HEADER OXIDOREDUCTASE 25-FEB-17 5X7E
TITLE CRYSTAL STRUCTURE OF VITAMIN D HYDROXYLASE CYTOCHROME P450 105A1 (R84A
TITLE 2 MUTANT) IN COMPLEX WITH 1,25-DIHYDROXYVITAMIN D2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VITAMIN D3 DIHYDROXYLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYP105A1,CYTOCHROME P450-CVA1,CYTOCHROME P450-SU1,VITAMIN D3
COMPND 5 HYDROXYLASE,VD3 HYDROXYLASE;
COMPND 6 EC: 1.14.15.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES GRISEOLUS;
SOURCE 3 ORGANISM_TAXID: 1909;
SOURCE 4 ATCC: 11796;
SOURCE 5 GENE: CYP105A1, SUAC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PKK223-3
KEYWDS METAL-BINDING, MONOOXYGENASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.HAYASHI,K.YASUDA,Y.SHIRO,H.SUGIMOTO,T.SAKAKI
REVDAT 2 22-NOV-23 5X7E 1 COMPND HETNAM
REVDAT 1 10-MAY-17 5X7E 0
JRNL AUTH K.YASUDA,Y.YOGO,H.SUGIMOTO,H.MANO,T.TAKITA,M.OHTA,
JRNL AUTH 2 M.KAMAKURA,S.IKUSHIRO,K.YASUKAWA,Y.SHIRO,T.SAKAKI
JRNL TITL PRODUCTION OF AN ACTIVE FORM OF VITAMIN D2 BY GENETICALLY
JRNL TITL 2 ENGINEERED CYP105A1
JRNL REF BIOCHEM. BIOPHYS. RES. V. 486 336 2017
JRNL REF 2 COMMUN.
JRNL REFN ESSN 1090-2104
JRNL PMID 28302483
JRNL DOI 10.1016/J.BBRC.2017.03.040
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 17.53
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 29341
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1563
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1877
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.30
REMARK 3 BIN R VALUE (WORKING SET) : 0.2060
REMARK 3 BIN FREE R VALUE SET COUNT : 103
REMARK 3 BIN FREE R VALUE : 0.2740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3090
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 74
REMARK 3 SOLVENT ATOMS : 294
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.78000
REMARK 3 B22 (A**2) : -0.26000
REMARK 3 B33 (A**2) : -0.52000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.172
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.155
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.103
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.426
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
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): 3246 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4447 ; 1.679 ; 2.025
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 405 ; 5.573 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 144 ;37.357 ;23.472
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 504 ;13.543 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;17.023 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 511 ; 0.114 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2512 ; 0.009 ; 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): 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 : NULL
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 4
REMARK 4 5X7E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1300003043.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU JUPITER 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30958
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.2
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.30000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2ZBZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEGMME 20000, 0.2 M NACL, 0.1 M
