HEADER CHAPERONE 29-MAR-13 4JYC
TITLE MEAB, A BACTERIAL HOMOLOG OF MMAA, IN ITS APO FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHYLMALONYL-COA MUTASE ACCESSORY PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHYLOBACTERIUM EXTORQUENS;
SOURCE 3 ORGANISM_TAXID: 272630;
SOURCE 4 STRAIN: AM1;
SOURCE 5 GENE: MEAB, MEXAM1_META1P0188;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-21D(+)
KEYWDS ALPHA AND BETA PROTEIN, P-LOOP CONTAINING NUCLEOSIDE TRIPHOSPHATE
KEYWDS 2 HYDROLASES, GTPASE, METALLOCHAPERONE, METHYLMALONYL-COA MUTASE
KEYWDS 3 (MCM), CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KOUTMOS,M.LOFGREN,D.PADOVANI,R.BANERJEE
REVDAT 4 20-SEP-23 4JYC 1 REMARK SEQADV
REVDAT 3 11-SEP-13 4JYC 1 JRNL
REVDAT 2 14-AUG-13 4JYC 1 JRNL
REVDAT 1 24-JUL-13 4JYC 0
JRNL AUTH M.LOFGREN,D.PADOVANI,M.KOUTMOS,R.BANERJEE
JRNL TITL A SWITCH III MOTIF RELAYS SIGNALING BETWEEN A B12 ENZYME AND
JRNL TITL 2 ITS G-PROTEIN CHAPERONE.
JRNL REF NAT.CHEM.BIOL. V. 9 535 2013
JRNL REFN ISSN 1552-4450
JRNL PMID 23873214
JRNL DOI 10.1038/NCHEMBIO.1298
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 73498
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3932
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4868
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.2560
REMARK 3 BIN FREE R VALUE SET COUNT : 245
REMARK 3 BIN FREE R VALUE : 0.3220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9335
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 403
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.08000
REMARK 3 B22 (A**2) : 2.87000
REMARK 3 B33 (A**2) : -2.98000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.74000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.238
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.208
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.149
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.814
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9546 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 9620 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12948 ; 1.398 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): 21798 ; 0.780 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1268 ; 6.024 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 368 ;33.898 ;22.011
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1600 ;15.565 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 111 ;19.262 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1544 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10776 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2039 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : BABINET MODEL WITH 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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4JYC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078658.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-APR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03262
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : K-B PAIR OF BIOMORPH MIRRORS FOR
REMARK 200 VERTICAL AND HORIZONTAL FOCUSING
