B 92 ARG B 100 1 9
HELIX 13 AB4 HIS B 102 ASN B 112 1 11
HELIX 14 AB5 THR B 125 LEU B 133 1 9
HELIX 15 AB6 HIS B 135 ASN B 145 1 11
SHEET 1 AA1 6 GLU A 37 ILE A 46 0
SHEET 2 AA1 6 GLU A 49 THR A 58 -1 O CYS A 51 N VAL A 44
SHEET 3 AA1 6 THR A 2 GLY A 10 1 N VAL A 8 O LEU A 56
SHEET 4 AA1 6 GLY A 77 ALA A 83 1 O LEU A 79 N VAL A 7
SHEET 5 AA1 6 MET A 111 ASN A 116 1 O ASN A 116 N PHE A 82
SHEET 6 AA1 6 PHE A 141 GLU A 143 1 O ILE A 142 N LEU A 113
LINK OG SER A 17 MG MG A 201 1555 1555 2.01
LINK OG1 THR A 35 MG MG A 201 1555 1555 2.05
LINK MG MG A 201 O HOH A 311 1555 1555 2.15
LINK MG MG A 201 O2B GSP A 202 1555 1555 1.97
LINK MG MG A 201 O2G GSP A 202 1555 1555 1.97
LINK MG MG A 201 O HOH A 318 1555 1555 2.06
SITE 1 AC1 5 SER A 17 THR A 35 GSP A 202 HOH A 311
SITE 2 AC1 5 HOH A 318
SITE 1 AC2 24 GLY A 13 VAL A 14 GLY A 15 LYS A 16
SITE 2 AC2 24 SER A 17 ALA A 18 PHE A 28 VAL A 29
SITE 3 AC2 24 ASP A 30 THR A 35 THR A 58 GLY A 60
SITE 4 AC2 24 ASN A 116 LYS A 117 ASP A 119 LEU A 120
SITE 5 AC2 24 SER A 145 ALA A 146 LYS A 147 MG A 201
SITE 6 AC2 24 HOH A 311 HOH A 318 HOH A 322 HOH A 345
SITE 1 AC3 9 ASN A 85 PHE A 90 GLU A 91 HIS A 94
SITE 2 AC3 9 SER A 122 THR A 124 LEU A 133 TYR A 137
SITE 3 AC3 9 HOH A 350
SITE 1 AC4 5 LYS A 5 ASP A 153 TYR A 157 HOH A 303
SITE 2 AC4 5 ARG B 121
CRYST1 112.830 112.830 66.770 90.00 90.00 120.00 H 3 9
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 0.008863 0.005117 0.000000 0.00000
SCALE2 0.000000 0.010234 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014977 0.00000
(ATOM LINES ARE NOT SHOWN.)
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