HEADER SIGNALING PROTEIN/INHIBITOR 20-DEC-00 1HH4
TITLE RAC1-RHOGDI COMPLEX INVOLVED IN NADPH OXIDASE ACTIVATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: P21-RAC1, RAS-LIKE PROTEIN TC25;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: RHO GDP-DISSOCIATION INHIBITOR 1;
COMPND 8 CHAIN: D, E;
COMPND 9 SYNONYM: RHO GDI 1, RHO-GDI ALPHA;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS SIGNALING PROTEIN/INHIBITOR, SINGAL PROTEIN INHIBITOR COMPLEX, SMALL
KEYWDS 2 G PROTEIN, GTPASE ACTIVATION, GTP-BINDING, PRENYLATION, LIPOPROTEIN,
KEYWDS 3 SIGNALING PROTEIN-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.GRIZOT,J.FAURE,F.FIESCHI,P.V.VIGNAIS,M.-C.DAGHER,E.PEBAY-PEYROULA
REVDAT 5 13-DEC-23 1HH4 1 LINK
REVDAT 4 15-MAY-19 1HH4 1 REMARK
REVDAT 3 08-MAY-19 1HH4 1 REMARK
REVDAT 2 24-FEB-09 1HH4 1 VERSN
REVDAT 1 28-AUG-01 1HH4 0
JRNL AUTH S.GRIZOT,J.FAURE,F.FIESCHI,P.V.VIGNAIS,M.-C.DAGHER,
JRNL AUTH 2 E.PEBAY-PEYROULA
JRNL TITL CRYSTAL STRUCTURE OF THE RAC1-RHOGDI COMPLEX INVOLVED IN
JRNL TITL 2 NADPH OXIDASE ACTIVATION
JRNL REF BIOCHEMISTRY V. 40 10007 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11513578
JRNL DOI 10.1021/BI010288K
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.5
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 85.1
REMARK 3 NUMBER OF REFLECTIONS : 20669
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 SET) : 0.256
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1062
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3068
REMARK 3 BIN R VALUE (WORKING SET) : 0.3780
REMARK 3 BIN FREE R VALUE : 0.4490
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 165
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.035
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5780
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 98
REMARK 3 SOLVENT ATOMS : 30
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 58.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.18000
REMARK 3 B22 (A**2) : -4.29000
REMARK 3 B33 (A**2) : 0.11000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.40
REMARK 3 ESD FROM SIGMAA (A) : 0.50
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.47
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.60
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.940
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 11.170; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 17.320; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 14.590; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 20.810; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.29
REMARK 3 BSOL : 36.50
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER-REP.PARAM
REMARK 3 PARAMETER FILE 4 : LIG.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 4 : LIG.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: TWO GROUPS WERE DEFINED FOR NCS
REMARK 3 RESTRAINTS, GROUP 1 BETWEEN CHAIN ID A AND B (ALL RESIDUES
REMARK 3 EXCEPT 28 - 40 AND 178 - 189), GROUP2 BETWEEN CHAIN ID D AND E
REMARK 3 (RESIDUES 330 - 353 AND 390 - 500)
REMARK 4
REMARK 4 1HH4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-DEC-00.
REMARK 100 THE DEPOSITION ID IS D_1290005664.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21165
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.7
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.43400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: 1DOA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP AT 20C WITH RESERVOIR:
REMARK 280 30% PEG 4000, 100 MM NA CITRATE PH=5.6, 5 MM MGCL2, 200 MM
REMARK 280 AMMONIUM ACETATE, PH 5.60, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 77.35000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.35000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 77.35000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.35000
REMARK 290 SMTRY3 4 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 300 REMARK: THE ASYMMETRIC UNIT CONTAINS TWO HETERODIMERS
REMARK 300 RAC-RHOGDI,RELATED BY NCS. THE CHAIN IDENTIFIERS
REMARK 300 ARE A AND D FOR DIMER1,AND B AND E FOR
REMARK 300 DIMER 2.