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77430
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.12400
REMARK 200 R SYM (I) : 0.08600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.56
REMARK 200 R MERGE FOR SHELL (I) : 0.56200
REMARK 200 R SYM FOR SHELL (I) : 0.50600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.240
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: PDB ENTRY 2QM7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG400, 50 MM HEPES PH 7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 92.73150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.18850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 92.73150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.18850
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 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: 5120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL
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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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 1
REMARK 465 SER A 2
REMARK 465 ALA A 3
REMARK 465 THR A 4
REMARK 465 LEU A 5
REMARK 465 GLY A 179
REMARK 465 ALA A 180
REMARK 465 GLY A 181
REMARK 465 ASP A 182
REMARK 465 GLU A 183
REMARK 465 LEU A 184
REMARK 465 GLN A 185
REMARK 465 GLY A 186
REMARK 465 ILE A 187
REMARK 465 ASP A 204
REMARK 465 ASP A 205
REMARK 465 GLY A 328
REMARK 465 LEU A 329
REMARK 465 LEU A 330
REMARK 465 GLU A 331
REMARK 465 HIS A 332
REMARK 465 HIS A 333
REMARK 465 HIS A 334
REMARK 465 HIS A 335
REMARK 465 HIS A 336
REMARK 465 HIS A 337
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLY B 179
REMARK 465 ALA B 180
REMARK 465 GLY B 181
REMARK 465 ASP B 182
REMARK 465 GLU B 183
REMARK 465 LEU B 184
REMARK 465 ALA B 203
REMARK 465 ASP B 204
REMARK 465 ASP B 205
REMARK 465 GLY B 206
REMARK 465 ASP B 207
REMARK 465 LEU B 329
REMARK 465 LEU B 330
REMARK 465 GLU B 331
REMARK 465 HIS B 332
REMARK 465 HIS B 333
REMARK 465 HIS B 334
REMARK 465 HIS B 335
REMARK 465 HIS B 336
REMARK 465 HIS B 337
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 ALA C 3
REMARK 465 THR C 4
REMARK 465 LEU C 5
REMARK 465 LEU C 330
REMARK 465 GLU C 331
REMARK 465 HIS C 332
REMARK 465 HIS C 333
REMARK 465 HIS C 334
REMARK 465 HIS C 335
REMARK 465 HIS C 336
REMARK 465 HIS C 337
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 ALA D 3
REMARK 465 THR D 4
REMARK 465 LEU D 5
REMARK 465 GLY D 99
REMARK 465 GLY D 100
REMARK 465 SER D 101
REMARK 465 ILE D 102
REMARK 465 LEU D 103
REMARK 465 GLY D 104
REMARK 465 ASP D 105
REMARK 465 LYS D 106
REMARK 465 GLY D 328
REMARK 465 LEU D 329
REMARK 465 LEU D 330
REMARK 465 GLU D 331
REMARK 465 HIS D 332
REMARK 465 HIS D 333
REMARK 465 HIS D 334
REMARK 465 HIS D 335
REMARK 465 HIS D 336
REMARK 465 HIS D 337
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG C 220 CA CB CG CD NE CZ NH1
REMARK 480 ARG C 220 NH2
REMARK 480 ARG D 14 CA CB CG CD NE CZ NH1
REMARK 480 ARG D 14 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HH12 ARG B 116 O HOH B 484 1.43
REMARK 500 H THR D 234 O HOH D 686 1.44
