HEADER SIGNALING PROTEIN 26-OCT-16 5M6X
TITLE CRYSTAL STRUCTURE OF HUMAN RHOGAP MUTATED IN ITS ARGININE FINGER
TITLE 2 (R85A) IN COMPLEX WITH RHOA.GDP.MGF3- HUMAN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RHO GTPASE-ACTIVATING PROTEIN 1;
COMPND 3 CHAIN: A, H;
COMPND 4 SYNONYM: CDC42 GTPASE-ACTIVATING PROTEIN,GTPASE-ACTIVATING PROTEIN
COMPND 5 RHOGAP,RHO-RELATED SMALL GTPASE PROTEIN ACTIVATOR,RHO-TYPE GTPASE-
COMPND 6 ACTIVATING PROTEIN 1,P50-RHOGAP;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: TRANSFORMING PROTEIN RHOA;
COMPND 10 CHAIN: B, I;
COMPND 11 SYNONYM: RHO CDNA CLONE 12,H12;
COMPND 12 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: ARHGAP1, CDC42GAP, RHOGAP1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: RHOA, ARH12, ARHA, RHO12;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS RHOGAP, ARGININE FINGER, RHOA, TRANSITION STATE, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.PELLEGRINI,M.W.BOWLER
REVDAT 3 17-JAN-24 5M6X 1 REMARK LINK
REVDAT 2 06-SEP-17 5M6X 1 JRNL
REVDAT 1 17-MAY-17 5M6X 0
JRNL AUTH Y.JIN,R.W.MOLT,E.PELLEGRINI,M.J.CLIFF,M.W.BOWLER,
JRNL AUTH 2 N.G.J.RICHARDS,G.M.BLACKBURN,J.P.WALTHO
JRNL TITL ASSESSING THE INFLUENCE OF MUTATION ON GTPASE TRANSITION
JRNL TITL 2 STATES BY USING X-RAY CRYSTALLOGRAPHY, (19) F NMR, AND DFT
JRNL TITL 3 APPROACHES.
JRNL REF ANGEW. CHEM. INT. ED. ENGL. V. 56 9732 2017
JRNL REFN ESSN 1521-3773
JRNL PMID 28498638
JRNL DOI 10.1002/ANIE.201703074
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 76.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.1
REMARK 3 NUMBER OF REFLECTIONS : 23276
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) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1260
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1777
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.51
REMARK 3 BIN R VALUE (WORKING SET) : 0.2900
REMARK 3 BIN FREE R VALUE SET COUNT : 107
REMARK 3 BIN FREE R VALUE : 0.3220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5838
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 183
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.91000
REMARK 3 B22 (A**2) : -2.06000
REMARK 3 B33 (A**2) : -0.15000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.60000
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): 0.361
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.269
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.050
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.907
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.857