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E
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 400
REMARK 400 COMPOUND
REMARK 400 RACS ARE GTP-BINDING PROTEINS ASSOCIATED WITH PLASMA MEMBRANE
REMARK 400 WHICH COULD REGULATE SECRETORY PROCESSES.
REMARK 400 RHO GDI 1 REGULATES THE GDP/GTP EXCHANGE REACTION OF THE RHO
REMARK 400 PROTEINS BY INHIBITING THE DISSOCIATION OF GDP FROM THEM.
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 LEU A 190
REMARK 465 LEU A 191
REMARK 465 LEU A 192
REMARK 465 LEU B 190
REMARK 465 LEU B 191
REMARK 465 LEU B 192
REMARK 465 MET D 301
REMARK 465 ALA D 302
REMARK 465 GLU D 303
REMARK 465 GLN D 304
REMARK 465 GLU D 305
REMARK 465 PRO D 306
REMARK 465 THR D 307
REMARK 465 ALA D 308
REMARK 465 VAL D 359
REMARK 465 ALA D 360
REMARK 465 VAL D 361
REMARK 465 SER D 362
REMARK 465 ALA D 363
REMARK 465 ASP D 364
REMARK 465 PRO D 365
REMARK 465 TRP D 502
REMARK 465 LYS D 503
REMARK 465 ASP D 504
REMARK 465 MET E 301
REMARK 465 ALA E 302
REMARK 465 GLU E 303
REMARK 465 GLN E 304
REMARK 465 GLU E 305
REMARK 465 PRO E 306
REMARK 465 THR E 307
REMARK 465 ALA E 308
REMARK 465 GLU E 309
REMARK 465 GLN E 310
REMARK 465 LEU E 311
REMARK 465 ALA E 312
REMARK 465 GLN E 313
REMARK 465 ILE E 314
REMARK 465 ALA E 315
REMARK 465 ALA E 316
REMARK 465 GLU E 317
REMARK 465 ASN E 318
REMARK 465 GLU E 319
REMARK 465 GLU E 320
REMARK 465 ASP E 321
REMARK 465 GLU E 322
REMARK 465 LYS E 503
REMARK 465 ASP E 504
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 TYR A 32 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 128 CG CD CE NZ
REMARK 470 GLU A 131 CG CD OE1 OE2
REMARK 470 ARG A 185 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 187 CG CD NE CZ NH1 NH2
REMARK 470 TYR B 32 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 128 CG CD CE NZ
REMARK 470 LYS B 130 CG CD CE NZ
REMARK 470 LYS B 133 CG CD CE NZ
REMARK 470 ARG B 187 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 188 CG CD CE NZ
REMARK 470 GLU D 309 CG CD OE1 OE2
REMARK 470 GLN D 310 CG CD OE1 NE2
REMARK 470 LEU D 311 CG CD1 CD2
REMARK 470 GLN D 313 CG CD OE1 NE2
REMARK 470 ILE D 314 CG1 CG2 CD1
REMARK 470 GLU D 317 CG CD OE1 OE2
REMARK 470 GLU D 319 CG CD OE1 OE2
REMARK 470 ASP D 321 CG OD1 OD2
REMARK 470 GLU D 322 CG CD OE1 OE2