REMARK 500 HH11 ARG C 137 OD1 ASP C 276 1.47
REMARK 500 HZ1 LYS C 271 O HOH C 477 1.54
REMARK 500 HH11 ARG D 137 OD1 ASP D 276 1.57
REMARK 500 NH1 ARG B 116 O HOH B 484 1.78
REMARK 500 NH1 ARG C 137 OD1 ASP C 276 2.14
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 137 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 137 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG B 259 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 273 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG D 137 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG D 137 NE - CZ - NH2 ANGL. DEV. = -3.9 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 ASP A 105 58.57 -148.68
REMARK 500 LYS A 202 60.15 75.05
REMARK 500 MET C 109 70.35 -115.33
REMARK 500 ASP C 204 58.84 71.77
REMARK 500 ASP C 205 -157.96 -149.17
REMARK 500 ALA C 231 -134.56 64.81
REMARK 500 ILE C 327 -145.82 -94.88
REMARK 500 ARG D 33 54.38 -91.00
REMARK 500 ASP D 36 -65.00 74.28
REMARK 500 GLN D 160 71.29 -105.14
REMARK 500 THR D 227 138.14 -175.42
REMARK 500 SER D 230 -154.34 -74.78
REMARK 500 ALA D 231 145.84 67.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL A 66 GLY A 67 122.43
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 GDP D 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QM7 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN BOUND WITH GDP
REMARK 900 RELATED ID: 2QM8 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH PI IN THE ACTIVE SITE
REMARK 900 RELATED ID: 4JYB RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH GNP IN THE ACTIVE SITE
DBREF 4JYC A 1 329 UNP C5AP93 C5AP93_METEA 1 329
DBREF 4JYC B 1 329 UNP C5AP93 C5AP93_METEA 1 329
DBREF 4JYC C 1 329 UNP C5AP93 C5AP93_METEA 1 329
DBREF 4JYC D 1 329 UNP C5AP93 C5AP93_METEA 1 329
SEQADV 4JYC PHE A 192 UNP C5AP93 LEU 192 ENGINEERED MUTATION
SEQADV 4JYC LEU A 330 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC GLU A 331 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS A 332 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS A 333 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS A 334 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS A 335 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS A 336 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS A 337 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC PHE B 192 UNP C5AP93 LEU 192 ENGINEERED MUTATION
SEQADV 4JYC LEU B 330 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC GLU B 331 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS B 332 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS B 333 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS B 334 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS B 335 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS B 336 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS B 337 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC PHE C 192 UNP C5AP93 LEU 192 ENGINEERED MUTATION
