HEADER OXIDOREDUCTASE 18-OCT-02 1N1P
TITLE ATOMIC RESOLUTION STRUCTURE OF CHOLESTEROL OXIDASE @ PH 7.4
TITLE 2 (STREPTOMYCES SP. SA-COO)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLESTEROL OXIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CHOD;
COMPND 5 EC: 1.1.3.6;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: FAD COFACTOR NON-COVALENTLY BOUND TO THE ENZYME
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES SP.;
SOURCE 3 ORGANISM_TAXID: 1931;
SOURCE 4 GENE: CHOA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCO202
KEYWDS FLAVOENZYME, STEROID METABOLISM, OXIDOREDUCTASE, ATOMIC RESOLUTION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.VRIELINK,P.I.LARIO
REVDAT 4 14-FEB-24 1N1P 1 REMARK LINK
REVDAT 3 13-JUL-11 1N1P 1 VERSN
REVDAT 2 24-FEB-09 1N1P 1 VERSN
REVDAT 1 28-OCT-03 1N1P 0
JRNL AUTH P.I.LARIO,A.VRIELINK
JRNL TITL ATOMIC RESOLUTION DENSITY MAPS REVEAL SECONDARY STRUCTURE
JRNL TITL 2 DEPENDENT DIFFERENCES IN ELECTRONIC DISTRIBUTION
JRNL REF J.AM.CHEM.SOC. V. 125 12787 2003
JRNL REFN ISSN 0002-7863
JRNL PMID 14558826
JRNL DOI 10.1021/JA0289954
REMARK 2
REMARK 2 RESOLUTION. 0.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.097
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.097
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.119
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 12008
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 239945
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.092
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.091
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.113
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 11055
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 221161
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3824
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 818
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 4483.3
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 3739.9
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 118
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 46576
REMARK 3 NUMBER OF RESTRAINTS : 61542
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.015
REMARK 3 ANGLE DISTANCES (A) : 0.030
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.034
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.100
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.105
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.042
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.005
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.035
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.080
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-228
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE FOLLOWING ARE RESIDUES THAT WERE NOT LOCATED IN THE EXPERIMENT:
REMARK 3 ASP A 6, ASN A 7, GLY A 8, THR A 507 (ONLY N WAS LOCATED), ALA A
REMARK 3 508, SER A 509. SOME VERY MOBILE SIDE CHAINS WERE MODELED AT
REMARK 3 EITHER 50% OR WERE NOT MODELLED. THE FOLLOWING ATOMS WERE NOT
REMARK 3 MODELLED: RES 146 CZ-> END IS MISSING.; RES 183 CD->END IS
REMARK 3 MISSING.; RES 241 NZ IS MISSING.; RES 436 CG->END IS MISSING.;
REMARK 3
REMARK 3 PARTIALLY OCCUPIED SIDE CHAIN ATOMS MODELED AT 50% FOR THE
REMARK 3 FOLLOWING: RES 73 ATOMS CD OE1 OE2;
REMARK 3
REMARK 3 RES 127 ATOMS CG 1HG 2HG CE 1HE 2HE NZ 1HZ 2HZ 3H;
REMARK 3
REMARK 3 RES 145 ATOMS CD OD1 OD2;
REMARK 3
REMARK 3 RES 146 ATOMS NE 1HE;
REMARK 3
REMARK 3 RES 156 ATOMS CD 1HD 2HD NE HE CZ NH1 1HH1 2HH1 NH2 1HH2 2HH2;
REMARK 3
REMARK 3 RES 163 ATOMS CE 1HE 2HE NZ 1HZ 2HZ 3HZ; RES 183 ATOMS CD 1HD 2HD;
REMARK 3 RES 241 ATOMS CE 1HE 2HE; RES 396 ATOMS CD 1HD 2HD NE HE CZ NH1
REMARK 3 1HH1 2HH1 NH2 1HH2 2HH2;
REMARK 4
REMARK 4 1N1P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-NOV-02.