REMARK 470 ARG D 420 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 438 CG CD CE NZ
REMARK 470 LYS D 467 CG CD CE NZ
REMARK 470 MET D 469 CG SD CE
REMARK 470 LEU D 470 CG CD1 CD2
REMARK 470 LYS E 438 CG CD CE NZ
REMARK 470 VAL E 462 CG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O THR A 35 O HOH A 2002 2.05
REMARK 500 O THR B 35 O HOH B 2001 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 ALA D 316 N - CA - CB ANGL. DEV. = 10.1 DEGREES
REMARK 500 ARG E 358 NE - CZ - NH2 ANGL. DEV. = 3.7 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 LYS A 96 -58.84 -123.26
REMARK 500 ILE A 126 24.95 -73.88
REMARK 500 GLU A 127 -59.53 -124.56
REMARK 500 CYS A 178 34.23 79.66
REMARK 500 ARG A 185 177.58 -59.32
REMARK 500 LYS A 186 18.06 52.10
REMARK 500 LYS A 188 129.32 -25.87
REMARK 500 ASN B 39 94.03 -58.16
REMARK 500 SER B 41 107.56 175.19
REMARK 500 GLU B 62 3.83 -67.51
REMARK 500 PRO B 69 -7.84 -53.12
REMARK 500 LYS B 96 -56.92 -125.74
REMARK 500 ILE B 126 30.44 -81.99
REMARK 500 GLU B 127 -59.65 -131.64
REMARK 500 CYS B 178 6.68 86.59
REMARK 500 PRO B 180 91.70 -62.22
REMARK 500 PRO B 181 0.98 -69.45
REMARK 500 LYS B 183 -41.66 -134.72
REMARK 500 LYS B 184 117.57 -173.42
REMARK 500 LYS B 186 94.77 -63.51
REMARK 500 ARG B 187 22.13 -148.08
REMARK 500 LYS B 188 -75.22 -118.55
REMARK 500 ILE D 314 91.02 -55.62
REMARK 500 ALA D 315 24.24 -164.50
REMARK 500 ALA D 316 76.26 -167.14
REMARK 500 ASN D 318 -169.38 57.35
REMARK 500 HIS D 323 44.05 -155.74
REMARK 500 ASN D 326 92.61 -62.66
REMARK 500 LEU D 341 -81.54 -63.13
REMARK 500 ASP D 342 72.72 -117.26
REMARK 500 SER D 380 43.30 -90.56
REMARK 500 SER D 381 -62.05 -138.98
REMARK 500 PRO D 383 178.60 -48.03
REMARK 500 PRO D 385 -159.90 -68.46
REMARK 500 LEU D 386 93.39 -163.65
REMARK 500 LEU D 390 26.03 -62.97
REMARK 500 ASN D 419 -72.04 -104.97
REMARK 500 ARG D 420 -65.56 -94.55
REMARK 500 LYS D 435 56.92 73.06
REMARK 500 LYS D 438 106.79 -59.06
REMARK 500 ASP D 440 143.59 172.01
REMARK 500 PRO D 466 173.84 -59.56
REMARK 500 LEU D 470 -63.46 -137.69
REMARK 500 ASP D 483 -165.21 -160.97
REMARK 500 SER D 491 142.47 -179.63
REMARK 500 SER E 324 101.30 -166.58
REMARK 500 ASN E 326 92.83 -68.89
REMARK 500 ALA E 331 155.98 -49.57
REMARK 500 LEU E 341 -99.90 -71.06
REMARK 500 VAL E 359 96.61 77.41
REMARK 500
REMARK 500 THIS ENTRY HAS 67 RAMACHANDRAN OUTLIERS.