REMARK 280 BISTRIS, PH 6.8, VAPOR DIFFUSION, TEMPERATURE 283K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 26.20450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.71800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.68000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.71800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.20450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.68000
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 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 THR A 2
REMARK 465 ASP A 3
REMARK 465 HIS A 408
REMARK 465 HIS A 409
REMARK 465 HIS A 410
REMARK 465 HIS A 411
REMARK 465 HIS A 412
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 NH1 ARG A 231 O HOH A 601 2.19
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 PHE A 150 -56.07 -152.79
REMARK 500 ASP A 222 -80.37 -107.56
REMARK 500 ALA A 289 64.75 31.52
REMARK 500 HIS A 344 12.47 80.11
REMARK 500 CYS A 355 118.20 -38.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 894 DISTANCE = 5.95 ANGSTROMS
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 HEM A 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 355 SG
REMARK 620 2 HEM A 501 NA 102.5
REMARK 620 3 HEM A 501 NB 89.8 88.4
REMARK 620 4 HEM A 501 NC 84.7 172.7 90.7
REMARK 620 5 HEM A 501 ND 98.2 89.5 172.0 90.3
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 HEM A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7ZU A 502
DBREF 5X7E A 1 406 UNP P18326 CPXE_STRGO 1 406
SEQADV 5X7E ALA A 84 UNP P18326 ARG 84 ENGINEERED MUTATION
SEQADV 5X7E GLN A 308 UNP P18326 HIS 308 VARIANT
SEQADV 5X7E HIS A 407 UNP P18326 EXPRESSION TAG
SEQADV 5X7E HIS A 408 UNP P18326 EXPRESSION TAG
SEQADV 5X7E HIS A 409 UNP P18326 EXPRESSION TAG
SEQADV 5X7E HIS A 410 UNP P18326 EXPRESSION TAG
SEQADV 5X7E HIS A 411 UNP P18326 EXPRESSION TAG
SEQADV 5X7E HIS A 412 UNP P18326 EXPRESSION TAG
SEQRES 1 A 412 MET THR ASP THR ALA THR THR PRO GLN THR THR ASP ALA
SEQRES 2 A 412 PRO ALA PHE PRO SER ASN ARG SER CYS PRO TYR GLN LEU
SEQRES 3 A 412 PRO ASP GLY TYR ALA GLN LEU ARG ASP THR PRO GLY PRO
SEQRES 4 A 412 LEU HIS ARG VAL THR LEU TYR ASP GLY ARG GLN ALA TRP
SEQRES 5 A 412 VAL VAL THR LYS HIS GLU ALA ALA ARG LYS LEU LEU GLY
SEQRES 6 A 412 ASP PRO ARG LEU SER SER ASN ARG THR ASP ASP ASN PHE
SEQRES 7 A 412 PRO ALA THR SER PRO ALA PHE GLU ALA VAL ARG GLU SER
SEQRES 8 A 412 PRO GLN ALA PHE ILE GLY LEU ASP PRO PRO GLU HIS GLY
SEQRES 9 A 412 THR ARG ARG ARG MET THR ILE SER GLU PHE THR VAL LYS
SEQRES 10 A 412 ARG ILE LYS GLY MET ARG PRO GLU VAL GLU GLU VAL VAL
SEQRES 11 A 412 HIS GLY PHE LEU ASP GLU MET LEU ALA ALA GLY PRO THR
SEQRES 12 A 412 ALA ASP LEU VAL SER GLN PHE ALA LEU PRO VAL PRO SER
SEQRES 13 A 412 MET VAL ILE CYS ARG LEU LEU GLY VAL PRO TYR ALA ASP
SEQRES 14 A 412 HIS GLU PHE PHE GLN ASP ALA SER LYS ARG LEU VAL GLN
SEQRES 15 A 412 SER THR ASP ALA GLN SER ALA LEU THR ALA ARG ASN ASP
SEQRES 16 A 412 LEU ALA GLY TYR LEU ASP GLY LEU ILE THR GLN PHE GLN
SEQRES 17 A 412 THR GLU PRO GLY ALA GLY LEU VAL GLY ALA LEU VAL ALA
SEQRES 18 A 412 ASP GLN LEU ALA ASN GLY GLU ILE ASP ARG GLU GLU LEU
SEQRES 19 A 412 ILE SER THR ALA MET LEU LEU LEU ILE ALA GLY HIS GLU
SEQRES 20 A 412 THR THR ALA SER MET THR SER LEU SER VAL ILE THR LEU
SEQRES 21 A 412 LEU ASP HIS PRO GLU GLN TYR ALA ALA LEU ARG ALA ASP