REMARK 100 THE DEPOSITION ID IS D_1000017408.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-AUG-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : CRYST
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 277783
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.950
REMARK 200 RESOLUTION RANGE LOW (A) : 49.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 0.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.34900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO PHASING
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: 1MXT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, MANGANESE SULFATE,GLYCINE,
REMARK 280 PH 7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
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 36.48200
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: 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 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 ASP A 6
REMARK 465 ASN A 7
REMARK 465 GLY A 8
REMARK 465 ALA A 508
REMARK 465 SER A 509
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 146 CZ NH1 NH2
REMARK 470 LYS A 183 CE NZ
REMARK 470 LYS A 241 NZ
REMARK 470 GLN A 436 CG CD OE1 NE2
REMARK 470 THR A 507 CA C O CB OG1 CG2
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 71 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP A 90 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 102 CB - CG - OD1 ANGL. DEV. = -8.2 DEGREES
REMARK 500 ARG A 254 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 283 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG A 283 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 328 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 328 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ASP A 349 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 PHE A 359 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 PHE A 359 CB - CG - CD2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG A 396 NH1 - CZ - NH2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG A 396 NE - CZ - NH2 ANGL. DEV. = -8.5 DEGREES
REMARK 500 ARG A 403 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 429 NE - CZ - NH2 ANGL. DEV. = -3.3 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 THR A 18 29.32 -143.06
REMARK 500 ASN A 46 13.28 -147.11
REMARK 500 ARG A 146 -56.47 -121.80
REMARK 500 SER A 211 -73.23 -140.92
REMARK 500 VAL A 217 -55.76 -167.17
REMARK 500 THR A 231 -97.83 -109.04
REMARK 500 ASN A 353 -3.33 78.92
REMARK 500 ASP A 443 30.62 -141.52
REMARK 500 ASP A 474 -160.91 -127.37
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 MN A 513 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 159 NE2
REMARK 620 2 HOH A1091 O 79.6
REMARK 620 3 HOH A1123 O 89.8 104.7
REMARK 620 4 HOH A1306 O 106.8 84.9 162.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 514 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 223 NE2
REMARK 620 2 HOH A 941 O 89.5
REMARK 620 3 HOH A1216 O 118.3 112.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 512 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 331 NE2
REMARK 620 2 ASN A 424 O 75.2
REMARK 620 3 HOH A 686 O 82.8 102.0
REMARK 620 4 HOH A1203 O 94.3 90.2 166.2
REMARK 620 5 HOH A1303 O 98.1 169.5 85.0 82.1
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 MN A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 511
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1B4V RELATED DB: PDB
REMARK 900 NATIVE ENZYME AT 1.5 A RESOLUTION