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6047 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5817 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8224 ; 1.135 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13391 ; 0.879 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 728 ; 5.027 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 289 ;34.022 ;25.017
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1042 ;11.878 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;11.792 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 937 ; 0.060 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6769 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1348 ; 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): 2927 ; 0.594 ; 2.435
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2926 ; 0.594 ; 2.434
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3650 ; 1.108 ; 3.646
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3651 ; 1.108 ; 3.647
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3120 ; 0.362 ; 2.472
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3106 ; 0.362 ; 2.476
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4556 ; 0.713 ; 3.674
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6753 ; 2.106 ;18.520
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6712 ; 2.058 ;18.537
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 : NULL
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 5M6X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1200001940.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAR-12
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 : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23276
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 40.290
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.3
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.17900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.66100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 1W30
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BIS TRIS PH 5.5-6.5 20-25%
REMARK 280 (W/V) PEG3350, MICROBATCH, TEMPERATURE 293.0K
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 33.34500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 3680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, I
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 HIS A 1
REMARK 465 VAL A 2
REMARK 465 LYS A 3
REMARK 465 LEU A 4
REMARK 465 GLU A 5
REMARK 465 GLN A 6
REMARK 465 LEU A 7
REMARK 465 GLY A 8
REMARK 465 ILE A 9
REMARK 465 PRO A 10
REMARK 465 ARG A 11
REMARK 465 GLN A 12
REMARK 465 VAL A 13
REMARK 465 LEU A 14
REMARK 465 LYS A 15
REMARK 465 TYR A 16
REMARK 465 ASP A 17
REMARK 465 ASP A 18
REMARK 465 PHE A 19
REMARK 465 LEU A 20
REMARK 465 LYS A 21
REMARK 465 SER A 22
REMARK 465 THR A 23
REMARK 465 GLN A 24
REMARK 465 LYS A 25
REMARK 465 SER A 26
REMARK 465 PRO A 27
REMARK 465 ALA A 28