SEQADV 4JYC LEU C 330 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC GLU C 331 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS C 332 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS C 333 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS C 334 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS C 335 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS C 336 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS C 337 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC PHE D 192 UNP C5AP93 LEU 192 ENGINEERED MUTATION
SEQADV 4JYC LEU D 330 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC GLU D 331 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS D 332 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS D 333 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS D 334 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS D 335 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS D 336 UNP C5AP93 EXPRESSION TAG
SEQADV 4JYC HIS D 337 UNP C5AP93 EXPRESSION TAG
SEQRES 1 A 337 MET SER ALA THR LEU PRO ASP MET ASP THR LEU ARG GLU
SEQRES 2 A 337 ARG LEU LEU ALA GLY ASP ARG ALA ALA LEU ALA ARG ALA
SEQRES 3 A 337 ILE THR LEU ALA GLU SER ARG ARG ALA ASP HIS ARG ALA
SEQRES 4 A 337 ALA VAL ARG ASP LEU ILE ASP ALA VAL LEU PRO GLN THR
SEQRES 5 A 337 GLY ARG ALA ILE ARG VAL GLY ILE THR GLY VAL PRO GLY
SEQRES 6 A 337 VAL GLY LYS SER THR THR ILE ASP ALA LEU GLY SER LEU
SEQRES 7 A 337 LEU THR ALA ALA GLY HIS LYS VAL ALA VAL LEU ALA VAL
SEQRES 8 A 337 ASP PRO SER SER THR ARG THR GLY GLY SER ILE LEU GLY
SEQRES 9 A 337 ASP LYS THR ARG MET ALA ARG LEU ALA ILE ASP ARG ASN
SEQRES 10 A 337 ALA PHE ILE ARG PRO SER PRO SER SER GLY THR LEU GLY
SEQRES 11 A 337 GLY VAL ALA ALA LYS THR ARG GLU THR MET LEU LEU CYS
SEQRES 12 A 337 GLU ALA ALA GLY PHE ASP VAL ILE LEU VAL GLU THR VAL
SEQRES 13 A 337 GLY VAL GLY GLN SER GLU THR ALA VAL ALA ASP LEU THR
SEQRES 14 A 337 ASP PHE PHE LEU VAL LEU MET LEU PRO GLY ALA GLY ASP
SEQRES 15 A 337 GLU LEU GLN GLY ILE LYS LYS GLY ILE PHE GLU LEU ALA
SEQRES 16 A 337 ASP MET ILE ALA VAL ASN LYS ALA ASP ASP GLY ASP GLY
SEQRES 17 A 337 GLU ARG ARG ALA SER ALA ALA ALA SER GLU TYR ARG ALA
SEQRES 18 A 337 ALA LEU HIS ILE LEU THR PRO PRO SER ALA THR TRP THR
SEQRES 19 A 337 PRO PRO VAL VAL THR ILE SER GLY LEU HIS GLY LYS GLY
SEQRES 20 A 337 LEU ASP SER LEU TRP SER ARG ILE GLU ASP HIS ARG SER
SEQRES 21 A 337 LYS LEU THR ALA THR GLY GLU ILE ALA GLY LYS ARG ARG
SEQRES 22 A 337 GLU GLN ASP VAL LYS TRP MET TRP ALA LEU VAL HIS GLU
SEQRES 23 A 337 ARG LEU HIS GLN ARG LEU VAL GLY SER ALA GLU VAL ARG
SEQRES 24 A 337 GLN ALA THR ALA GLU ALA GLU ARG ALA VAL ALA GLY GLY
SEQRES 25 A 337 GLU HIS SER PRO ALA ALA GLY ALA ASP ALA ILE ALA THR
SEQRES 26 A 337 LEU ILE GLY LEU LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 337 MET SER ALA THR LEU PRO ASP MET ASP THR LEU ARG GLU
SEQRES 2 B 337 ARG LEU LEU ALA GLY ASP ARG ALA ALA LEU ALA ARG ALA
SEQRES 3 B 337 ILE THR LEU ALA GLU SER ARG ARG ALA ASP HIS ARG ALA
SEQRES 4 B 337 ALA VAL ARG ASP LEU ILE ASP ALA VAL LEU PRO GLN THR
SEQRES 5 B 337 GLY ARG ALA ILE ARG VAL GLY ILE THR GLY VAL PRO GLY
SEQRES 6 B 337 VAL GLY LYS SER THR THR ILE ASP ALA LEU GLY SER LEU
SEQRES 7 B 337 LEU THR ALA ALA GLY HIS LYS VAL ALA VAL LEU ALA VAL
