HEADER ISOMERASE 14-APR-10 3MKC
TITLE CRYSTAL STRUCTURE OF A PUTATIVE RACEMASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RACEMASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOVIBRIO SP. JE062;
SOURCE 3 ORGANISM_TAXID: 439495;
SOURCE 4 GENE: PJE062_745;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-CODON+RIL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: BC - PSGX3 (BC)
KEYWDS METABOLIC PROCESS, MADALATE RACEMASE, PSI2, NYSGXRC, STRUCTURAL
KEYWDS 2 GENOMICS, PROTEIN STRUCTURE INITIATIVE, NEW YORK SGX RESEARCH CENTER
KEYWDS 3 FOR STRUCTURAL GENOMICS, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.ESWARAMOORTHY,S.K.BURLEY,S.SWAMINATHAN,NEW YORK SGX RESEARCH CENTER
AUTHOR 2 FOR STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 2 10-FEB-21 3MKC 1 AUTHOR JRNL LINK
REVDAT 1 28-APR-10 3MKC 0
JRNL AUTH S.ESWARAMOORTHY,S.K.BURLEY,S.SWAMINATHAN
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE RACEMASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 40312
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) : 0.216
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1612
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.77
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.88
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2550
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 241
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2963
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 152
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.92000
REMARK 3 B22 (A**2) : -1.92000
REMARK 3 B33 (A**2) : 3.83000
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) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.14
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) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.16
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3MKC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058652.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9788
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42424
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 29.00
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : 0.08300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 25.80
REMARK 200 R MERGE FOR SHELL (I) : 0.45000
REMARK 200 R SYM FOR SHELL (I) : 0.45000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHARP, SHELX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE; 0.1M BIS-TRIS PH
REMARK 280 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 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 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 67.41900
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 67.41900
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 47.16150
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 67.41900
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 67.41900
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 47.16150
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 67.41900
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 67.41900
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 47.16150
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 67.41900
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 67.41900
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 47.16150
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 67.41900
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 67.41900
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 47.16150
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 67.41900
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 67.41900
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 47.16150
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 67.41900
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 67.41900
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 47.16150
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 67.41900