REMARK 900 RELATED ID: 1MXT RELATED DB: PDB
REMARK 900 ATOMIC RESOLUTION @ PH 5.0
REMARK 900 RELATED ID: 1B8S RELATED DB: PDB
REMARK 900 E361Q MUTANT
REMARK 900 RELATED ID: 1CC2 RELATED DB: PDB
REMARK 900 H447Q MUTANT
REMARK 900 RELATED ID: 1IJH RELATED DB: PDB
REMARK 900 N485L MUTANT
REMARK 900 RELATED ID: 1CBO RELATED DB: PDB
REMARK 900 H447N MUTANT
REMARK 900 RELATED ID: 1N4V RELATED DB: PDB
REMARK 900 ATOMIC RESOLUTION @ PH 5.8
REMARK 900 RELATED ID: 1N4W RELATED DB: PDB
REMARK 900 ATOMIC RESOLUTION @ PH 7.3
REMARK 900 RELATED ID: 1N4U RELATED DB: PDB
REMARK 900 ATOMIC RESOLUTION @ PH 4.5
DBREF 1N1P A 6 509 UNP P12676 CHOD_STRS0 43 546
SEQRES 1 A 504 ASP ASN GLY GLY TYR VAL PRO ALA VAL VAL ILE GLY THR
SEQRES 2 A 504 GLY TYR GLY ALA ALA VAL SER ALA LEU ARG LEU GLY GLU
SEQRES 3 A 504 ALA GLY VAL GLN THR LEU MET LEU GLU MET GLY GLN LEU
SEQRES 4 A 504 TRP ASN GLN PRO GLY PRO ASP GLY ASN ILE PHE CYS GLY
SEQRES 5 A 504 MET LEU ASN PRO ASP LYS ARG SER SER TRP PHE LYS ASN
SEQRES 6 A 504 ARG THR GLU ALA PRO LEU GLY SER PHE LEU TRP LEU ASP
SEQRES 7 A 504 VAL VAL ASN ARG ASN ILE ASP PRO TYR ALA GLY VAL LEU
SEQRES 8 A 504 ASP ARG VAL ASN TYR ASP GLN MET SER VAL TYR VAL GLY
SEQRES 9 A 504 ARG GLY VAL GLY GLY GLY SER LEU VAL ASN GLY GLY MET
SEQRES 10 A 504 ALA VAL GLU PRO LYS ARG SER TYR PHE GLU GLU ILE LEU
SEQRES 11 A 504 PRO ARG VAL ASP SER SER GLU MET TYR ASP ARG TYR PHE
SEQRES 12 A 504 PRO ARG ALA ASN SER MET LEU ARG VAL ASN HIS ILE ASP
SEQRES 13 A 504 THR LYS TRP PHE GLU ASP THR GLU TRP TYR LYS PHE ALA
SEQRES 14 A 504 ARG VAL SER ARG GLU GLN ALA GLY LYS ALA GLY LEU GLY
SEQRES 15 A 504 THR VAL PHE VAL PRO ASN VAL TYR ASP PHE GLY TYR MET
SEQRES 16 A 504 GLN ARG GLU ALA ALA GLY GLU VAL PRO LYS SER ALA LEU
SEQRES 17 A 504 ALA THR GLU VAL ILE TYR GLY ASN ASN HIS GLY LYS GLN
SEQRES 18 A 504 SER LEU ASP LYS THR TYR LEU ALA ALA ALA LEU GLY THR
SEQRES 19 A 504 GLY LYS VAL THR ILE GLN THR LEU HIS GLN VAL LYS THR
SEQRES 20 A 504 ILE ARG GLN THR LYS ASP GLY GLY TYR ALA LEU THR VAL
SEQRES 21 A 504 GLU GLN LYS ASP THR ASP GLY LYS LEU LEU ALA THR LYS
SEQRES 22 A 504 GLU ILE SER CYS ARG TYR LEU PHE LEU GLY ALA GLY SER
SEQRES 23 A 504 LEU GLY SER THR GLU LEU LEU VAL ARG ALA ARG ASP THR
SEQRES 24 A 504 GLY THR LEU PRO ASN LEU ASN SER GLU VAL GLY ALA GLY
SEQRES 25 A 504 TRP GLY PRO ASN GLY ASN ILE MET THR ALA ARG ALA ASN
SEQRES 26 A 504 HIS MET TRP ASN PRO THR GLY ALA HIS GLN SER SER ILE
SEQRES 27 A 504 PRO ALA LEU GLY ILE ASP ALA TRP ASP ASN SER ASP SER
SEQRES 28 A 504 SER VAL PHE ALA GLU ILE ALA PRO MET PRO ALA GLY LEU
SEQRES 29 A 504 GLU THR TRP VAL SER LEU TYR LEU ALA ILE THR LYS ASN
SEQRES 30 A 504 PRO GLN ARG GLY THR PHE VAL TYR ASP ALA ALA THR ASP
SEQRES 31 A 504 ARG ALA LYS LEU ASN TRP THR ARG ASP GLN ASN ALA PRO
SEQRES 32 A 504 ALA VAL ASN ALA ALA LYS ALA LEU PHE ASP ARG ILE ASN
SEQRES 33 A 504 LYS ALA ASN GLY THR ILE TYR ARG TYR ASP LEU PHE GLY
SEQRES 34 A 504 THR GLN LEU LYS ALA PHE ALA ASP ASP PHE CYS TYR HIS
SEQRES 35 A 504 PRO LEU GLY GLY CYS VAL LEU GLY LYS ALA THR ASP ASP
SEQRES 36 A 504 TYR GLY ARG VAL ALA GLY TYR LYS ASN LEU TYR VAL THR
SEQRES 37 A 504 ASP GLY SER LEU ILE PRO GLY SER VAL GLY VAL ASN PRO
SEQRES 38 A 504 PHE VAL THR ILE THR ALA LEU ALA GLU ARG ASN VAL GLU
SEQRES 39 A 504 ARG ILE ILE LYS GLN ASP VAL THR ALA SER
HET MN A 512 1
HET MN A 513 1
HET MN A 514 1
HET FAD A 510 84
HET GOL A 511 6
HETNAM MN MANGANESE (II) ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 MN 3(MN 2+)
FORMUL 5 FAD C27 H33 N9 O15 P2