SEQRES 8 B 337 ASP PRO SER SER THR ARG THR GLY GLY SER ILE LEU GLY
SEQRES 9 B 337 ASP LYS THR ARG MET ALA ARG LEU ALA ILE ASP ARG ASN
SEQRES 10 B 337 ALA PHE ILE ARG PRO SER PRO SER SER GLY THR LEU GLY
SEQRES 11 B 337 GLY VAL ALA ALA LYS THR ARG GLU THR MET LEU LEU CYS
SEQRES 12 B 337 GLU ALA ALA GLY PHE ASP VAL ILE LEU VAL GLU THR VAL
SEQRES 13 B 337 GLY VAL GLY GLN SER GLU THR ALA VAL ALA ASP LEU THR
SEQRES 14 B 337 ASP PHE PHE LEU VAL LEU MET LEU PRO GLY ALA GLY ASP
SEQRES 15 B 337 GLU LEU GLN GLY ILE LYS LYS GLY ILE PHE GLU LEU ALA
SEQRES 16 B 337 ASP MET ILE ALA VAL ASN LYS ALA ASP ASP GLY ASP GLY
SEQRES 17 B 337 GLU ARG ARG ALA SER ALA ALA ALA SER GLU TYR ARG ALA
SEQRES 18 B 337 ALA LEU HIS ILE LEU THR PRO PRO SER ALA THR TRP THR
SEQRES 19 B 337 PRO PRO VAL VAL THR ILE SER GLY LEU HIS GLY LYS GLY
SEQRES 20 B 337 LEU ASP SER LEU TRP SER ARG ILE GLU ASP HIS ARG SER
SEQRES 21 B 337 LYS LEU THR ALA THR GLY GLU ILE ALA GLY LYS ARG ARG
SEQRES 22 B 337 GLU GLN ASP VAL LYS TRP MET TRP ALA LEU VAL HIS GLU
SEQRES 23 B 337 ARG LEU HIS GLN ARG LEU VAL GLY SER ALA GLU VAL ARG
SEQRES 24 B 337 GLN ALA THR ALA GLU ALA GLU ARG ALA VAL ALA GLY GLY
SEQRES 25 B 337 GLU HIS SER PRO ALA ALA GLY ALA ASP ALA ILE ALA THR
SEQRES 26 B 337 LEU ILE GLY LEU LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 337 MET SER ALA THR LEU PRO ASP MET ASP THR LEU ARG GLU
SEQRES 2 C 337 ARG LEU LEU ALA GLY ASP ARG ALA ALA LEU ALA ARG ALA
SEQRES 3 C 337 ILE THR LEU ALA GLU SER ARG ARG ALA ASP HIS ARG ALA
SEQRES 4 C 337 ALA VAL ARG ASP LEU ILE ASP ALA VAL LEU PRO GLN THR
SEQRES 5 C 337 GLY ARG ALA ILE ARG VAL GLY ILE THR GLY VAL PRO GLY
SEQRES 6 C 337 VAL GLY LYS SER THR THR ILE ASP ALA LEU GLY SER LEU
SEQRES 7 C 337 LEU THR ALA ALA GLY HIS LYS VAL ALA VAL LEU ALA VAL
SEQRES 8 C 337 ASP PRO SER SER THR ARG THR GLY GLY SER ILE LEU GLY
SEQRES 9 C 337 ASP LYS THR ARG MET ALA ARG LEU ALA ILE ASP ARG ASN
SEQRES 10 C 337 ALA PHE ILE ARG PRO SER PRO SER SER GLY THR LEU GLY
SEQRES 11 C 337 GLY VAL ALA ALA LYS THR ARG GLU THR MET LEU LEU CYS
SEQRES 12 C 337 GLU ALA ALA GLY PHE ASP VAL ILE LEU VAL GLU THR VAL
SEQRES 13 C 337 GLY VAL GLY GLN SER GLU THR ALA VAL ALA ASP LEU THR
SEQRES 14 C 337 ASP PHE PHE LEU VAL LEU MET LEU PRO GLY ALA GLY ASP
SEQRES 15 C 337 GLU LEU GLN GLY ILE LYS LYS GLY ILE PHE GLU LEU ALA
SEQRES 16 C 337 ASP MET ILE ALA VAL ASN LYS ALA ASP ASP GLY ASP GLY
SEQRES 17 C 337 GLU ARG ARG ALA SER ALA ALA ALA SER GLU TYR ARG ALA
SEQRES 18 C 337 ALA LEU HIS ILE LEU THR PRO PRO SER ALA THR TRP THR
SEQRES 19 C 337 PRO PRO VAL VAL THR ILE SER GLY LEU HIS GLY LYS GLY
SEQRES 20 C 337 LEU ASP SER LEU TRP SER ARG ILE GLU ASP HIS ARG SER
SEQRES 21 C 337 LYS LEU THR ALA THR GLY GLU ILE ALA GLY LYS ARG ARG
SEQRES 22 C 337 GLU GLN ASP VAL LYS TRP MET TRP ALA LEU VAL HIS GLU
SEQRES 23 C 337 ARG LEU HIS GLN ARG LEU VAL GLY SER ALA GLU VAL ARG
SEQRES 24 C 337 GLN ALA THR ALA GLU ALA GLU ARG ALA VAL ALA GLY GLY
SEQRES 25 C 337 GLU HIS SER PRO ALA ALA GLY ALA ASP ALA ILE ALA THR
SEQRES 26 C 337 LEU ILE GLY LEU LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 337 MET SER ALA THR LEU PRO ASP MET ASP THR LEU ARG GLU