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 A1191 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 16 NZ
REMARK 620 2 THR A 17 OG1 142.7
REMARK 620 3 THR A 35 O 147.2 69.3
REMARK 620 4 ASP A 57 OD2 111.6 65.8 85.8
REMARK 620 5 ASP A 57 OD1 66.6 101.9 124.1 44.9
REMARK 620 6 GDP A1190 O2B 95.7 63.8 96.3 124.8 130.3
REMARK 620 7 HOH A2002 O 133.2 60.3 43.5 115.0 159.7 53.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1191 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 17 OG1
REMARK 620 2 ASP B 57 OD1 99.8
REMARK 620 3 ASP B 57 OD2 57.2 45.8
REMARK 620 4 GDP B1190 O2B 66.1 150.2 122.5
REMARK 620 5 HOH B2001 O 81.4 156.6 123.0 51.2
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 A1191
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1191
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A1190
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B1190
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GER D1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GER E1503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E96 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE RAC/P67PHOX COMPLEX
REMARK 900 RELATED ID: 1HE1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE GAP DOMAIN OF THE
REMARK 900 PSEUDOMONAS AERUGINOSA EXOS TOXIN AND HUMAN RAC
REMARK 900 RELATED ID: 1MH1 RELATED DB: PDB
REMARK 900 SMALL G-PROTEIN
REMARK 900 RELATED ID: 1CC0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX
REMARK 900 RELATED ID: 1RHO RELATED DB: PDB
REMARK 900 STRUCTURE OF RHO GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR
DBREF 1HH4 A 1 192 UNP P15154 RAC1_HUMAN 1 192
DBREF 1HH4 B 1 192 UNP P15154 RAC1_HUMAN 1 192
DBREF 1HH4 D 301 504 UNP P52565 GDIR_HUMAN 1 204
DBREF 1HH4 E 301 504 UNP P52565 GDIR_HUMAN 1 204
SEQADV 1HH4 SER A 78 UNP P15154 PHE 78 CLONING ARTIFACT
SEQADV 1HH4 PRO A 1 UNP P15154 MET 1 CLONING ARTIFACT
SEQADV 1HH4 SER B 78 UNP P15154 PHE 78 CLONING ARTIFACT
SEQADV 1HH4 PRO B 1 UNP P15154 MET 1 CLONING ARTIFACT
SEQRES 1 A 192 PRO GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA
SEQRES 2 A 192 VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN
SEQRES 3 A 192 ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN
SEQRES 4 A 192 TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN
SEQRES 5 A 192 LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP
SEQRES 6 A 192 ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL SER
SEQRES 7 A 192 LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU
SEQRES 8 A 192 ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS
SEQRES 9 A 192 CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU
SEQRES 10 A 192 ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS
SEQRES 11 A 192 GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU
SEQRES 12 A 192 ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU
SEQRES 13 A 192 CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE
SEQRES 14 A 192 ASP GLU ALA ILE ARG ALA VAL LEU CYS PRO PRO PRO VAL
SEQRES 15 A 192 LYS LYS ARG LYS ARG LYS CYS LEU LEU LEU
SEQRES 1 B 192 PRO GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA
SEQRES 2 B 192 VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN
SEQRES 3 B 192 ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN
SEQRES 4 B 192 TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN
SEQRES 5 B 192 LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP
SEQRES 6 B 192 ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL SER
SEQRES 7 B 192 LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU
SEQRES 8 B 192 ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS
SEQRES 9 B 192 CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU
SEQRES 10 B 192 ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS
SEQRES 11 B 192 GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU
SEQRES 12 B 192 ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU
SEQRES 13 B 192 CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE
SEQRES 14 B 192 ASP GLU ALA ILE ARG ALA VAL LEU CYS PRO PRO PRO VAL
SEQRES 15 B 192 LYS LYS ARG LYS ARG LYS CYS LEU LEU LEU
SEQRES 1 D 204 MET ALA GLU GLN GLU PRO THR ALA GLU GLN LEU ALA GLN
SEQRES 2 D 204 ILE ALA ALA GLU ASN GLU GLU ASP GLU HIS SER VAL ASN
SEQRES 3 D 204 TYR LYS PRO PRO ALA GLN LYS SER ILE GLN GLU ILE GLN
SEQRES 4 D 204 GLU LEU ASP LYS ASP ASP GLU SER LEU ARG LYS TYR LYS
SEQRES 5 D 204 GLU ALA LEU LEU GLY ARG VAL ALA VAL SER ALA ASP PRO
SEQRES 6 D 204 ASN VAL PRO ASN VAL VAL VAL THR GLY LEU THR LEU VAL
SEQRES 7 D 204 CYS SER SER ALA PRO GLY PRO LEU GLU LEU ASP LEU THR
SEQRES 8 D 204 GLY ASP LEU GLU SER PHE LYS LYS GLN SER PHE VAL LEU
SEQRES 9 D 204 LYS GLU GLY VAL GLU TYR ARG ILE LYS ILE SER PHE ARG
SEQRES 10 D 204 VAL ASN ARG GLU ILE VAL SER GLY MET LYS TYR ILE GLN
SEQRES 11 D 204 HIS THR TYR ARG LYS GLY VAL LYS ILE ASP LYS THR ASP
SEQRES 12 D 204 TYR MET VAL GLY SER TYR GLY PRO ARG ALA GLU GLU TYR
SEQRES 13 D 204 GLU PHE LEU THR PRO VAL GLU GLU ALA PRO LYS GLY MET
SEQRES 14 D 204 LEU ALA ARG GLY SER TYR SER ILE LYS SER ARG PHE THR
SEQRES 15 D 204 ASP ASP ASP LYS THR ASP HIS LEU SER TRP GLU TRP ASN
SEQRES 16 D 204 LEU THR ILE LYS LYS ASP TRP LYS ASP
SEQRES 1 E 204 MET ALA GLU GLN GLU PRO THR ALA GLU GLN LEU ALA GLN
SEQRES 2 E 204 ILE ALA ALA GLU ASN GLU GLU ASP GLU HIS SER VAL ASN
SEQRES 3 E 204 TYR LYS PRO PRO ALA GLN LYS SER ILE GLN GLU ILE GLN
SEQRES 4 E 204 GLU LEU ASP LYS ASP ASP GLU SER LEU ARG LYS TYR LYS
SEQRES 5 E 204 GLU ALA LEU LEU GLY ARG VAL ALA VAL SER ALA ASP PRO
SEQRES 6 E 204 ASN VAL PRO ASN VAL VAL VAL THR GLY LEU THR LEU VAL