REMARK 465 THR A 29
REMARK 465 ALA A 30
REMARK 465 PRO A 31
REMARK 465 LYS A 32
REMARK 465 PRO A 33
REMARK 465 MET A 34
REMARK 465 PRO A 35
REMARK 465 PRO A 36
REMARK 465 ARG A 37
REMARK 465 PRO A 38
REMARK 465 PRO A 39
REMARK 465 LEU A 40
REMARK 465 PRO A 41
REMARK 465 ASN A 42
REMARK 465 PRO A 57
REMARK 465 GLU A 58
REMARK 465 GLN A 59
REMARK 465 GLU A 60
REMARK 465 PRO A 235
REMARK 465 SER A 236
REMARK 465 PRO A 237
REMARK 465 ASP A 238
REMARK 465 PRO A 239
REMARK 465 SER A 240
REMARK 465 ALA B 2
REMARK 465 ALA B 181
REMARK 465 ARG B 182
REMARK 465 ARG B 183
REMARK 465 GLY B 184
REMARK 465 LYS B 185
REMARK 465 LYS B 186
REMARK 465 LYS B 187
REMARK 465 SER B 188
REMARK 465 GLY B 189
REMARK 465 CYS B 190
REMARK 465 LEU B 191
REMARK 465 VAL B 192
REMARK 465 LEU B 193
REMARK 465 HIS H 1
REMARK 465 VAL H 2
REMARK 465 LYS H 3
REMARK 465 LEU H 4
REMARK 465 GLU H 5
REMARK 465 GLN H 6
REMARK 465 LEU H 7
REMARK 465 GLY H 8
REMARK 465 ILE H 9
REMARK 465 PRO H 10
REMARK 465 ARG H 11
REMARK 465 GLN H 12
REMARK 465 VAL H 13
REMARK 465 LEU H 14
REMARK 465 LYS H 15
REMARK 465 TYR H 16
REMARK 465 ASP H 17
REMARK 465 ASP H 18
REMARK 465 PHE H 19
REMARK 465 LEU H 20
REMARK 465 LYS H 21
REMARK 465 SER H 22
REMARK 465 THR H 23
REMARK 465 GLN H 24
REMARK 465 LYS H 25
REMARK 465 SER H 26
REMARK 465 PRO H 27
REMARK 465 ALA H 28
REMARK 465 THR H 29
REMARK 465 ALA H 30
REMARK 465 PRO H 31
REMARK 465 LYS H 32
REMARK 465 PRO H 33
REMARK 465 MET H 34
REMARK 465 PRO H 35
REMARK 465 PRO H 36
REMARK 465 ARG H 37
REMARK 465 PRO H 38
REMARK 465 PRO H 39
REMARK 465 LEU H 40
REMARK 465 PRO H 41
REMARK 465 ASN H 42
REMARK 465 ASN H 56
REMARK 465 PRO H 57
REMARK 465 GLU H 58
REMARK 465 GLN H 59
REMARK 465 GLU H 60
REMARK 465 PRO H 235
REMARK 465 SER H 236
REMARK 465 PRO H 237
REMARK 465 ASP H 238
REMARK 465 PRO H 239
REMARK 465 SER H 240
REMARK 465 ALA I 2
REMARK 465 ALA I 3
REMARK 465 ARG I 182
REMARK 465 ARG I 183
REMARK 465 GLY I 184
REMARK 465 LYS I 185
REMARK 465 LYS I 186
REMARK 465 LYS I 187
REMARK 465 SER I 188
REMARK 465 GLY I 189
REMARK 465 CYS I 190
REMARK 465 LEU I 191
REMARK 465 VAL I 192
REMARK 465 LEU I 193
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 PHE A 84 -6.25 73.57
REMARK 500 THR A 134 149.75 80.74
REMARK 500 VAL B 38 -65.29 -98.24
REMARK 500 LYS B 98 -59.42 -134.39
REMARK 500 ASN B 109 -1.70 74.80
REMARK 500 HIS H 76 -47.30 -133.81
REMARK 500 PHE H 84 -8.66 74.96
REMARK 500 THR H 134 150.03 84.14
REMARK 500 HIS H 229 42.85 -108.85
REMARK 500 VAL I 38 -70.78 -94.43
REMARK 500 LYS I 98 -64.21 -139.65
REMARK 500 ASN I 109 -2.96 74.61
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 A 353 DISTANCE = 7.20 ANGSTROMS
REMARK 525 HOH I 344 DISTANCE = 8.78 ANGSTROMS
