HEADER OXIDOREDUCTASE 24-FEB-09 3GDO
TITLE CRYSTAL STRUCTURE OF PUTATIVE OXIDOREDUCTASE YVAA FROM BACILLUS
TITLE 2 SUBTILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED OXIDOREDUCTASE YVAA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 12-358;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 224308;
SOURCE 4 STRAIN: 168;
SOURCE 5 GENE: BSU33530, YVAA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: BC-PSGX4(BC)
KEYWDS STRUCTURAL GENOMICS, PUTATIVE OXIDOREDUCTASE YVAA, OXIDOREDUCTASE,
KEYWDS 2 PSI-2, PROTEIN STRUCTURE INITIATIVE, NEW YORK SGX RESEARCH CENTER
KEYWDS 3 FOR STRUCTURAL GENOMICS, NYSGXRC
EXPDTA X-RAY DIFFRACTION
AUTHOR U.A.RAMAGOPAL,R.TORO,S.K.BURLEY,S.C.ALMO,NEW YORK SGX RESEARCH CENTER
AUTHOR 2 FOR STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 5 21-FEB-24 3GDO 1 REMARK
REVDAT 4 10-FEB-21 3GDO 1 AUTHOR JRNL SEQADV
REVDAT 3 01-NOV-17 3GDO 1 REMARK
REVDAT 2 13-JUL-11 3GDO 1 VERSN
REVDAT 1 24-MAR-09 3GDO 0
JRNL AUTH U.A.RAMAGOPAL,R.TORO,S.K.BURLEY,S.C.ALMO
JRNL TITL STRUCTURE OF PUTATIVE OXIDOREDUCTASE YVAA FROM BACILLUS
JRNL TITL 2 SUBTILIS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.03 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.03
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 49797
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2533
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) : 2.03
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.09
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3016
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.23
REMARK 3 BIN R VALUE (WORKING SET) : 0.2810
REMARK 3 BIN FREE R VALUE SET COUNT : 164
REMARK 3 BIN FREE R VALUE : 0.3100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5285
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 124
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.87000
REMARK 3 B22 (A**2) : -1.03000
REMARK 3 B33 (A**2) : 1.70000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.02000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.197
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.176
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.132
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.835
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5448 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7387 ; 1.515 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 689 ; 6.196 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 248 ;39.259 ;24.435
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 965 ;16.011 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;18.280 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 835 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4099 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 3380 ; 0.909 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5469 ; 1.630 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2068 ; 2.499 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1911 ; 4.030 ; 4.500
