HEADER SIGNALING PROTEIN/TRANSCRIPTION/INHIBITO21-APR-16 5JHH
TITLE CRYSTAL STRUCTURE OF THE TERNARY COMPLEX BETWEEN THE HUMAN RHOA, ITS
TITLE 2 INHIBITOR AND THE DH/PH DOMAIN OF HUMAN ARHGEF11
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 11;
COMPND 3 CHAIN: A, E;
COMPND 4 FRAGMENT: UNP RESIDUES 714-1081;
COMPND 5 SYNONYM: PDZ-RHOGEF;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: TRANSFORMING PROTEIN RHOA;
COMPND 9 CHAIN: B, F;
COMPND 10 FRAGMENT: UNP RESIDUES 1-181;
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: ARHGEF11, KIAA0380;
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 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: RHOA, ARH12, ARHA, RHO12;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS RHOA-INHIBITOR-ARHGEF11 TERNARY COMPLEX, TARGET-BASED PHARMACEUTICAL
KEYWDS 2 DESIGN, SIGNALING PROTEIN-TRANSCRIPTION-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.LV,R.WANG,L.MA,Q.MIAO,J.WU,Z.YAN,J.LI,L.MIAO,F.WANG
REVDAT 2 20-MAR-24 5JHH 1 REMARK
REVDAT 1 26-APR-17 5JHH 0
JRNL AUTH R.WANG,Z.YAN,Z.LV,L.MA,Q.MIAO,Q.CHEN,F.WANG,J.LI,L.MIAO
JRNL TITL CRYSTALLIZATION AND PRELIMINARY X-RAY CRYSTALLOGRAPHIC
JRNL TITL 2 ANALYSIS OF A SMALL GTPASE RHOA BOUND WITH ITS INHIBITOR AND
JRNL TITL 3 PDZRHOGEF
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 82.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 69765
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3565
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4872
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.41
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE SET COUNT : 255
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8673
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 478
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : -0.04000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.245
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.207
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.156
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.560
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9064 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8940 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12238 ; 1.619 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): 20600 ; 0.814 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1097 ; 6.850 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 437 ;37.496 ;23.959
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1755 ;19.478 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 85 ;22.638 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1366 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10121 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2022 ; 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): 4358 ; 3.446 ; 3.822