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 B 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 19 OG1
REMARK 620 2 THR B 37 OG1 76.1
REMARK 620 3 GDP B 202 O2B 90.7 166.7
REMARK 620 4 HOH B 301 O 77.7 81.1 98.1
REMARK 620 5 HOH B 306 O 94.3 89.6 89.5 168.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MGF B 203 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GDP B 202 O3B
REMARK 620 2 MGF B 203 F1 98.9
REMARK 620 3 MGF B 203 F2 91.4 119.7
REMARK 620 4 MGF B 203 F3 87.5 119.7 119.9
REMARK 620 5 HOH B 309 O 176.9 84.2 86.6 91.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR I 19 OG1
REMARK 620 2 THR I 37 OG1 76.2
REMARK 620 3 GDP I 202 O1B 87.4 163.5
REMARK 620 4 HOH I 306 O 77.8 77.7 97.1
REMARK 620 5 HOH I 314 O 91.5 86.2 96.3 162.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MGF I 203 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GDP I 202 O3B
REMARK 620 2 MGF I 203 F1 96.3
REMARK 620 3 MGF I 203 F2 85.3 120.6
REMARK 620 4 MGF I 203 F3 90.8 119.3 120.0
REMARK 620 5 HOH I 311 O 172.2 86.0 100.0 81.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MGF B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP I 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MGF I 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5C4M RELATED DB: PDB
REMARK 900 5C4M SHOWS THE STRUCTURE OF ONE OF THE TWO PROTEINS, IN COMPLEX FOR
REMARK 900 THIS ENTRY
DBREF 5M6X A 1 240 UNP Q07960 RHG01_HUMAN 198 437
DBREF 5M6X B 2 193 UNP P61586 RHOA_HUMAN 2 193
DBREF 5M6X H 1 240 UNP Q07960 RHG01_HUMAN 198 437
DBREF 5M6X I 2 193 UNP P61586 RHOA_HUMAN 2 193
SEQADV 5M6X ALA A 85 UNP Q07960 ARG 282 ENGINEERED MUTATION
SEQADV 5M6X ASN B 25 UNP P61586 PHE 25 CONFLICT
SEQADV 5M6X ALA H 85 UNP Q07960 ARG 282 ENGINEERED MUTATION
SEQADV 5M6X ASN I 25 UNP P61586 PHE 25 CONFLICT
SEQRES 1 A 240 HIS VAL LYS LEU GLU GLN LEU GLY ILE PRO ARG GLN VAL
SEQRES 2 A 240 LEU LYS TYR ASP ASP PHE LEU LYS SER THR GLN LYS SER
SEQRES 3 A 240 PRO ALA THR ALA PRO LYS PRO MET PRO PRO ARG PRO PRO
SEQRES 4 A 240 LEU PRO ASN GLN GLN PHE GLY VAL SER LEU GLN HIS LEU
SEQRES 5 A 240 GLN GLU LYS ASN PRO GLU GLN GLU PRO ILE PRO ILE VAL
SEQRES 6 A 240 LEU ARG GLU THR VAL ALA TYR LEU GLN ALA HIS ALA LEU
SEQRES 7 A 240 THR THR GLU GLY ILE PHE ALA ARG SER ALA ASN THR GLN
SEQRES 8 A 240 VAL VAL ARG GLU VAL GLN GLN LYS TYR ASN MET GLY LEU
SEQRES 9 A 240 PRO VAL ASP PHE ASP GLN TYR ASN GLU LEU HIS LEU PRO
SEQRES 10 A 240 ALA VAL ILE LEU LYS THR PHE LEU ARG GLU LEU PRO GLU
SEQRES 11 A 240 PRO LEU LEU THR PHE ASP LEU TYR PRO HIS VAL VAL GLY
SEQRES 12 A 240 PHE LEU ASN ILE ASP GLU SER GLN ARG VAL PRO ALA THR
SEQRES 13 A 240 LEU GLN VAL LEU GLN THR LEU PRO GLU GLU ASN TYR GLN
SEQRES 14 A 240 VAL LEU ARG PHE LEU THR ALA PHE LEU VAL GLN ILE SER