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 : 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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. U VALUES: REFINED INDIVIDUALLY.
REMARK 4
REMARK 4 3GDO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-FEB-09.
REMARK 100 THE DEPOSITION ID IS D_1000051730.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-NOV-08
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 : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49833
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.030
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : 0.07800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.1310
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.45900
REMARK 200 R SYM FOR SHELL (I) : 0.36200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD, PHENIX, CCP4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH 8.5, 25% PEG 3350,
REMARK 280 0.2M MGCL2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K, PH
REMARK 280 6.5
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 75.65450
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: 3040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.6 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 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 9
REMARK 465 GLN A 169
REMARK 465 ALA A 170
REMARK 465 ARG A 171
REMARK 465 TRP A 172
REMARK 465 ARG A 173
REMARK 465 GLU A 174
REMARK 465 LYS A 175
REMARK 465 GLU A 176
REMARK 465 GLY A 177
REMARK 465 THR A 178
REMARK 465 HIS A 358
REMARK 465 GLU A 359
REMARK 465 GLY A 360
REMARK 465 HIS A 361
REMARK 465 HIS A 362
REMARK 465 HIS A 363
REMARK 465 HIS A 364
REMARK 465 HIS A 365
REMARK 465 HIS A 366
REMARK 465 MET B 9
REMARK 465 ALA B 170
REMARK 465 ARG B 171
REMARK 465 TRP B 172
REMARK 465 ARG B 173
REMARK 465 GLU B 174
REMARK 465 LYS B 175
REMARK 465 GLU B 176
REMARK 465 GLY B 177
REMARK 465 THR B 178
REMARK 465 HIS B 358
REMARK 465 GLU B 359
REMARK 465 GLY B 360
REMARK 465 HIS B 361
REMARK 465 HIS B 362
REMARK 465 HIS B 363
REMARK 465 HIS B 364
REMARK 465 HIS B 365
REMARK 465 HIS B 366
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 ARG A 294 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 169 CG CD OE1 NE2
REMARK 470 ARG B 294 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 357 CG CD OE1 OE2
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 OE1 GLU A 114 NH1 ARG A 339 2.12
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 GLU A 275 -34.42 -134.17