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4357 ; 3.440 ; 3.821
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5465 ; 5.130 ; 5.711
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5466 ; 5.131 ; 5.712
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4706 ; 4.493 ; 4.376
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4707 ; 4.493 ; 4.377
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6774 ; 7.028 ; 6.344
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 10838 ; 9.720 ;30.646
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 10839 ; 9.720 ;30.654
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 : 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 5JHH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220427.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
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 FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.541782
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73383
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 82.440
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.2680
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.51300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2% V/V TACSIMATE PH 5.0, 0.1M SODIUM
REMARK 280 CITRATE TRIBASIC DIHYDRATE PH 5.6, 16% PEG 3350, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
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 59.52450
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: 3600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 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: 3190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 MET A 713
REMARK 465 SER A 1009
REMARK 465 LYS A 1010
REMARK 465 THR A 1011
REMARK 465 ALA A 1012
REMARK 465 VAL A 1013
REMARK 465 GLY A 1014
REMARK 465 SER A 1015
REMARK 465 SER A 1016
REMARK 465 ASP A 1017
REMARK 465 SER A 1018
REMARK 465 LYS A 1019
REMARK 465 GLN A 1020
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ALA B 181
REMARK 465 MET E 713
REMARK 465 THR E 1011
REMARK 465 ALA E 1012
REMARK 465 VAL E 1013
REMARK 465 GLY E 1014
REMARK 465 SER E 1015
REMARK 465 SER E 1016
REMARK 465 ASP E 1017
REMARK 465 SER E 1018
REMARK 465 LYS E 1019
REMARK 465 GLN E 1020
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 ALA F 181
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 CAT RA0 F 201 O HOH F 329 1.08
REMARK 500 O ARG A 868 NH2 ARG B 5 1.56
REMARK 500 O ARG E 868 NH1 ARG F 5 1.73
REMARK 500 CAB RA0 F 201 O HOH F 321 1.75
REMARK 500 OAW RA0 F 201 O HOH F 301 1.77
REMARK 500 NH1 ARG A 772 O HOH A 1201 1.83