SEQRES 7 E 204 CYS SER SER ALA PRO GLY PRO LEU GLU LEU ASP LEU THR
SEQRES 8 E 204 GLY ASP LEU GLU SER PHE LYS LYS GLN SER PHE VAL LEU
SEQRES 9 E 204 LYS GLU GLY VAL GLU TYR ARG ILE LYS ILE SER PHE ARG
SEQRES 10 E 204 VAL ASN ARG GLU ILE VAL SER GLY MET LYS TYR ILE GLN
SEQRES 11 E 204 HIS THR TYR ARG LYS GLY VAL LYS ILE ASP LYS THR ASP
SEQRES 12 E 204 TYR MET VAL GLY SER TYR GLY PRO ARG ALA GLU GLU TYR
SEQRES 13 E 204 GLU PHE LEU THR PRO VAL GLU GLU ALA PRO LYS GLY MET
SEQRES 14 E 204 LEU ALA ARG GLY SER TYR SER ILE LYS SER ARG PHE THR
SEQRES 15 E 204 ASP ASP ASP LYS THR ASP HIS LEU SER TRP GLU TRP ASN
SEQRES 16 E 204 LEU THR ILE LYS LYS ASP TRP LYS ASP
HET GDP A1190 28
HET MG A1191 1
HET GDP B1190 28
HET MG B1191 1
HET GER D1502 20
HET GER E1503 20
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM GER GERAN-8-YL GERAN
FORMUL 5 GDP 2(C10 H15 N5 O11 P2)
FORMUL 6 MG 2(MG 2+)
FORMUL 9 GER 2(C20 H34)
FORMUL 11 HOH *30(H2 O)
HELIX 1 1 GLY A 15 THR A 25 1 11
HELIX 2 2 GLN A 61 ASP A 65 5 5
HELIX 3 3 LEU A 67 TYR A 72 5 6
HELIX 4 4 SER A 86 LYS A 96 1 11
HELIX 5 5 LYS A 96 CYS A 105 1 10
HELIX 6 6 LYS A 116 ARG A 120 5 5
HELIX 7 7 ASP A 124 LEU A 129 1 6
HELIX 8 8 THR A 138 GLY A 150 1 13
HELIX 9 9 GLY A 164 LEU A 177 1 14
HELIX 10 10 GLY B 15 THR B 25 1 11
HELIX 11 11 LEU B 67 TYR B 72 5 6
HELIX 12 12 SER B 86 LYS B 96 1 11
HELIX 13 13 LYS B 96 CYS B 105 1 10
HELIX 14 14 LYS B 116 ARG B 120 5 5
HELIX 15 15 ASP B 124 LEU B 129 1 6
HELIX 16 16 LYS B 130 LYS B 133 5 4
HELIX 17 17 THR B 138 GLY B 150 1 13
HELIX 18 18 GLY B 164 LEU B 177 1 14
HELIX 19 19 SER D 334 GLU D 340 1 7
HELIX 20 20 ASP D 345 GLY D 357 1 13
HELIX 21 21 LEU D 394 LYS D 399 5 6
HELIX 22 22 SER E 334 GLU E 340 1 7
HELIX 23 23 ASP E 345 GLY E 357 1 13
HELIX 24 24 LEU E 394 LYS E 399 5 6
HELIX 25 25 LYS E 467 ARG E 472 1 6
SHEET 1 AA 6 TYR A 40 MET A 45 0
SHEET 2 AA 6 PRO A 50 ASP A 57 -1 O VAL A 51 N VAL A 44
SHEET 3 AA 6 LYS A 5 GLY A 10 1 O CYS A 6 N TRP A 56
SHEET 4 AA 6 VAL A 77 SER A 83 1 O VAL A 77 N VAL A 7
SHEET 5 AA 6 ILE A 110 THR A 115 1 O ILE A 111 N ILE A 80
SHEET 6 AA 6 LYS A 153 GLU A 156 1 O LYS A 153 N LEU A 112
SHEET 1 BA 6 ALA B 42 MET B 45 0
SHEET 2 BA 6 PRO B 50 ASP B 57 -1 O VAL B 51 N VAL B 44
SHEET 3 BA 6 GLN B 2 GLY B 10 1 O GLN B 2 N ASN B 52
SHEET 4 BA 6 VAL B 77 SER B 83 1 O VAL B 77 N VAL B 7
SHEET 5 BA 6 ILE B 110 THR B 115 1 O ILE B 111 N ILE B 80
SHEET 6 BA 6 LYS B 153 GLU B 156 1 O LYS B 153 N LEU B 112
SHEET 1 DA 4 GLU D 387 ASP D 389 0
SHEET 2 DA 4 VAL D 370 CYS D 379 -1 O LEU D 375 N LEU D 388
SHEET 3 DA 4 GLU D 409 VAL D 418 -1 O ARG D 411 N VAL D 378
SHEET 4 DA 4 GLU D 463 GLU D 464 -1 O GLU D 463 N TYR D 410
SHEET 1 DB 4 GLU D 387 ASP D 389 0
SHEET 2 DB 4 VAL D 370 CYS D 379 -1 O LEU D 375 N LEU D 388
SHEET 3 DB 4 GLU D 409 VAL D 418 -1 O ARG D 411 N VAL D 378