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 67.41900
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 47.16150
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 29530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 97920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 BIOMT1 2 -1.000000 0.000000 0.000000 134.83800
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 134.83800
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 134.83800
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 134.83800
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 5 -1.000000 0.000000 0.000000 134.83800
REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 6 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 6 0.000000 -1.000000 0.000000 134.83800
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 7 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 7 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 8 0.000000 -1.000000 0.000000 134.83800
REMARK 350 BIOMT2 8 -1.000000 0.000000 0.000000 134.83800
REMARK 350 BIOMT3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 134.83800
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 395 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 396 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 499 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 540 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MSE A 1
REMARK 465 ALA A 24
REMARK 465 SER A 25
REMARK 465 ASN A 26
REMARK 465 TRP A 27
REMARK 465 VAL A 150
REMARK 465 GLU A 387
REMARK 465 GLY A 388
REMARK 465 HIS A 389
REMARK 465 HIS A 390
REMARK 465 HIS A 391
REMARK 465 HIS A 392
REMARK 465 HIS A 393
REMARK 465 HIS A 394
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 SER A 2 OG
REMARK 470 GLN A 23 CG CD OE1 NE2
REMARK 470 SER A 28 OG
REMARK 470 ASP A 151 CG OD1 OD2
REMARK 470 LYS A 159 CG CD CE NZ
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 GLN A 97 11.16 -140.12
REMARK 500 TYR A 145 115.48 -164.34
REMARK 500 ALA A 152 -171.29 -69.93
REMARK 500 LYS A 183 26.33 -76.41
REMARK 500 THR A 268 160.62 74.05
REMARK 500 LYS A 280 18.98 58.96
REMARK 500 ARG A 290 -51.07 -128.63
REMARK 500 TRP A 316 69.94 -152.24
REMARK 500 LYS A 317 -124.88 -136.60
REMARK 500 THR A 318 -167.25 -111.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-9801A RELATED DB: TARGETDB
DBREF 3MKC A 1 386 UNP B6R2Z6 B6R2Z6_9RHOB 1 386
SEQADV 3MKC GLU A 387 UNP B6R2Z6 EXPRESSION TAG
SEQADV 3MKC GLY A 388 UNP B6R2Z6 EXPRESSION TAG
SEQADV 3MKC HIS A 389 UNP B6R2Z6 EXPRESSION TAG
SEQADV 3MKC HIS A 390 UNP B6R2Z6 EXPRESSION TAG
SEQADV 3MKC HIS A 391 UNP B6R2Z6 EXPRESSION TAG
SEQADV 3MKC HIS A 392 UNP B6R2Z6 EXPRESSION TAG
SEQADV 3MKC HIS A 393 UNP B6R2Z6 EXPRESSION TAG
SEQADV 3MKC HIS A 394 UNP B6R2Z6 EXPRESSION TAG
SEQRES 1 A 394 MSE SER LEU ALA LEU ASN PRO ALA VAL ALA PRO ILE LYS
SEQRES 2 A 394 SER ILE GLU PHE ILE PRO VAL ASN TYR GLN ALA SER ASN
SEQRES 3 A 394 TRP SER GLN ASN THR VAL VAL VAL LYS VAL THR ASP GLU
SEQRES 4 A 394 ASN GLY VAL TYR GLY LEU GLY GLU ALA ASP GLY SER PRO
SEQRES 5 A 394 ASP ALA ILE LEU ALA TYR ALA ASN ILE GLU THR GLU HIS
SEQRES 6 A 394 LYS TRP LEU THR ASN ILE THR GLU LYS ALA ILE GLY ARG
SEQRES 7 A 394 LEU PRO ILE GLU ILE ASN ALA ILE TRP ASP ALA MSE TYR
SEQRES 8 A 394 ASP ALA THR GLN TRP GLN GLY MSE ARG GLY LEU GLY MSE
SEQRES 9 A 394 PHE ALA LEU SER GLY ILE ASP MSE ALA LEU TYR ASP LEU
SEQRES 10 A 394 ALA GLY LYS GLN LEU GLY VAL PRO ALA TYR GLN LEU LEU
SEQRES 11 A 394 GLY GLY THR ASN LYS ASP LYS VAL HIS PRO TYR LEU THR
SEQRES 12 A 394 LEU TYR PRO ALA ILE PRO VAL ASP ALA SER LEU ASP VAL
SEQRES 13 A 394 ALA ILE LYS GLY TYR ALA PRO LEU LEU GLU LYS ALA LYS
SEQRES 14 A 394 ALA HIS ASN ILE ARG ALA VAL LYS VAL CYS VAL PRO ILE
SEQRES 15 A 394 LYS ALA ASP TRP SER THR LYS GLU VAL ALA TYR TYR LEU
SEQRES 16 A 394 ARG GLU LEU ARG GLY ILE LEU GLY HIS ASP THR ASP MSE
SEQRES 17 A 394 MSE VAL ASP TYR LEU TYR ARG PHE THR ASP TRP TYR GLU