REMARK 500 NE2 HIS E 863 OE1 GLN E 865 1.85
REMARK 500 CAR RA0 F 201 O HOH F 329 1.95
REMARK 500 O ASN A 715 CG2 THR A 719 1.95
REMARK 500 NH2 ARG A 772 O HOH A 1202 1.98
REMARK 500 O ASN E 715 CG2 THR E 719 2.00
REMARK 500 CB ASP A 979 O HOH A 1301 2.06
REMARK 500 O HOH A 1310 O HOH A 1322 2.07
REMARK 500 NZ LYS A 998 O HOH A 1203 2.08
REMARK 500 O TRP A 716 O HIS A 718 2.08
REMARK 500 O HOH B 362 O HOH B 370 2.09
REMARK 500 O HIS A 1008 O HOH A 1204 2.09
REMARK 500 CAA RA0 F 201 O HOH F 321 2.11
REMARK 500 NZ LYS A 884 O HOH A 1205 2.14
REMARK 500 NH1 ARG A 964 OD2 ASP A 991 2.15
REMARK 500 N THR B 19 OAW RA0 B 201 2.17
REMARK 500 O HOH A 1339 O HOH A 1359 2.18
REMARK 500 O HOH A 1213 O HOH A 1271 2.19
REMARK 500 NH2 ARG B 129 O HOH B 301 2.19
REMARK 500 O HOH A 1249 O HOH B 375 2.19
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 ARG A 816 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 816 NE - CZ - NH2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG B 70 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 122 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 122 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG B 176 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG F 122 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG F 122 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG F 176 NE - CZ - NH2 ANGL. DEV. = -4.7 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 ASN A 715 128.00 151.77
REMARK 500 THR A 719 -138.98 51.71
REMARK 500 ASN A 781 46.68 -156.93
REMARK 500 GLU A 802 39.54 -82.92
REMARK 500 LYS A 807 -122.05 -92.52
REMARK 500 ALA A 942 46.05 -105.75
REMARK 500 ALA A 944 -4.50 -56.62
REMARK 500 ARG A 947 -158.99 -87.77
REMARK 500 SER A 949 -90.83 -110.64
REMARK 500 ASP A1000 -115.21 56.98
REMARK 500 GLU B 32 -72.60 -72.13
REMARK 500 LYS B 135 36.81 74.36
REMARK 500 ASN E 715 121.55 164.91
REMARK 500 THR E 719 -88.36 -107.19
REMARK 500 LYS E 722 -123.32 -175.41
REMARK 500 ASP E 723 22.62 -75.45
REMARK 500 ASN E 781 43.34 -153.79
REMARK 500 LYS E 807 -123.15 -95.94
REMARK 500 ALA E 944 12.45 -66.81
REMARK 500 ASP E 979 -9.18 78.51
REMARK 500 ASP E1000 -113.55 61.16
REMARK 500 LEU E1051 -84.37 -98.24
REMARK 500 ASP F 49 46.76 38.05
REMARK 500 ASP F 120 3.00 -61.26
REMARK 500 LYS F 133 -27.97 -39.67
REMARK 500 LYS F 164 -4.85 78.03
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 GOL A 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue RA0 B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue RA0 F 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JHG RELATED DB: PDB
DBREF 5JHH A 714 1081 UNP O15085 ARHGB_HUMAN 714 1081
DBREF 5JHH B 1 181 UNP P61586 RHOA_HUMAN 1 181
DBREF 5JHH E 714 1081 UNP O15085 ARHGB_HUMAN 714 1081