SEQRES 15 A 240 ALA HIS SER ASP GLN ASN LYS MET THR ASN THR ASN LEU
SEQRES 16 A 240 ALA VAL VAL PHE GLY PRO ASN LEU LEU TRP ALA LYS ASP
SEQRES 17 A 240 ALA ALA ILE THR LEU LYS ALA ILE ASN PRO ILE ASN THR
SEQRES 18 A 240 PHE THR LYS PHE LEU LEU ASP HIS GLN GLY GLU LEU PHE
SEQRES 19 A 240 PRO SER PRO ASP PRO SER
SEQRES 1 B 192 ALA ALA ILE ARG LYS LYS LEU VAL ILE VAL GLY ASP GLY
SEQRES 2 B 192 ALA CYS GLY LYS THR CYS LEU LEU ILE VAL ASN SER LYS
SEQRES 3 B 192 ASP GLN PHE PRO GLU VAL TYR VAL PRO THR VAL PHE GLU
SEQRES 4 B 192 ASN TYR VAL ALA ASP ILE GLU VAL ASP GLY LYS GLN VAL
SEQRES 5 B 192 GLU LEU ALA LEU TRP ASP THR ALA GLY GLN GLU ASP TYR
SEQRES 6 B 192 ASP ARG LEU ARG PRO LEU SER TYR PRO ASP THR ASP VAL
SEQRES 7 B 192 ILE LEU MET CYS PHE SER ILE ASP SER PRO ASP SER LEU
SEQRES 8 B 192 GLU ASN ILE PRO GLU LYS TRP THR PRO GLU VAL LYS HIS
SEQRES 9 B 192 PHE CYS PRO ASN VAL PRO ILE ILE LEU VAL GLY ASN LYS
SEQRES 10 B 192 LYS ASP LEU ARG ASN ASP GLU HIS THR ARG ARG GLU LEU
SEQRES 11 B 192 ALA LYS MET LYS GLN GLU PRO VAL LYS PRO GLU GLU GLY
SEQRES 12 B 192 ARG ASP MET ALA ASN ARG ILE GLY ALA PHE GLY TYR MET
SEQRES 13 B 192 GLU CYS SER ALA LYS THR LYS ASP GLY VAL ARG GLU VAL
SEQRES 14 B 192 PHE GLU MET ALA THR ARG ALA ALA LEU GLN ALA ARG ARG
SEQRES 15 B 192 GLY LYS LYS LYS SER GLY CYS LEU VAL LEU
SEQRES 1 H 240 HIS VAL LYS LEU GLU GLN LEU GLY ILE PRO ARG GLN VAL
SEQRES 2 H 240 LEU LYS TYR ASP ASP PHE LEU LYS SER THR GLN LYS SER
SEQRES 3 H 240 PRO ALA THR ALA PRO LYS PRO MET PRO PRO ARG PRO PRO
SEQRES 4 H 240 LEU PRO ASN GLN GLN PHE GLY VAL SER LEU GLN HIS LEU
SEQRES 5 H 240 GLN GLU LYS ASN PRO GLU GLN GLU PRO ILE PRO ILE VAL
SEQRES 6 H 240 LEU ARG GLU THR VAL ALA TYR LEU GLN ALA HIS ALA LEU
SEQRES 7 H 240 THR THR GLU GLY ILE PHE ALA ARG SER ALA ASN THR GLN
SEQRES 8 H 240 VAL VAL ARG GLU VAL GLN GLN LYS TYR ASN MET GLY LEU
SEQRES 9 H 240 PRO VAL ASP PHE ASP GLN TYR ASN GLU LEU HIS LEU PRO
SEQRES 10 H 240 ALA VAL ILE LEU LYS THR PHE LEU ARG GLU LEU PRO GLU
SEQRES 11 H 240 PRO LEU LEU THR PHE ASP LEU TYR PRO HIS VAL VAL GLY
SEQRES 12 H 240 PHE LEU ASN ILE ASP GLU SER GLN ARG VAL PRO ALA THR
SEQRES 13 H 240 LEU GLN VAL LEU GLN THR LEU PRO GLU GLU ASN TYR GLN
SEQRES 14 H 240 VAL LEU ARG PHE LEU THR ALA PHE LEU VAL GLN ILE SER
SEQRES 15 H 240 ALA HIS SER ASP GLN ASN LYS MET THR ASN THR ASN LEU
SEQRES 16 H 240 ALA VAL VAL PHE GLY PRO ASN LEU LEU TRP ALA LYS ASP
SEQRES 17 H 240 ALA ALA ILE THR LEU LYS ALA ILE ASN PRO ILE ASN THR
SEQRES 18 H 240 PHE THR LYS PHE LEU LEU ASP HIS GLN GLY GLU LEU PHE
SEQRES 19 H 240 PRO SER PRO ASP PRO SER
SEQRES 1 I 192 ALA ALA ILE ARG LYS LYS LEU VAL ILE VAL GLY ASP GLY
SEQRES 2 I 192 ALA CYS GLY LYS THR CYS LEU LEU ILE VAL ASN SER LYS
SEQRES 3 I 192 ASP GLN PHE PRO GLU VAL TYR VAL PRO THR VAL PHE GLU