SEQRES 18 A 394 VAL ALA ARG LEU LEU ASN SER ILE GLU ASP LEU GLU LEU
SEQRES 19 A 394 TYR PHE ALA GLU ALA THR LEU GLN HIS ASP ASP LEU SER
SEQRES 20 A 394 GLY HIS ALA LYS LEU VAL GLU ASN THR ARG SER ARG ILE
SEQRES 21 A 394 CYS GLY ALA GLU MSE SER THR THR ARG PHE GLU ALA GLU
SEQRES 22 A 394 GLU TRP ILE THR LYS GLY LYS VAL HIS LEU LEU GLN SER
SEQRES 23 A 394 ASP TYR ASN ARG CYS GLY GLY LEU THR GLU LEU ARG ARG
SEQRES 24 A 394 ILE THR GLU MSE ALA THR ALA ASN ASN VAL GLN VAL MSE
SEQRES 25 A 394 PRO HIS ASN TRP LYS THR GLY ILE THR SER ALA ALA ALA
SEQRES 26 A 394 ILE HIS TYR GLN PHE ALA VAL GLY ASN ALA PRO TYR PHE
SEQRES 27 A 394 GLU TYR VAL HIS PRO GLU PHE CYS ASP GLY GLU LEU ARG
SEQRES 28 A 394 LYS TYR LEU VAL THR PRO GLU ALA GLU LEU VAL ASP GLY
SEQRES 29 A 394 GLY PHE ALA LYS PRO THR ALA PRO GLY LEU GLY ILE ASP
SEQRES 30 A 394 LEU ASN GLN GLU PHE LEU ALA SER LEU GLU GLY HIS HIS
SEQRES 31 A 394 HIS HIS HIS HIS
MODRES 3MKC MSE A 90 MET SELENOMETHIONINE
MODRES 3MKC MSE A 99 MET SELENOMETHIONINE
MODRES 3MKC MSE A 104 MET SELENOMETHIONINE
MODRES 3MKC MSE A 112 MET SELENOMETHIONINE
MODRES 3MKC MSE A 208 MET SELENOMETHIONINE
MODRES 3MKC MSE A 209 MET SELENOMETHIONINE
MODRES 3MKC MSE A 265 MET SELENOMETHIONINE
MODRES 3MKC MSE A 303 MET SELENOMETHIONINE
MODRES 3MKC MSE A 312 MET SELENOMETHIONINE
HET MSE A 90 8
HET MSE A 99 8
HET MSE A 104 8
HET MSE A 112 8
HET MSE A 208 8
HET MSE A 209 8
HET MSE A 265 8
HET MSE A 303 8
HET MSE A 312 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 9(C5 H11 N O2 SE)
FORMUL 2 HOH *152(H2 O)
HELIX 1 1 SER A 51 ASN A 60 1 10
HELIX 2 2 GLU A 82 THR A 94 1 13
HELIX 3 3 THR A 94 MSE A 99 1 6
HELIX 4 4 GLY A 101 GLY A 123 1 23
HELIX 5 5 PRO A 125 LEU A 130 1 6
HELIX 6 6 SER A 153 HIS A 171 1 19
HELIX 7 7 SER A 187 GLY A 203 1 17
HELIX 8 8 ASP A 218 ILE A 229 1 12
HELIX 9 9 GLU A 230 GLU A 233 5 4
HELIX 10 10 ASP A 245 THR A 256 1 12
HELIX 11 11 THR A 267 LYS A 278 1 12
HELIX 12 12 GLY A 292 ASN A 307 1 16
HELIX 13 13 THR A 318 VAL A 332 1 15
HELIX 14 14 HIS A 342 CYS A 346 5 5
HELIX 15 15 GLY A 348 LEU A 354 1 7
HELIX 16 16 ASN A 379 SER A 385 1 7
SHEET 1 A 3 ILE A 12 TYR A 22 0
SHEET 2 A 3 GLN A 29 ASP A 38 -1 O VAL A 33 N ILE A 18
SHEET 3 A 3 TYR A 43 ALA A 48 -1 O GLY A 46 N VAL A 34
SHEET 1 B 2 LYS A 137 VAL A 138 0
SHEET 2 B 2 PHE A 366 ALA A 367 -1 O PHE A 366 N VAL A 138
SHEET 1 C 5 PHE A 236 GLU A 238 0
SHEET 2 C 5 ASP A 207 ASP A 211 1 N VAL A 210 O GLU A 238
SHEET 3 C 5 ALA A 175 CYS A 179 1 N VAL A 176 O MSE A 209
SHEET 4 C 5 TYR A 141 THR A 143 1 N LEU A 142 O ALA A 175
SHEET 5 C 5 GLU A 339 TYR A 340 1 O TYR A 340 N TYR A 141
SHEET 1 D 3 CYS A 261 GLY A 262 0
SHEET 2 D 3 LEU A 283 LEU A 284 1 O LEU A 283 N GLY A 262
SHEET 3 D 3 GLN A 310 VAL A 311 1 O GLN A 310 N LEU A 284
SHEET 1 E 2 VAL A 355 THR A 356 0
SHEET 2 E 2 ASP A 377 LEU A 378 -1 O ASP A 377 N THR A 356
LINK C ALA A 89 N MSE A 90 1555 1555 1.33
LINK C MSE A 90 N TYR A 91 1555 1555 1.33
LINK C GLY A 98 N MSE A 99 1555 1555 1.33
LINK C MSE A 99 N ARG A 100 1555 1555 1.33
LINK C GLY A 103 N MSE A 104 1555 1555 1.33
LINK C MSE A 104 N PHE A 105 1555 1555 1.33
LINK C ASP A 111 N MSE A 112 1555 1555 1.33
LINK C MSE A 112 N ALA A 113 1555 1555 1.33
LINK C ASP A 207 N MSE A 208 1555 1555 1.33
LINK C MSE A 208 N MSE A 209 1555 1555 1.33
LINK C MSE A 209 N VAL A 210 1555 1555 1.33
LINK C GLU A 264 N MSE A 265 1555 1555 1.33
LINK C MSE A 265 N SER A 266 1555 1555 1.33
LINK C GLU A 302 N MSE A 303 1555 1555 1.33
LINK C MSE A 303 N ALA A 304 1555 1555 1.33
LINK C VAL A 311 N MSE A 312 1555 1555 1.33
LINK C MSE A 312 N PRO A 313 1555 1555 1.34
CISPEP 1 THR A 356 PRO A 357 0 -0.25
CRYST1 134.838 134.838 94.323 90.00 90.00 90.00 I 4 2 2 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 0.007416 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007416 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010602 0.00000
(ATOM LINES ARE NOT SHOWN.)
END