REMARK 500 LEU B 151 59.56 -146.23
REMARK 500 GLU B 275 -14.87 -140.61
REMARK 500 ALA B 325 150.64 -48.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-11137J RELATED DB: TARGETDB
REMARK 900 RELATED ID: 3GFG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PUTATIVE OXIDOREDUCTASE YVAA FROM BACILLUS
REMARK 900 SUBTILIS, TRICLINIC FORM
DBREF 3GDO A 12 358 UNP O32223 YVAA_BACSU 12 358
DBREF 3GDO B 12 358 UNP O32223 YVAA_BACSU 12 358
SEQADV 3GDO MET A 9 UNP O32223 EXPRESSION TAG
SEQADV 3GDO SER A 10 UNP O32223 EXPRESSION TAG
SEQADV 3GDO LEU A 11 UNP O32223 EXPRESSION TAG
SEQADV 3GDO GLU A 359 UNP O32223 EXPRESSION TAG
SEQADV 3GDO GLY A 360 UNP O32223 EXPRESSION TAG
SEQADV 3GDO HIS A 361 UNP O32223 EXPRESSION TAG
SEQADV 3GDO HIS A 362 UNP O32223 EXPRESSION TAG
SEQADV 3GDO HIS A 363 UNP O32223 EXPRESSION TAG
SEQADV 3GDO HIS A 364 UNP O32223 EXPRESSION TAG
SEQADV 3GDO HIS A 365 UNP O32223 EXPRESSION TAG
SEQADV 3GDO HIS A 366 UNP O32223 EXPRESSION TAG
SEQADV 3GDO MET B 9 UNP O32223 EXPRESSION TAG
SEQADV 3GDO SER B 10 UNP O32223 EXPRESSION TAG
SEQADV 3GDO LEU B 11 UNP O32223 EXPRESSION TAG
SEQADV 3GDO GLU B 359 UNP O32223 EXPRESSION TAG
SEQADV 3GDO GLY B 360 UNP O32223 EXPRESSION TAG
SEQADV 3GDO HIS B 361 UNP O32223 EXPRESSION TAG
SEQADV 3GDO HIS B 362 UNP O32223 EXPRESSION TAG
SEQADV 3GDO HIS B 363 UNP O32223 EXPRESSION TAG
SEQADV 3GDO HIS B 364 UNP O32223 EXPRESSION TAG
SEQADV 3GDO HIS B 365 UNP O32223 EXPRESSION TAG
SEQADV 3GDO HIS B 366 UNP O32223 EXPRESSION TAG
SEQRES 1 A 358 MET SER LEU ASP THR ILE LYS VAL GLY ILE LEU GLY TYR
SEQRES 2 A 358 GLY LEU SER GLY SER VAL PHE HIS GLY PRO LEU LEU ASP
SEQRES 3 A 358 VAL LEU ASP GLU TYR GLN ILE SER LYS ILE MET THR SER
SEQRES 4 A 358 ARG THR GLU GLU VAL LYS ARG ASP PHE PRO ASP ALA GLU
SEQRES 5 A 358 VAL VAL HIS GLU LEU GLU GLU ILE THR ASN ASP PRO ALA
SEQRES 6 A 358 ILE GLU LEU VAL ILE VAL THR THR PRO SER GLY LEU HIS
SEQRES 7 A 358 TYR GLU HIS THR MET ALA CYS ILE GLN ALA GLY LYS HIS
SEQRES 8 A 358 VAL VAL MET GLU LYS PRO MET THR ALA THR ALA GLU GLU
SEQRES 9 A 358 GLY GLU THR LEU LYS ARG ALA ALA ASP GLU LYS GLY VAL
SEQRES 10 A 358 LEU LEU SER VAL TYR HIS ASN ARG ARG TRP ASP ASN ASP
SEQRES 11 A 358 PHE LEU THR ILE LYS LYS LEU ILE SER GLU GLY SER LEU
SEQRES 12 A 358 GLU ASP ILE ASN THR TYR GLN VAL SER TYR ASN ARG TYR
SEQRES 13 A 358 ARG PRO GLU VAL GLN ALA ARG TRP ARG GLU LYS GLU GLY
SEQRES 14 A 358 THR ALA THR GLY THR LEU TYR ASP LEU GLY SER HIS ILE
SEQRES 15 A 358 ILE ASP GLN THR LEU HIS LEU PHE GLY MET PRO LYS ALA
SEQRES 16 A 358 VAL THR ALA ASN VAL MET ALA GLN ARG GLU ASN ALA GLU
SEQRES 17 A 358 THR VAL ASP TYR PHE HIS LEU THR LEU ASP TYR GLY LYS
SEQRES 18 A 358 LEU GLN ALA ILE LEU TYR GLY GLY SER ILE VAL PRO ALA
SEQRES 19 A 358 ASN GLY PRO ARG TYR GLN ILE HIS GLY LYS ASP SER SER