DBREF 5JHH F 1 181 UNP P61586 RHOA_HUMAN 1 181
SEQADV 5JHH MET A 713 UNP O15085 EXPRESSION TAG
SEQADV 5JHH MET E 713 UNP O15085 EXPRESSION TAG
SEQRES 1 A 369 MET GLN ASN TRP GLN HIS THR VAL GLY LYS ASP VAL VAL
SEQRES 2 A 369 ALA GLY LEU THR GLN ARG GLU ILE ASP ARG GLN GLU VAL
SEQRES 3 A 369 ILE ASN GLU LEU PHE VAL THR GLU ALA SER HIS LEU ARG
SEQRES 4 A 369 THR LEU ARG VAL LEU ASP LEU ILE PHE TYR GLN ARG MET
SEQRES 5 A 369 LYS LYS GLU ASN LEU MET PRO ARG GLU GLU LEU ALA ARG
SEQRES 6 A 369 LEU PHE PRO ASN LEU PRO GLU LEU ILE GLU ILE HIS ASN
SEQRES 7 A 369 SER TRP CYS GLU ALA MET LYS LYS LEU ARG GLU GLU GLY
SEQRES 8 A 369 PRO ILE ILE LYS GLU ILE SER ASP LEU MET LEU ALA ARG
SEQRES 9 A 369 PHE ASP GLY PRO ALA ARG GLU GLU LEU GLN GLN VAL ALA
SEQRES 10 A 369 ALA GLN PHE CYS SER TYR GLN SER ILE ALA LEU GLU LEU
SEQRES 11 A 369 ILE LYS THR LYS GLN ARG LYS GLU SER ARG PHE GLN LEU
SEQRES 12 A 369 PHE MET GLN GLU ALA GLU SER HIS PRO GLN CYS ARG ARG
SEQRES 13 A 369 LEU GLN LEU ARG ASP LEU ILE ILE SER GLU MET GLN ARG
SEQRES 14 A 369 LEU THR LYS TYR PRO LEU LEU LEU GLU SER ILE ILE LYS
SEQRES 15 A 369 HIS THR GLU GLY GLY THR SER GLU HIS GLU LYS LEU CYS
SEQRES 16 A 369 ARG ALA ARG ASP GLN CYS ARG GLU ILE LEU LYS TYR VAL
SEQRES 17 A 369 ASN GLU ALA VAL LYS GLN THR GLU ASN ARG HIS ARG LEU
SEQRES 18 A 369 GLU GLY TYR GLN LYS ARG LEU ASP ALA THR ALA LEU GLU
SEQRES 19 A 369 ARG ALA SER ASN PRO LEU ALA ALA GLU PHE LYS SER LEU
SEQRES 20 A 369 ASP LEU THR THR ARG LYS MET ILE HIS GLU GLY PRO LEU
SEQRES 21 A 369 THR TRP ARG ILE SER LYS ASP LYS THR LEU ASP LEU HIS
SEQRES 22 A 369 VAL LEU LEU LEU GLU ASP LEU LEU VAL LEU LEU GLN LYS
SEQRES 23 A 369 GLN ASP GLU LYS LEU LEU LEU LYS CYS HIS SER LYS THR
SEQRES 24 A 369 ALA VAL GLY SER SER ASP SER LYS GLN THR PHE SER PRO
SEQRES 25 A 369 VAL LEU LYS LEU ASN ALA VAL LEU ILE ARG SER VAL ALA
SEQRES 26 A 369 THR ASP LYS ARG ALA PHE PHE ILE ILE CYS THR SER LYS
SEQRES 27 A 369 LEU GLY PRO PRO GLN ILE TYR GLU LEU VAL ALA LEU THR
SEQRES 28 A 369 SER SER ASP LYS ASN THR TRP MET GLU LEU LEU GLU GLU
SEQRES 29 A 369 ALA VAL ARG ASN ALA
SEQRES 1 B 181 MET ALA ALA ILE ARG LYS LYS LEU VAL ILE VAL GLY ASP
SEQRES 2 B 181 GLY ALA CYS GLY LYS THR CYS LEU LEU ILE VAL PHE SER
SEQRES 3 B 181 LYS ASP GLN PHE PRO GLU VAL TYR VAL PRO THR VAL PHE
SEQRES 4 B 181 GLU ASN TYR VAL ALA ASP ILE GLU VAL ASP GLY LYS GLN
SEQRES 5 B 181 VAL GLU LEU ALA LEU TRP ASP THR ALA GLY GLN GLU ASP
SEQRES 6 B 181 TYR ASP ARG LEU ARG PRO LEU SER TYR PRO ASP THR ASP
SEQRES 7 B 181 VAL ILE LEU MET CYS PHE SER ILE ASP SER PRO ASP SER
SEQRES 8 B 181 LEU GLU ASN ILE PRO GLU LYS TRP THR PRO GLU VAL LYS
SEQRES 9 B 181 HIS PHE CYS PRO ASN VAL PRO ILE ILE LEU VAL GLY ASN