SEQRES 2 D 337 ARG LEU LEU ALA GLY ASP ARG ALA ALA LEU ALA ARG ALA
SEQRES 3 D 337 ILE THR LEU ALA GLU SER ARG ARG ALA ASP HIS ARG ALA
SEQRES 4 D 337 ALA VAL ARG ASP LEU ILE ASP ALA VAL LEU PRO GLN THR
SEQRES 5 D 337 GLY ARG ALA ILE ARG VAL GLY ILE THR GLY VAL PRO GLY
SEQRES 6 D 337 VAL GLY LYS SER THR THR ILE ASP ALA LEU GLY SER LEU
SEQRES 7 D 337 LEU THR ALA ALA GLY HIS LYS VAL ALA VAL LEU ALA VAL
SEQRES 8 D 337 ASP PRO SER SER THR ARG THR GLY GLY SER ILE LEU GLY
SEQRES 9 D 337 ASP LYS THR ARG MET ALA ARG LEU ALA ILE ASP ARG ASN
SEQRES 10 D 337 ALA PHE ILE ARG PRO SER PRO SER SER GLY THR LEU GLY
SEQRES 11 D 337 GLY VAL ALA ALA LYS THR ARG GLU THR MET LEU LEU CYS
SEQRES 12 D 337 GLU ALA ALA GLY PHE ASP VAL ILE LEU VAL GLU THR VAL
SEQRES 13 D 337 GLY VAL GLY GLN SER GLU THR ALA VAL ALA ASP LEU THR
SEQRES 14 D 337 ASP PHE PHE LEU VAL LEU MET LEU PRO GLY ALA GLY ASP
SEQRES 15 D 337 GLU LEU GLN GLY ILE LYS LYS GLY ILE PHE GLU LEU ALA
SEQRES 16 D 337 ASP MET ILE ALA VAL ASN LYS ALA ASP ASP GLY ASP GLY
SEQRES 17 D 337 GLU ARG ARG ALA SER ALA ALA ALA SER GLU TYR ARG ALA
SEQRES 18 D 337 ALA LEU HIS ILE LEU THR PRO PRO SER ALA THR TRP THR
SEQRES 19 D 337 PRO PRO VAL VAL THR ILE SER GLY LEU HIS GLY LYS GLY
SEQRES 20 D 337 LEU ASP SER LEU TRP SER ARG ILE GLU ASP HIS ARG SER
SEQRES 21 D 337 LYS LEU THR ALA THR GLY GLU ILE ALA GLY LYS ARG ARG
SEQRES 22 D 337 GLU GLN ASP VAL LYS TRP MET TRP ALA LEU VAL HIS GLU
SEQRES 23 D 337 ARG LEU HIS GLN ARG LEU VAL GLY SER ALA GLU VAL ARG
SEQRES 24 D 337 GLN ALA THR ALA GLU ALA GLU ARG ALA VAL ALA GLY GLY
SEQRES 25 D 337 GLU HIS SER PRO ALA ALA GLY ALA ASP ALA ILE ALA THR
SEQRES 26 D 337 LEU ILE GLY LEU LEU GLU HIS HIS HIS HIS HIS HIS
HET GDP D 501 40
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 5 GDP C10 H15 N5 O11 P2
FORMUL 6 HOH *403(H2 O)
HELIX 1 1 ASP A 7 ALA A 17 1 11
HELIX 2 2 ASP A 19 SER A 32 1 14
HELIX 3 3 ARG A 34 LEU A 49 1 16
HELIX 4 4 PRO A 50 THR A 52 5 3
HELIX 5 5 GLY A 67 ALA A 82 1 16
HELIX 6 6 ASP A 92 ARG A 97 5 6
HELIX 7 7 ASP A 105 ARG A 108 5 4
HELIX 8 8 MET A 109 ASP A 115 1 7
HELIX 9 9 THR A 128 ALA A 146 1 19
HELIX 10 10 SER A 161 ASP A 167 1 7
HELIX 11 11 LYS A 189 ALA A 195 1 7
HELIX 12 12 GLY A 208 ILE A 225 1 18
HELIX 13 13 GLY A 247 THR A 265 1 19
HELIX 14 14 GLY A 266 VAL A 293 1 28
HELIX 15 15 SER A 295 GLY A 311 1 17
HELIX 16 16 SER A 315 ILE A 327 1 13
HELIX 17 17 ASP B 7 ALA B 17 1 11
HELIX 18 18 ASP B 19 SER B 32 1 14
HELIX 19 19 ARG B 34 LEU B 49 1 16
HELIX 20 20 PRO B 50 THR B 52 5 3
HELIX 21 21 GLY B 65 ALA B 82 1 18
HELIX 22 22 ASP B 92 ARG B 97 5 6
HELIX 23 23 ASP B 105 MET B 109 5 5
HELIX 24 24 ARG B 111 ASP B 115 5 5
HELIX 25 25 THR B 128 ALA B 146 1 19
HELIX 26 26 SER B 161 ASP B 167 1 7
HELIX 27 27 LYS B 188 ALA B 195 5 8
HELIX 28 28 GLU B 209 THR B 227 1 19
HELIX 29 29 GLY B 247 THR B 265 1 19
HELIX 30 30 GLY B 266 LEU B 292 1 27
HELIX 31 31 SER B 295 GLY B 311 1 17
HELIX 32 32 SER B 315 GLY B 328 1 14
HELIX 33 33 ASP C 7 ALA C 17 1 11
HELIX 34 34 ASP C 19 SER C 32 1 14
HELIX 35 35 ARG C 34 LEU C 49 1 16