FORMUL 6 GOL C3 H8 O3
FORMUL 7 HOH *818(H2 O)
HELIX 1 1 GLY A 19 ALA A 32 1 14
HELIX 2 2 ASP A 62 SER A 66 5 5
HELIX 3 3 SER A 78 ASP A 83 1 6
HELIX 4 4 VAL A 84 ASN A 86 5 3
HELIX 5 5 GLY A 113 VAL A 118 5 6
HELIX 6 6 LYS A 127 LEU A 135 1 9
HELIX 7 7 ASP A 139 ARG A 146 1 8
HELIX 8 8 ARG A 146 ARG A 156 1 11
HELIX 9 9 ASP A 161 THR A 168 1 8
HELIX 10 10 TYR A 171 ALA A 184 1 14
HELIX 11 11 ASP A 196 ALA A 205 1 10
HELIX 12 12 SER A 211 THR A 215 5 5
HELIX 13 13 THR A 231 THR A 239 1 9
HELIX 14 14 ALA A 289 THR A 304 1 16
HELIX 15 15 THR A 402 GLN A 405 5 4
HELIX 16 16 ASN A 406 GLY A 425 1 20
HELIX 17 17 ASP A 474 ILE A 478 5 5
HELIX 18 18 PRO A 486 VAL A 506 1 21
SHEET 1 A 6 HIS A 248 GLN A 255 0
SHEET 2 A 6 TYR A 261 LYS A 268 -1 O GLU A 266 N GLN A 249
SHEET 3 A 6 LEU A 274 LEU A 287 -1 O LEU A 275 N GLN A 267
SHEET 4 A 6 TYR A 10 ILE A 16 1 N VAL A 14 O PHE A 286
SHEET 5 A 6 THR A 36 GLU A 40 1 O LEU A 37 N VAL A 15
SHEET 6 A 6 VAL A 242 THR A 246 1 O THR A 243 N MET A 38
SHEET 1 B 4 HIS A 248 GLN A 255 0
SHEET 2 B 4 TYR A 261 LYS A 268 -1 O GLU A 266 N GLN A 249
SHEET 3 B 4 LEU A 274 LEU A 287 -1 O LEU A 275 N GLN A 267
SHEET 4 B 4 LEU A 470 VAL A 472 1 O TYR A 471 N LEU A 287
SHEET 1 C 3 LEU A 96 ASN A 100 0
SHEET 2 C 3 SER A 105 GLY A 109 -1 O VAL A 106 N VAL A 99
SHEET 3 C 3 PHE A 444 CYS A 445 1 O CYS A 445 N SER A 105
SHEET 1 D 6 THR A 188 PHE A 190 0
SHEET 2 D 6 LEU A 346 ALA A 350 -1 O GLY A 347 N VAL A 189
SHEET 3 D 6 VAL A 358 ALA A 363 -1 O ALA A 360 N ILE A 348
SHEET 4 D 6 VAL A 373 THR A 380 -1 O ILE A 379 N PHE A 359
SHEET 5 D 6 ILE A 324 ALA A 329 -1 N ILE A 324 O ALA A 378
SHEET 6 D 6 PHE A 440 ALA A 441 -1 O ALA A 441 N MET A 325
SHEET 1 E 2 THR A 387 ASP A 391 0
SHEET 2 E 2 ARG A 396 ASN A 400 -1 O ASN A 400 N THR A 387
LINK NE2 HIS A 159 MN A MN A 513 1555 1555 2.33
LINK NE2 HIS A 223 MN A MN A 514 1555 1555 2.21
LINK NE2 HIS A 331 MN A MN A 512 1555 1555 2.33
LINK O ASN A 424 MN A MN A 512 1555 1555 2.22
LINK MN A MN A 512 O HOH A 686 1555 1555 2.17
LINK MN A MN A 512 O HOH A1203 1555 1555 2.23
LINK MN A MN A 512 O HOH A1303 1555 1555 2.04
LINK MN A MN A 513 O HOH A1091 1555 1555 2.04
LINK MN A MN A 513 O HOH A1123 1555 1555 2.46
LINK MN A MN A 513 O HOH A1306 1555 1555 2.21
LINK MN A MN A 514 O HOH A 941 1555 1555 2.40
LINK MN A MN A 514 O HOH A1216 1555 1555 2.40
SITE 1 AC1 6 HIS A 331 ASN A 424 HOH A 686 HOH A1071
SITE 2 AC1 6 HOH A1203 HOH A1303
SITE 1 AC2 5 HIS A 159 HOH A1091 HOH A1123 HOH A1306
SITE 2 AC2 5 HOH A1308
SITE 1 AC3 5 HIS A 223 HOH A 741 HOH A 941 HOH A 954
SITE 2 AC3 5 HOH A1216
SITE 1 AC4 43 ILE A 16 GLY A 17 GLY A 19 TYR A 20
SITE 2 AC4 43 GLY A 21 LEU A 39 GLU A 40 MET A 41
SITE 3 AC4 43 TYR A 107 GLY A 109 ARG A 110 GLY A 111
SITE 4 AC4 43 GLY A 114 GLY A 115 ASN A 119 GLY A 120
SITE 5 AC4 43 GLY A 121 MET A 122 ILE A 218 HIS A 248
SITE 6 AC4 43 GLN A 249 VAL A 250 GLY A 288 ALA A 289
SITE 7 AC4 43 GLY A 290 TYR A 446 HIS A 447 ASP A 474
SITE 8 AC4 43 GLY A 475 ASN A 485 PRO A 486 PHE A 487
SITE 9 AC4 43 HOH A 541 HOH A 567 HOH A 595 HOH A 601
SITE 10 AC4 43 HOH A 611 HOH A 625 HOH A 682 HOH A 697
SITE 11 AC4 43 HOH A 972 HOH A 973 HOH A1323
SITE 1 AC5 3 ILE A 244 HOH A 614 HOH A 701
CRYST1 51.273 72.964 63.036 90.00 105.18 90.00 P 1 21 1 2
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 0.019503 0.000000 0.005292 0.00000
SCALE2 0.000000 0.013705 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016438 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