SEQRES 10 B 181 LYS LYS ASP LEU ARG ASN ASP GLU HIS THR ARG ARG GLU
SEQRES 11 B 181 LEU ALA LYS MET LYS GLN GLU PRO VAL LYS PRO GLU GLU
SEQRES 12 B 181 GLY ARG ASP MET ALA ASN ARG ILE GLY ALA PHE GLY TYR
SEQRES 13 B 181 MET GLU CYS SER ALA LYS THR LYS ASP GLY VAL ARG GLU
SEQRES 14 B 181 VAL PHE GLU MET ALA THR ARG ALA ALA LEU GLN ALA
SEQRES 1 E 369 MET GLN ASN TRP GLN HIS THR VAL GLY LYS ASP VAL VAL
SEQRES 2 E 369 ALA GLY LEU THR GLN ARG GLU ILE ASP ARG GLN GLU VAL
SEQRES 3 E 369 ILE ASN GLU LEU PHE VAL THR GLU ALA SER HIS LEU ARG
SEQRES 4 E 369 THR LEU ARG VAL LEU ASP LEU ILE PHE TYR GLN ARG MET
SEQRES 5 E 369 LYS LYS GLU ASN LEU MET PRO ARG GLU GLU LEU ALA ARG
SEQRES 6 E 369 LEU PHE PRO ASN LEU PRO GLU LEU ILE GLU ILE HIS ASN
SEQRES 7 E 369 SER TRP CYS GLU ALA MET LYS LYS LEU ARG GLU GLU GLY
SEQRES 8 E 369 PRO ILE ILE LYS GLU ILE SER ASP LEU MET LEU ALA ARG
SEQRES 9 E 369 PHE ASP GLY PRO ALA ARG GLU GLU LEU GLN GLN VAL ALA
SEQRES 10 E 369 ALA GLN PHE CYS SER TYR GLN SER ILE ALA LEU GLU LEU
SEQRES 11 E 369 ILE LYS THR LYS GLN ARG LYS GLU SER ARG PHE GLN LEU
SEQRES 12 E 369 PHE MET GLN GLU ALA GLU SER HIS PRO GLN CYS ARG ARG
SEQRES 13 E 369 LEU GLN LEU ARG ASP LEU ILE ILE SER GLU MET GLN ARG
SEQRES 14 E 369 LEU THR LYS TYR PRO LEU LEU LEU GLU SER ILE ILE LYS
SEQRES 15 E 369 HIS THR GLU GLY GLY THR SER GLU HIS GLU LYS LEU CYS
SEQRES 16 E 369 ARG ALA ARG ASP GLN CYS ARG GLU ILE LEU LYS TYR VAL
SEQRES 17 E 369 ASN GLU ALA VAL LYS GLN THR GLU ASN ARG HIS ARG LEU
SEQRES 18 E 369 GLU GLY TYR GLN LYS ARG LEU ASP ALA THR ALA LEU GLU
SEQRES 19 E 369 ARG ALA SER ASN PRO LEU ALA ALA GLU PHE LYS SER LEU
SEQRES 20 E 369 ASP LEU THR THR ARG LYS MET ILE HIS GLU GLY PRO LEU
SEQRES 21 E 369 THR TRP ARG ILE SER LYS ASP LYS THR LEU ASP LEU HIS
SEQRES 22 E 369 VAL LEU LEU LEU GLU ASP LEU LEU VAL LEU LEU GLN LYS
SEQRES 23 E 369 GLN ASP GLU LYS LEU LEU LEU LYS CYS HIS SER LYS THR
SEQRES 24 E 369 ALA VAL GLY SER SER ASP SER LYS GLN THR PHE SER PRO
SEQRES 25 E 369 VAL LEU LYS LEU ASN ALA VAL LEU ILE ARG SER VAL ALA
SEQRES 26 E 369 THR ASP LYS ARG ALA PHE PHE ILE ILE CYS THR SER LYS
SEQRES 27 E 369 LEU GLY PRO PRO GLN ILE TYR GLU LEU VAL ALA LEU THR
SEQRES 28 E 369 SER SER ASP LYS ASN THR TRP MET GLU LEU LEU GLU GLU
SEQRES 29 E 369 ALA VAL ARG ASN ALA
SEQRES 1 F 181 MET ALA ALA ILE ARG LYS LYS LEU VAL ILE VAL GLY ASP
SEQRES 2 F 181 GLY ALA CYS GLY LYS THR CYS LEU LEU ILE VAL PHE SER
SEQRES 3 F 181 LYS ASP GLN PHE PRO GLU VAL TYR VAL PRO THR VAL PHE
SEQRES 4 F 181 GLU ASN TYR VAL ALA ASP ILE GLU VAL ASP GLY LYS GLN
SEQRES 5 F 181 VAL GLU LEU ALA LEU TRP ASP THR ALA GLY GLN GLU ASP
SEQRES 6 F 181 TYR ASP ARG LEU ARG PRO LEU SER TYR PRO ASP THR ASP
SEQRES 7 F 181 VAL ILE LEU MET CYS PHE SER ILE ASP SER PRO ASP SER