HELIX 36 36 PRO C 50 THR C 52 5 3
HELIX 37 37 PRO C 64 ALA C 82 1 19
HELIX 38 38 ASP C 92 THR C 98 5 7
HELIX 39 39 MET C 109 ILE C 114 1 6
HELIX 40 40 THR C 128 ALA C 146 1 19
HELIX 41 41 SER C 161 ASP C 167 1 7
HELIX 42 42 ILE C 191 ALA C 195 5 5
HELIX 43 43 GLY C 208 THR C 227 1 20
HELIX 44 44 GLY C 247 THR C 265 1 19
HELIX 45 45 GLY C 266 ARG C 291 1 26
HELIX 46 46 LEU C 292 GLY C 294 5 3
HELIX 47 47 SER C 295 GLY C 311 1 17
HELIX 48 48 SER C 315 LEU C 326 1 12
HELIX 49 49 ASP D 7 ALA D 17 1 11
HELIX 50 50 ASP D 19 SER D 32 1 14
HELIX 51 51 ASP D 36 VAL D 48 1 13
HELIX 52 52 LEU D 49 THR D 52 5 4
HELIX 53 53 GLY D 67 ALA D 82 1 16
HELIX 54 54 ASP D 92 ARG D 97 5 6
HELIX 55 55 ARG D 111 ASP D 115 5 5
HELIX 56 56 THR D 128 ALA D 146 1 19
HELIX 57 57 SER D 161 ASP D 167 1 7
HELIX 58 58 ALA D 180 LEU D 184 5 5
HELIX 59 59 GLY D 206 LEU D 226 1 21
HELIX 60 60 GLY D 247 THR D 265 1 19
HELIX 61 61 GLY D 266 VAL D 293 1 28
HELIX 62 62 SER D 295 GLY D 311 1 17
HELIX 63 63 SER D 315 ILE D 327 1 13
SHEET 1 A 7 ALA A 118 ARG A 121 0
SHEET 2 A 7 VAL A 86 VAL A 91 1 N VAL A 88 O PHE A 119
SHEET 3 A 7 VAL A 150 THR A 155 1 O LEU A 152 N ALA A 87
SHEET 4 A 7 ILE A 56 GLY A 62 1 N VAL A 58 O VAL A 153
SHEET 5 A 7 PHE A 171 MET A 176 1 O LEU A 173 N GLY A 59
SHEET 6 A 7 MET A 197 ASN A 201 1 O ASN A 201 N MET A 176
SHEET 7 A 7 VAL A 237 ILE A 240 1 O VAL A 238 N VAL A 200
SHEET 1 B 7 ALA B 118 ARG B 121 0
SHEET 2 B 7 VAL B 86 VAL B 91 1 N VAL B 88 O PHE B 119
SHEET 3 B 7 VAL B 150 THR B 155 1 O GLU B 154 N LEU B 89
SHEET 4 B 7 ILE B 56 THR B 61 1 N VAL B 58 O ILE B 151
SHEET 5 B 7 PHE B 171 MET B 176 1 O LEU B 173 N GLY B 59
SHEET 6 B 7 MET B 197 ASN B 201 1 O ASN B 201 N MET B 176
SHEET 7 B 7 VAL B 237 ILE B 240 1 O VAL B 238 N VAL B 200
SHEET 1 C 7 ALA C 118 ARG C 121 0
SHEET 2 C 7 VAL C 86 VAL C 91 1 N VAL C 88 O PHE C 119
SHEET 3 C 7 VAL C 150 THR C 155 1 O LEU C 152 N ALA C 87
SHEET 4 C 7 ILE C 56 THR C 61 1 N VAL C 58 O VAL C 153
SHEET 5 C 7 PHE C 171 MET C 176 1 O LEU C 173 N GLY C 59
SHEET 6 C 7 MET C 197 ASN C 201 1 O ASN C 201 N MET C 176
SHEET 7 C 7 VAL C 237 ILE C 240 1 O VAL C 238 N VAL C 200
SHEET 1 D 7 ALA D 118 ARG D 121 0
SHEET 2 D 7 VAL D 86 VAL D 91 1 N VAL D 88 O PHE D 119
SHEET 3 D 7 VAL D 150 THR D 155 1 O LEU D 152 N LEU D 89
SHEET 4 D 7 ILE D 56 THR D 61 1 N VAL D 58 O ILE D 151
SHEET 5 D 7 PHE D 171 MET D 176 1 O LEU D 173 N GLY D 59
SHEET 6 D 7 MET D 197 VAL D 200 1 O ALA D 199 N VAL D 174
SHEET 7 D 7 VAL D 237 THR D 239 1 O VAL D 238 N VAL D 200
CISPEP 1 GLU C 183 LEU C 184 0 -10.83
CISPEP 2 ALA C 231 THR C 232 0 -16.06
SITE 1 AC1 16 GLY D 65 VAL D 66 GLY D 67 LYS D 68
SITE 2 AC1 16 SER D 69 THR D 70 ASN D 201 LYS D 202
SITE 3 AC1 16 ASP D 204 SER D 241 GLY D 242 LEU D 243
SITE 4 AC1 16 HOH D 620 HOH D 629 HOH D 638 HOH D 639
CRYST1 185.463 58.377 155.280 90.00 110.07 90.00 C 1 2 1 16
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 0.005392 0.000000 0.001970 0.00000
SCALE2 0.000000 0.017130 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006856 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