SHEET 4 DB 4 TYR D 456 LEU D 459 -1 O TYR D 456 N PHE D 416
SHEET 1 DC 5 SER D 401 LEU D 404 0
SHEET 2 DC 5 LEU D 490 ILE D 498 1 O ASN D 495 N PHE D 402
SHEET 3 DC 5 SER D 474 THR D 482 -1 O TYR D 475 N LEU D 496
SHEET 4 DC 5 VAL D 423 TYR D 433 -1 O LYS D 427 N THR D 482
SHEET 5 DC 5 LYS D 438 TYR D 449 -1 N ILE D 439 O THR D 432
SHEET 1 EA 4 LEU E 386 ASP E 389 0
SHEET 2 EA 4 VAL E 370 CYS E 379 -1 O LEU E 375 N LEU E 388
SHEET 3 EA 4 GLU E 409 VAL E 418 -1 O ARG E 411 N VAL E 378
SHEET 4 EA 4 GLU E 463 GLU E 464 -1 O GLU E 463 N TYR E 410
SHEET 1 EB 4 LEU E 386 ASP E 389 0
SHEET 2 EB 4 VAL E 370 CYS E 379 -1 O LEU E 375 N LEU E 388
SHEET 3 EB 4 GLU E 409 VAL E 418 -1 O ARG E 411 N VAL E 378
SHEET 4 EB 4 TYR E 456 LEU E 459 -1 O TYR E 456 N PHE E 416
SHEET 1 EC 5 SER E 401 LYS E 405 0
SHEET 2 EC 5 LEU E 490 LYS E 499 1 O ASN E 495 N PHE E 402
SHEET 3 EC 5 SER E 474 THR E 482 -1 O TYR E 475 N LEU E 496
SHEET 4 EC 5 VAL E 423 TYR E 433 -1 O LYS E 427 N THR E 482
SHEET 5 EC 5 LYS E 438 TYR E 449 -1 N ILE E 439 O THR E 432
LINK NZ LYS A 16 MG MG A1191 1555 1555 2.97
LINK OG1 THR A 17 MG MG A1191 1555 1555 2.38
LINK O THR A 35 MG MG A1191 1555 1555 2.89
LINK OD2 ASP A 57 MG MG A1191 1555 1555 2.74
LINK OD1 ASP A 57 MG MG A1191 1555 1555 2.97
LINK O2B GDP A1190 MG MG A1191 1555 1555 2.79
LINK MG MG A1191 O HOH A2002 1555 1555 2.59
LINK OG1 THR B 17 MG MG B1191 1555 1555 2.63
LINK OD1 ASP B 57 MG MG B1191 1555 1555 2.78
LINK OD2 ASP B 57 MG MG B1191 1555 1555 2.90
LINK O2B GDP B1190 MG MG B1191 1555 1555 2.77
LINK MG MG B1191 O HOH B2001 1555 1555 2.48
SITE 1 AC1 7 LYS A 16 THR A 17 THR A 35 ASP A 57
SITE 2 AC1 7 THR A 58 GDP A1190 HOH A2002
SITE 1 AC2 7 LYS B 16 THR B 17 THR B 35 ASP B 57
SITE 2 AC2 7 THR B 58 GDP B1190 HOH B2001
SITE 1 AC3 16 GLY A 12 ALA A 13 VAL A 14 GLY A 15
SITE 2 AC3 16 LYS A 16 THR A 17 CYS A 18 PHE A 28
SITE 3 AC3 16 ILE A 33 LYS A 116 ASP A 118 LEU A 119
SITE 4 AC3 16 ALA A 159 LEU A 160 MG A1191 HOH A2002
SITE 1 AC4 17 GLY B 12 ALA B 13 VAL B 14 GLY B 15
SITE 2 AC4 17 LYS B 16 THR B 17 CYS B 18 PHE B 28
SITE 3 AC4 17 ILE B 33 LYS B 116 ASP B 118 LEU B 119
SITE 4 AC4 17 ALA B 159 LEU B 160 MG B1191 HOH B2001
SITE 5 AC4 17 HOH B2006
SITE 1 AC5 9 LEU D 377 TYR D 410 GLN D 430 THR D 432
SITE 2 AC5 9 ILE D 439 PRO D 466 ALA D 471 TRP D 494
SITE 3 AC5 9 LEU D 496
SITE 1 AC6 12 ARG B 187 LYS B 188 CYS B 189 LEU E 377
SITE 2 AC6 12 TYR E 410 GLN E 430 THR E 432 ILE E 439
SITE 3 AC6 12 PRO E 466 ALA E 471 TRP E 494 LEU E 496
CRYST1 154.700 88.700 62.600 90.00 90.00 90.00 P 21 21 2 8
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 0.006464 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011274 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015974 0.00000
(ATOM LINES ARE NOT SHOWN.)
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