SEQRES 8 F 181 LEU GLU ASN ILE PRO GLU LYS TRP THR PRO GLU VAL LYS
SEQRES 9 F 181 HIS PHE CYS PRO ASN VAL PRO ILE ILE LEU VAL GLY ASN
SEQRES 10 F 181 LYS LYS ASP LEU ARG ASN ASP GLU HIS THR ARG ARG GLU
SEQRES 11 F 181 LEU ALA LYS MET LYS GLN GLU PRO VAL LYS PRO GLU GLU
SEQRES 12 F 181 GLY ARG ASP MET ALA ASN ARG ILE GLY ALA PHE GLY TYR
SEQRES 13 F 181 MET GLU CYS SER ALA LYS THR LYS ASP GLY VAL ARG GLU
SEQRES 14 F 181 VAL PHE GLU MET ALA THR ARG ALA ALA LEU GLN ALA
HET GOL A1101 6
HET GOL A1102 6
HET RA0 B 201 24
HET GOL E1101 6
HET RA0 F 201 24
HETNAM GOL GLYCEROL
HETNAM RA0 3-{3-[ETHYL(QUINOLIN-2-YL)AMINO]PHENYL}PROPANOIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 3(C3 H8 O3)
FORMUL 7 RA0 2(C20 H20 N2 O2)
FORMUL 10 HOH *478(H2 O)
HELIX 1 AA1 THR A 729 PHE A 760 1 32
HELIX 2 AA2 PHE A 760 GLU A 767 1 8
HELIX 3 AA3 PRO A 771 PHE A 779 1 9
HELIX 4 AA4 ASN A 781 GLU A 802 1 22
HELIX 5 AA5 ILE A 809 ASP A 818 1 10
HELIX 6 AA6 ASP A 818 SER A 834 1 17
HELIX 7 AA7 TYR A 835 GLU A 850 1 16
HELIX 8 AA8 GLU A 850 HIS A 863 1 14
HELIX 9 AA9 PRO A 864 ARG A 867 5 4
HELIX 10 AB1 GLN A 870 ILE A 875 1 6
HELIX 11 AB2 ILE A 876 HIS A 895 1 20
HELIX 12 AB3 THR A 900 ARG A 939 1 40
HELIX 13 AB4 ASN A 950 LYS A 957 5 8
HELIX 14 AB5 ASP A 960 ARG A 964 5 5
HELIX 15 AB6 THR A 1063 ALA A 1081 1 19
HELIX 16 AB7 GLY B 17 ASP B 28 1 12
HELIX 17 AB8 LEU B 69 TYR B 74 5 6
HELIX 18 AB9 SER B 88 LYS B 98 1 11
HELIX 19 AC1 LYS B 98 CYS B 107 1 10
HELIX 20 AC2 LYS B 118 ARG B 122 5 5
HELIX 21 AC3 ASP B 124 MET B 134 1 11
HELIX 22 AC4 LYS B 140 GLY B 152 1 13
HELIX 23 AC5 GLY B 166 GLN B 180 1 15
HELIX 24 AC6 THR E 729 PHE E 760 1 32
HELIX 25 AC7 PHE E 760 GLU E 767 1 8
HELIX 26 AC8 PRO E 771 PHE E 779 1 9
HELIX 27 AC9 ASN E 781 GLU E 802 1 22
HELIX 28 AD1 ILE E 809 ASP E 818 1 10
HELIX 29 AD2 ASP E 818 TYR E 835 1 18
HELIX 30 AD3 TYR E 835 GLU E 850 1 16
HELIX 31 AD4 GLU E 850 HIS E 863 1 14
HELIX 32 AD5 PRO E 864 ARG E 867 5 4
HELIX 33 AD6 GLN E 870 ILE E 875 1 6
HELIX 34 AD7 ILE E 876 HIS E 895 1 20
HELIX 35 AD8 THR E 900 ARG E 939 1 40
HELIX 36 AD9 ALA E 942 GLU E 946 5 5
HELIX 37 AE1 ASN E 950 GLU E 955 1 6
HELIX 38 AE2 ASP E 960 ARG E 964 5 5
HELIX 39 AE3 THR E 1063 ASN E 1080 1 18
HELIX 40 AE4 GLY F 17 ASP F 28 1 12
HELIX 41 AE5 LEU F 69 TYR F 74 5 6
HELIX 42 AE6 SER F 88 LYS F 98 1 11
HELIX 43 AE7 LYS F 98 CYS F 107 1 10
HELIX 44 AE8 LYS F 118 ARG F 122 5 5
HELIX 45 AE9 ASP F 124 LYS F 133 1 10
HELIX 46 AF1 LYS F 140 ILE F 151 1 12
HELIX 47 AF2 GLY F 166 GLN F 180 1 15
SHEET 1 AA1 4 LEU A 940 ASP A 941 0
SHEET 2 AA1 4 LYS A1002 LEU A1004 1 O LEU A1003 N ASP A 941
SHEET 3 AA1 4 LEU A 992 GLN A 999 -1 N GLN A 997 O LEU A1004
SHEET 4 AA1 4 VAL A1025 LYS A1027 -1 O LEU A1026 N LEU A 993