SEQRES 20 A 358 PHE ILE LYS TYR GLY ILE ASP GLY GLN GLU ASP ALA LEU
SEQRES 21 A 358 ARG ALA GLY ARG LYS PRO GLU ASP ASP SER TRP GLY ALA
SEQRES 22 A 358 ASP VAL PRO GLU PHE TYR GLY LYS LEU THR THR ILE ARG
SEQRES 23 A 358 GLY SER ASP LYS LYS THR GLU THR ILE PRO SER VAL ASN
SEQRES 24 A 358 GLY SER TYR LEU THR TYR TYR ARG LYS ILE ALA GLU SER
SEQRES 25 A 358 ILE ARG GLU GLY ALA ALA LEU PRO VAL THR ALA GLU GLU
SEQRES 26 A 358 GLY ILE ASN VAL ILE ARG ILE ILE GLU ALA ALA MET GLU
SEQRES 27 A 358 SER SER LYS GLU LYS ARG THR ILE MET LEU GLU HIS GLU
SEQRES 28 A 358 GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 B 358 MET SER LEU ASP THR ILE LYS VAL GLY ILE LEU GLY TYR
SEQRES 2 B 358 GLY LEU SER GLY SER VAL PHE HIS GLY PRO LEU LEU ASP
SEQRES 3 B 358 VAL LEU ASP GLU TYR GLN ILE SER LYS ILE MET THR SER
SEQRES 4 B 358 ARG THR GLU GLU VAL LYS ARG ASP PHE PRO ASP ALA GLU
SEQRES 5 B 358 VAL VAL HIS GLU LEU GLU GLU ILE THR ASN ASP PRO ALA
SEQRES 6 B 358 ILE GLU LEU VAL ILE VAL THR THR PRO SER GLY LEU HIS
SEQRES 7 B 358 TYR GLU HIS THR MET ALA CYS ILE GLN ALA GLY LYS HIS
SEQRES 8 B 358 VAL VAL MET GLU LYS PRO MET THR ALA THR ALA GLU GLU
SEQRES 9 B 358 GLY GLU THR LEU LYS ARG ALA ALA ASP GLU LYS GLY VAL
SEQRES 10 B 358 LEU LEU SER VAL TYR HIS ASN ARG ARG TRP ASP ASN ASP
SEQRES 11 B 358 PHE LEU THR ILE LYS LYS LEU ILE SER GLU GLY SER LEU
SEQRES 12 B 358 GLU ASP ILE ASN THR TYR GLN VAL SER TYR ASN ARG TYR
SEQRES 13 B 358 ARG PRO GLU VAL GLN ALA ARG TRP ARG GLU LYS GLU GLY
SEQRES 14 B 358 THR ALA THR GLY THR LEU TYR ASP LEU GLY SER HIS ILE
SEQRES 15 B 358 ILE ASP GLN THR LEU HIS LEU PHE GLY MET PRO LYS ALA
SEQRES 16 B 358 VAL THR ALA ASN VAL MET ALA GLN ARG GLU ASN ALA GLU
SEQRES 17 B 358 THR VAL ASP TYR PHE HIS LEU THR LEU ASP TYR GLY LYS
SEQRES 18 B 358 LEU GLN ALA ILE LEU TYR GLY GLY SER ILE VAL PRO ALA
SEQRES 19 B 358 ASN GLY PRO ARG TYR GLN ILE HIS GLY LYS ASP SER SER
SEQRES 20 B 358 PHE ILE LYS TYR GLY ILE ASP GLY GLN GLU ASP ALA LEU
SEQRES 21 B 358 ARG ALA GLY ARG LYS PRO GLU ASP ASP SER TRP GLY ALA
SEQRES 22 B 358 ASP VAL PRO GLU PHE TYR GLY LYS LEU THR THR ILE ARG
SEQRES 23 B 358 GLY SER ASP LYS LYS THR GLU THR ILE PRO SER VAL ASN
SEQRES 24 B 358 GLY SER TYR LEU THR TYR TYR ARG LYS ILE ALA GLU SER
SEQRES 25 B 358 ILE ARG GLU GLY ALA ALA LEU PRO VAL THR ALA GLU GLU
SEQRES 26 B 358 GLY ILE ASN VAL ILE ARG ILE ILE GLU ALA ALA MET GLU
SEQRES 27 B 358 SER SER LYS GLU LYS ARG THR ILE MET LEU GLU HIS GLU
SEQRES 28 B 358 GLY HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *124(H2 O)
HELIX 1 1 GLY A 22 PHE A 28 1 7
HELIX 2 2 HIS A 29 ASP A 34 1 6
HELIX 3 3 ARG A 48 PHE A 56 1 9
HELIX 4 4 LEU A 65 ASN A 70 1 6
HELIX 5 5 LEU A 85 ALA A 96 1 12
HELIX 6 6 THR A 109 GLY A 124 1 16