SEQRES 4 I 192 ASN TYR VAL ALA ASP ILE GLU VAL ASP GLY LYS GLN VAL
SEQRES 5 I 192 GLU LEU ALA LEU TRP ASP THR ALA GLY GLN GLU ASP TYR
SEQRES 6 I 192 ASP ARG LEU ARG PRO LEU SER TYR PRO ASP THR ASP VAL
SEQRES 7 I 192 ILE LEU MET CYS PHE SER ILE ASP SER PRO ASP SER LEU
SEQRES 8 I 192 GLU ASN ILE PRO GLU LYS TRP THR PRO GLU VAL LYS HIS
SEQRES 9 I 192 PHE CYS PRO ASN VAL PRO ILE ILE LEU VAL GLY ASN LYS
SEQRES 10 I 192 LYS ASP LEU ARG ASN ASP GLU HIS THR ARG ARG GLU LEU
SEQRES 11 I 192 ALA LYS MET LYS GLN GLU PRO VAL LYS PRO GLU GLU GLY
SEQRES 12 I 192 ARG ASP MET ALA ASN ARG ILE GLY ALA PHE GLY TYR MET
SEQRES 13 I 192 GLU CYS SER ALA LYS THR LYS ASP GLY VAL ARG GLU VAL
SEQRES 14 I 192 PHE GLU MET ALA THR ARG ALA ALA LEU GLN ALA ARG ARG
SEQRES 15 I 192 GLY LYS LYS LYS SER GLY CYS LEU VAL LEU
HET MG B 201 1
HET GDP B 202 28
HET MGF B 203 4
HET MG I 201 1
HET GDP I 202 28
HET MGF I 203 4
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM MGF TRIFLUOROMAGNESATE
FORMUL 5 MG 2(MG 2+)
FORMUL 6 GDP 2(C10 H15 N5 O11 P2)
FORMUL 7 MGF 2(F3 MG 1-)
FORMUL 11 HOH *183(H2 O)
HELIX 1 AA1 SER A 48 ASN A 56 1 9
HELIX 2 AA2 PRO A 63 ALA A 77 1 15
HELIX 3 AA3 ASN A 89 GLY A 103 1 15
HELIX 4 AA4 ASP A 107 TYR A 111 5 5
HELIX 5 AA5 LEU A 114 GLU A 127 1 14
HELIX 6 AA6 THR A 134 ASP A 136 5 3
HELIX 7 AA7 LEU A 137 GLY A 143 1 7
HELIX 8 AA8 PHE A 144 ILE A 147 5 4
HELIX 9 AA9 GLN A 151 THR A 162 1 12
HELIX 10 AB1 PRO A 164 HIS A 184 1 21
HELIX 11 AB2 HIS A 184 LYS A 189 1 6
HELIX 12 AB3 THR A 191 LEU A 204 1 14
HELIX 13 AB4 ASP A 208 ALA A 215 1 8
HELIX 14 AB5 ALA A 215 HIS A 229 1 15
HELIX 15 AB6 HIS A 229 PHE A 234 1 6
HELIX 16 AB7 GLY B 17 ASP B 28 1 12
HELIX 17 AB8 GLN B 63 ASP B 67 5 5
HELIX 18 AB9 LEU B 69 TYR B 74 5 6
HELIX 19 AC1 SER B 88 LYS B 98 1 11
HELIX 20 AC2 LYS B 98 CYS B 107 1 10
HELIX 21 AC3 LYS B 118 ASN B 123 5 6
HELIX 22 AC4 ASP B 124 MET B 134 1 11
HELIX 23 AC5 LYS B 140 GLY B 152 1 13
HELIX 24 AC6 GLY B 166 GLN B 180 1 15
HELIX 25 AC7 SER H 48 LYS H 55 1 8
HELIX 26 AC8 PRO H 63 ALA H 77 1 15
HELIX 27 AC9 ASN H 89 MET H 102 1 14
HELIX 28 AD1 ASP H 107 TYR H 111 5 5
HELIX 29 AD2 LEU H 114 LEU H 128 1 15
HELIX 30 AD3 THR H 134 ASP H 136 5 3
HELIX 31 AD4 LEU H 137 GLY H 143 1 7
HELIX 32 AD5 PHE H 144 ILE H 147 5 4
HELIX 33 AD6 GLN H 151 GLN H 161 1 11
HELIX 34 AD7 PRO H 164 ALA H 183 1 20
HELIX 35 AD8 HIS H 184 LYS H 189 1 6
HELIX 36 AD9 THR H 191 LEU H 204 1 14
HELIX 37 AE1 ASP H 208 ALA H 215 1 8
HELIX 38 AE2 ALA H 215 HIS H 229 1 15
HELIX 39 AE3 HIS H 229 PHE H 234 1 6
HELIX 40 AE4 GLY I 17 ASP I 28 1 12
HELIX 41 AE5 GLN I 63 ASP I 67 5 5
HELIX 42 AE6 LEU I 69 TYR I 74 5 6
HELIX 43 AE7 SER I 88 LYS I 98 1 11
HELIX 44 AE8 LYS I 98 CYS I 107 1 10
HELIX 45 AE9 LYS I 118 ARG I 122 5 5