SHEET 1 AA2 8 LEU A 940 ASP A 941 0
SHEET 2 AA2 8 LYS A1002 LEU A1004 1 O LEU A1003 N ASP A 941
SHEET 3 AA2 8 LEU A 992 GLN A 999 -1 N GLN A 997 O LEU A1004
SHEET 4 AA2 8 THR A 981 LEU A 989 -1 N HIS A 985 O LEU A 996
SHEET 5 AA2 8 MET A 966 ARG A 975 -1 N TRP A 974 O LEU A 982
SHEET 6 AA2 8 TYR A1057 VAL A1060 -1 O VAL A1060 N THR A 973
SHEET 7 AA2 8 ALA A1042 CYS A1047 -1 N PHE A1043 O LEU A1059
SHEET 8 AA2 8 VAL A1031 SER A1035 -1 N ARG A1034 O PHE A1044
SHEET 1 AA3 6 TYR B 42 VAL B 48 0
SHEET 2 AA3 6 LYS B 51 TRP B 58 -1 O LEU B 55 N ALA B 44
SHEET 3 AA3 6 ARG B 5 GLY B 12 1 N LYS B 6 O ALA B 56
SHEET 4 AA3 6 VAL B 79 SER B 85 1 O CYS B 83 N VAL B 11
SHEET 5 AA3 6 ILE B 112 ASN B 117 1 O VAL B 115 N MET B 82
SHEET 6 AA3 6 GLY B 155 GLU B 158 1 O MET B 157 N GLY B 116
SHEET 1 AA4 4 LEU E 940 ASP E 941 0
SHEET 2 AA4 4 LYS E1002 LEU E1004 1 O LEU E1003 N ASP E 941
SHEET 3 AA4 4 LEU E 992 GLN E 999 -1 N GLN E 997 O LEU E1004
SHEET 4 AA4 4 VAL E1025 LYS E1027 -1 O LEU E1026 N LEU E 993
SHEET 1 AA5 8 LEU E 940 ASP E 941 0
SHEET 2 AA5 8 LYS E1002 LEU E1004 1 O LEU E1003 N ASP E 941
SHEET 3 AA5 8 LEU E 992 GLN E 999 -1 N GLN E 997 O LEU E1004
SHEET 4 AA5 8 LYS E 980 LEU E 989 -1 N LEU E 987 O VAL E 994
SHEET 5 AA5 8 MET E 966 SER E 977 -1 N ILE E 967 O LEU E 988
SHEET 6 AA5 8 GLN E1055 VAL E1060 -1 O GLU E1058 N ARG E 975
SHEET 7 AA5 8 ALA E1042 CYS E1047 -1 N CYS E1047 O GLN E1055
SHEET 8 AA5 8 VAL E1031 SER E1035 -1 N ARG E1034 O PHE E1044
SHEET 1 AA6 6 TYR F 42 VAL F 48 0
SHEET 2 AA6 6 LYS F 51 TRP F 58 -1 O LEU F 55 N ALA F 44
SHEET 3 AA6 6 ILE F 4 GLY F 12 1 N ILE F 4 O GLU F 54
SHEET 4 AA6 6 VAL F 79 SER F 85 1 O CYS F 83 N VAL F 11
SHEET 5 AA6 6 ILE F 112 ASN F 117 1 O ILE F 113 N ILE F 80
SHEET 6 AA6 6 GLY F 155 GLU F 158 1 O MET F 157 N GLY F 116
SITE 1 AC1 7 ILE A 788 SER A 791 TRP A 792 ALA A 795
SITE 2 AC1 7 ALA A 815 ARG A 816 HOH A1312
SITE 1 AC2 5 HIS A 968 HOH A1230 HOH A1313 GLU B 102
SITE 2 AC2 5 HIS B 105
SITE 1 AC3 12 GLY B 14 ALA B 15 GLY B 17 LYS B 18
SITE 2 AC3 12 THR B 19 CYS B 20 LYS B 118 ASP B 120
SITE 3 AC3 12 ALA B 161 LYS B 162 HOH B 303 HOH B 377
SITE 1 AC4 6 SER E 791 TRP E 792 ALA E 795 ALA E 815
SITE 2 AC4 6 ARG E 816 HOH E1251
SITE 1 AC5 17 GLY F 14 ALA F 15 GLY F 17 LYS F 18
SITE 2 AC5 17 THR F 19 CYS F 20 VAL F 35 ALA F 61
SITE 3 AC5 17 LYS F 118 ASP F 120 SER F 160 ALA F 161
SITE 4 AC5 17 LYS F 162 HOH F 301 HOH F 321 HOH F 329
SITE 5 AC5 17 HOH F 357
CRYST1 88.855 119.049 90.526 90.00 114.39 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 0.011254 0.000000 0.005104 0.00000
SCALE2 0.000000 0.008400 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012129 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