HELIX 7 7 HIS A 131 TRP A 135 5 5
HELIX 8 8 ASP A 136 GLU A 148 1 13
HELIX 9 9 GLY A 181 LEU A 186 1 6
HELIX 10 10 LEU A 186 GLY A 199 1 14
HELIX 11 11 GLY A 263 ALA A 270 1 8
HELIX 12 12 VAL A 283 TYR A 287 5 5
HELIX 13 13 TYR A 310 GLY A 324 1 15
HELIX 14 14 THR A 330 LYS A 351 1 22
HELIX 15 15 GLY B 22 PHE B 28 1 7
HELIX 16 16 HIS B 29 VAL B 35 1 7
HELIX 17 17 ARG B 48 PHE B 56 1 9
HELIX 18 18 LEU B 65 ASN B 70 1 6
HELIX 19 19 LEU B 85 ALA B 96 1 12
HELIX 20 20 THR B 109 GLY B 124 1 16
HELIX 21 21 HIS B 131 TRP B 135 5 5
HELIX 22 22 ASP B 136 GLU B 148 1 13
HELIX 23 23 GLY B 181 LEU B 186 1 6
HELIX 24 24 LEU B 186 GLY B 199 1 14
HELIX 25 25 GLY B 263 ALA B 270 1 8
HELIX 26 26 VAL B 283 TYR B 287 5 5
HELIX 27 27 TYR B 310 GLY B 324 1 15
HELIX 28 28 THR B 330 LYS B 351 1 22
SHEET 1 A 6 GLU A 60 VAL A 62 0
SHEET 2 A 6 TYR A 39 MET A 45 1 N SER A 42 O GLU A 60
SHEET 3 A 6 ILE A 14 LEU A 19 1 N ILE A 14 O GLN A 40
SHEET 4 A 6 LEU A 76 VAL A 79 1 O ILE A 78 N LEU A 19
SHEET 5 A 6 HIS A 99 GLU A 103 1 O VAL A 101 N VAL A 79
SHEET 6 A 6 LEU A 127 TYR A 130 1 O TYR A 130 N MET A 102
SHEET 1 B 9 ASP A 297 ILE A 303 0
SHEET 2 B 9 GLY A 288 ARG A 294 -1 N ARG A 294 O ASP A 297
SHEET 3 B 9 SER A 254 LYS A 258 -1 N SER A 255 O THR A 291
SHEET 4 B 9 TYR A 247 HIS A 250 -1 N TYR A 247 O LYS A 258
SHEET 5 B 9 THR A 156 SER A 160 -1 N GLN A 158 O GLN A 248
SHEET 6 B 9 LEU A 230 GLY A 236 1 O ILE A 233 N VAL A 159
SHEET 7 B 9 TYR A 220 TYR A 227 -1 N LEU A 223 O LEU A 234
SHEET 8 B 9 ALA A 203 MET A 209 -1 N ALA A 203 O ASP A 226
SHEET 9 B 9 ILE A 354 MET A 355 -1 O ILE A 354 N VAL A 204
SHEET 1 C 6 GLU B 60 VAL B 62 0
SHEET 2 C 6 TYR B 39 MET B 45 1 N SER B 42 O GLU B 60
SHEET 3 C 6 ILE B 14 LEU B 19 1 N VAL B 16 O GLN B 40
SHEET 4 C 6 LEU B 76 VAL B 79 1 O ILE B 78 N LEU B 19
SHEET 5 C 6 HIS B 99 GLU B 103 1 O VAL B 101 N VAL B 79
SHEET 6 C 6 LEU B 127 TYR B 130 1 O TYR B 130 N MET B 102
SHEET 1 D 9 ASP B 297 ILE B 303 0
SHEET 2 D 9 GLY B 288 ARG B 294 -1 N LEU B 290 O GLU B 301
SHEET 3 D 9 SER B 254 LYS B 258 -1 N SER B 255 O THR B 291
SHEET 4 D 9 TYR B 247 GLY B 251 -1 N GLY B 251 O SER B 254
SHEET 5 D 9 ILE B 154 SER B 160 -1 N ASN B 155 O HIS B 250
SHEET 6 D 9 LEU B 230 GLY B 236 1 O ILE B 233 N TYR B 157
SHEET 7 D 9 TYR B 220 TYR B 227 -1 N LEU B 223 O LEU B 234
SHEET 8 D 9 ALA B 203 MET B 209 -1 N THR B 205 O THR B 224
SHEET 9 D 9 ILE B 354 MET B 355 -1 O ILE B 354 N VAL B 204
CISPEP 1 LYS A 104 PRO A 105 0 -5.11
CISPEP 2 LYS B 104 PRO B 105 0 -11.88
CRYST1 49.324 151.309 56.395 90.00 107.14 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 0.020274 0.000000 0.006252 0.00000
SCALE2 0.000000 0.006609 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018556 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