SEQRES 22 A 412 ARG SER LEU VAL PRO GLY ALA VAL GLU GLU LEU LEU ARG
SEQRES 23 A 412 TYR LEU ALA ILE ALA ASP ILE ALA GLY GLY ARG VAL ALA
SEQRES 24 A 412 THR ALA ASP ILE GLU VAL GLU GLY GLN LEU ILE ARG ALA
SEQRES 25 A 412 GLY GLU GLY VAL ILE VAL VAL ASN SER ILE ALA ASN ARG
SEQRES 26 A 412 ASP GLY THR VAL TYR GLU ASP PRO ASP ALA LEU ASP ILE
SEQRES 27 A 412 HIS ARG SER ALA ARG HIS HIS LEU ALA PHE GLY PHE GLY
SEQRES 28 A 412 VAL HIS GLN CYS LEU GLY GLN ASN LEU ALA ARG LEU GLU
SEQRES 29 A 412 LEU GLU VAL ILE LEU ASN ALA LEU MET ASP ARG VAL PRO
SEQRES 30 A 412 THR LEU ARG LEU ALA VAL PRO VAL GLU GLN LEU VAL LEU
SEQRES 31 A 412 ARG PRO GLY THR THR ILE GLN GLY VAL ASN GLU LEU PRO
SEQRES 32 A 412 VAL THR TRP HIS HIS HIS HIS HIS HIS
HET HEM A 501 43
HET 7ZU A 502 31
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM 7ZU (1R,3S,5Z)-5-[(2E)-2-[(1R,3AS,7AR)-1-[(E,2R,5S)-5,6-
HETNAM 2 7ZU DIMETHYL-6-OXIDANYL-HEPT-3-EN-2-YL]-7A-METHYL-2,3,3A,
HETNAM 3 7ZU 5,6,7-HEXAHYDR O-1H-INDEN-4-YLIDENE]ETHYLIDENE]-4-
HETNAM 4 7ZU METHYLIDENE-CYCLOHEXANE-1,3-DIOL
HETSYN HEM HEME
HETSYN 7ZU 1,25-DIHYDROXYVITAMIN D2
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 7ZU C28 H44 O3
FORMUL 4 HOH *294(H2 O)
HELIX 1 AA1 PRO A 27 THR A 36 1 10
HELIX 2 AA2 LYS A 56 GLY A 65 1 10
HELIX 3 AA3 SER A 82 ALA A 84 5 3
HELIX 4 AA4 PHE A 85 SER A 91 1 7
HELIX 5 AA5 ALA A 94 LEU A 98 5 5
HELIX 6 AA6 PRO A 101 ARG A 108 1 8
HELIX 7 AA7 MET A 109 PHE A 114 5 6
HELIX 8 AA8 THR A 115 GLY A 141 1 27
HELIX 9 AA9 LEU A 146 PHE A 150 1 5
HELIX 10 AB1 LEU A 152 GLY A 164 1 13
HELIX 11 AB2 PRO A 166 ALA A 168 5 3
HELIX 12 AB3 ASP A 169 SER A 183 1 15
HELIX 13 AB4 ASP A 185 GLU A 210 1 26
HELIX 14 AB5 ALA A 213 ASP A 222 1 10
HELIX 15 AB6 ASP A 230 ASP A 262 1 33
HELIX 16 AB7 HIS A 263 ASP A 273 1 11
HELIX 17 AB8 LEU A 276 ALA A 289 1 14
HELIX 18 AB9 VAL A 319 ASN A 324 1 6
HELIX 19 AC1 GLY A 357 VAL A 376 1 20
HELIX 20 AC2 PRO A 384 LEU A 388 5 5
SHEET 1 AA1 5 LEU A 40 THR A 44 0
SHEET 2 AA1 5 GLN A 50 VAL A 54 -1 O VAL A 53 N HIS A 41
SHEET 3 AA1 5 GLY A 315 VAL A 318 1 O ILE A 317 N TRP A 52
SHEET 4 AA1 5 GLY A 296 ALA A 299 -1 N ARG A 297 O VAL A 316
SHEET 5 AA1 5 LEU A 69 SER A 70 -1 N SER A 70 O VAL A 298
SHEET 1 AA2 3 ALA A 144 ASP A 145 0
SHEET 2 AA2 3 PRO A 403 THR A 405 -1 O VAL A 404 N ALA A 144
SHEET 3 AA2 3 ARG A 380 LEU A 381 -1 N ARG A 380 O THR A 405
SHEET 1 AA3 2 ILE A 303 VAL A 305 0
SHEET 2 AA3 2 GLN A 308 ILE A 310 -1 O GLN A 308 N VAL A 305
LINK SG CYS A 355 FE HEM A 501 1555 1555 2.36
CISPEP 1 PHE A 16 PRO A 17 0 -3.96
CISPEP 2 PRO A 100 PRO A 101 0 4.48
CISPEP 3 PRO A 142 THR A 143 0 -0.49
SITE 1 AC1 21 PHE A 95 ILE A 96 HIS A 103 ARG A 107
SITE 2 AC1 21 LEU A 241 ALA A 244 THR A 248 THR A 249
SITE 3 AC1 21 ALA A 294 ARG A 297 ALA A 347 PHE A 348
SITE 4 AC1 21 GLY A 349 VAL A 352 HIS A 353 CYS A 355
SITE 5 AC1 21 GLY A 357 ALA A 361 HOH A 647 HOH A 666
SITE 6 AC1 21 HOH A 693
SITE 1 AC2 10 PRO A 79 THR A 81 VAL A 88 PRO A 92
SITE 2 AC2 10 ARG A 193 ILE A 243 ILE A 293 GLY A 296
SITE 3 AC2 10 HOH A 649 HOH A 770
CRYST1 52.409 53.360 139.436 90.00 90.00 90.00 P 21 21 21 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 0.019081 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018741 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007172 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