HELIX 46 AF1 ASP I 124 LYS I 133 1 10
HELIX 47 AF2 LYS I 140 GLY I 152 1 13
HELIX 48 AF3 GLY I 166 LEU I 179 1 14
SHEET 1 AA1 6 PHE B 39 VAL B 48 0
SHEET 2 AA1 6 LYS B 51 THR B 60 -1 O LEU B 57 N TYR B 42
SHEET 3 AA1 6 ILE B 4 GLY B 12 1 N LEU B 8 O TRP B 58
SHEET 4 AA1 6 VAL B 79 SER B 85 1 O LEU B 81 N VAL B 11
SHEET 5 AA1 6 ILE B 112 ASN B 117 1 O VAL B 115 N MET B 82
SHEET 6 AA1 6 GLY B 155 GLU B 158 1 O MET B 157 N GLY B 116
SHEET 1 AA2 6 PHE I 39 GLU I 47 0
SHEET 2 AA2 6 GLN I 52 THR I 60 -1 O LEU I 57 N TYR I 42
SHEET 3 AA2 6 ARG I 5 GLY I 12 1 N LEU I 8 O ALA I 56
SHEET 4 AA2 6 VAL I 79 SER I 85 1 O CYS I 83 N VAL I 11
SHEET 5 AA2 6 ILE I 112 ASN I 117 1 O ASN I 117 N PHE I 84
SHEET 6 AA2 6 GLY I 155 GLU I 158 1 O GLY I 155 N LEU I 114
LINK OG1 THR B 19 MG MG B 201 1555 1555 2.08
LINK OG1 THR B 37 MG MG B 201 1555 1555 2.28
LINK MG MG B 201 O2B GDP B 202 1555 1555 2.06
LINK MG MG B 201 O HOH B 301 1555 1555 2.02
LINK MG MG B 201 O HOH B 306 1555 1555 2.06
LINK O3B GDP B 202 MG MGF B 203 1555 1555 2.17
LINK MG MGF B 203 O HOH B 309 1555 1555 1.94
LINK OG1 THR I 19 MG MG I 201 1555 1555 2.28
LINK OG1 THR I 37 MG MG I 201 1555 1555 2.28
LINK MG MG I 201 O1B GDP I 202 1555 1555 2.01
LINK MG MG I 201 O HOH I 306 1555 1555 2.07
LINK MG MG I 201 O HOH I 314 1555 1555 1.91
LINK O3B GDP I 202 MG MGF I 203 1555 1555 2.12
LINK MG MGF I 203 O HOH I 311 1555 1555 1.98
SITE 1 AC1 6 THR B 19 THR B 37 GDP B 202 MGF B 203
SITE 2 AC1 6 HOH B 301 HOH B 306
SITE 1 AC2 22 LYS A 189 HOH A 311 ALA B 15 CYS B 16
SITE 2 AC2 22 GLY B 17 LYS B 18 THR B 19 CYS B 20
SITE 3 AC2 22 PHE B 30 TYR B 34 LYS B 118 ASP B 120
SITE 4 AC2 22 LEU B 121 SER B 160 ALA B 161 LYS B 162
SITE 5 AC2 22 MG B 201 MGF B 203 HOH B 301 HOH B 306
SITE 6 AC2 22 HOH B 315 HOH B 316
SITE 1 AC3 12 GLY B 14 LYS B 18 TYR B 34 PRO B 36
SITE 2 AC3 12 THR B 37 GLY B 62 GLN B 63 MG B 201
SITE 3 AC3 12 GDP B 202 HOH B 301 HOH B 306 HOH B 309
SITE 1 AC4 6 THR I 19 THR I 37 GDP I 202 MGF I 203
SITE 2 AC4 6 HOH I 306 HOH I 314
SITE 1 AC5 22 LYS H 189 ALA I 15 CYS I 16 GLY I 17
SITE 2 AC5 22 LYS I 18 THR I 19 CYS I 20 PHE I 30
SITE 3 AC5 22 TYR I 34 LYS I 118 ASP I 120 LEU I 121
SITE 4 AC5 22 SER I 160 ALA I 161 LYS I 162 MG I 201
SITE 5 AC5 22 MGF I 203 HOH I 303 HOH I 306 HOH I 314
SITE 6 AC5 22 HOH I 316 HOH I 328
SITE 1 AC6 13 GLY I 14 ALA I 15 LYS I 18 TYR I 34
SITE 2 AC6 13 PRO I 36 THR I 37 GLY I 62 GLN I 63
SITE 3 AC6 13 MG I 201 GDP I 202 HOH I 306 HOH I 311
SITE 4 AC6 13 HOH I 314
CRYST1 73.470 66.690 76.890 90.00 95.41 90.00 P 1 21 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 0.013611 0.000000 0.001289 0.00000
SCALE2 0.000000 0.014995 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013064 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
