HEADER TRANSFERASE 11-FEB-15 4Y5F
TITLE PAS-GAF FRAGMENT FROM DEINOCOCCUS RADIODURANS BPHP ASSEMBLED WITH BV -
TITLE 2 Y307S, HIGH DOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BACTERIOPHYTOCHROME;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PAS-GAF FRAGMENT (UNP RESIDUES 4-321);
COMPND 5 SYNONYM: PHYTOCHROME-LIKE PROTEIN;
COMPND 6 EC: 2.7.13.3;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS (STRAIN ATCC 13939 /
SOURCE 3 DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 /
SOURCE 4 VKM B-1422);
SOURCE 5 ORGANISM_TAXID: 243230;
SOURCE 6 GENE: BPHP, DR_A0050;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS HIGH-DOSE, SPECTROSCOPY, BILIN CHROMOPHORE, PHYTHOCHROME, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.LI,E.S.BURGIE,T.YU,A.HEROUX,G.C.SCHATZ,R.D.VIERSTRA,A.M.ORVILLE
REVDAT 5 27-SEP-23 4Y5F 1 COMPND HETNAM
REVDAT 4 27-NOV-19 4Y5F 1 REMARK
REVDAT 3 22-NOV-17 4Y5F 1 REMARK
REVDAT 2 06-SEP-17 4Y5F 1 SOURCE REMARK
REVDAT 1 20-MAY-15 4Y5F 0
JRNL AUTH F.LI,E.S.BURGIE,T.YU,A.HEROUX,G.C.SCHATZ,R.D.VIERSTRA,
JRNL AUTH 2 A.M.ORVILLE
JRNL TITL X-RAY RADIATION INDUCES DEPROTONATION OF THE BILIN
JRNL TITL 2 CHROMOPHORE IN CRYSTALLINE D. RADIODURANS PHYTOCHROME.
JRNL REF J.AM.CHEM.SOC. V. 137 2792 2015
JRNL REFN ESSN 1520-5126
JRNL PMID 25650486
JRNL DOI 10.1021/JA510923M
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 33245
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) : 0.146
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1761
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1929
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 76.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.1920
REMARK 3 BIN FREE R VALUE SET COUNT : 112
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2403
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 156
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.49000
REMARK 3 B22 (A**2) : 0.56000
REMARK 3 B33 (A**2) : -0.20000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.24000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.140
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.107
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.076
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.155
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2648 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2550 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3647 ; 2.043 ; 1.998
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5879 ; 1.234 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 334 ; 6.431 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 113 ;38.283 ;23.717
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 406 ;13.950 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;19.197 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 423 ; 0.127 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2997 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 586 ; 0.004 ; 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): 1296 ; 4.976 ; 2.676
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1295 ; 4.950 ; 2.672
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1624 ; 5.801 ; 4.027
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1625 ; 5.807 ; 4.030
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1352 ; 6.187 ; 2.968
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1353 ; 6.186 ; 2.968
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2018 ; 6.917 ; 4.359
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2971 ; 6.691 ;22.267
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2972 ; 6.691 ;22.270
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 5198 ; 6.052 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 48 ;21.846 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 5228 ;13.881 ; 5.000
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 ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4Y5F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000206855.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-AUG-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33245
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
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 (%) : 96.2
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.45900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2O9C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG3350, 19% ISOPROPANOL, 5%
REMARK 280 GLYCEROL, 100 MM CITRIC ACID/NAOH, PH 5.6, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 296K
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 44.63700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.90150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 44.63700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.90150
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 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 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 507 LIES ON A SPECIAL POSITION.
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 ASP A 4 CG OD1 OD2
REMARK 470 ARG A 70 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 193 CG CD OE1 OE2
REMARK 470 HIS A 196 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 310 CG CD NE CZ NH1 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 O ASP A 133 OD2 ASP A 300 2.15
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 PHE A 9 CB - CA - C ANGL. DEV. = -12.2 DEGREES
REMARK 500 ARG A 165 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 191 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG A 191 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ASP A 300 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 300 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
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 LBV A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4Y3I RELATED DB: PDB
REMARK 900 PAS-GAF FRAGMENT FROM DEINOCOCCUS RADIODURANS BPHP, LOW-DOSE (LESS
REMARK 900 THAN 15 KGY) COLLECTION
DBREF 4Y5F A 4 321 UNP Q9RZA4 BPHY_DEIRA 4 321
SEQADV 4Y5F SER A 307 UNP Q9RZA4 TYR 307 ENGINEERED MUTATION
SEQADV 4Y5F HIS A 322 UNP Q9RZA4 EXPRESSION TAG
SEQRES 1 A 319 ASP PRO LEU PRO PHE PHE PRO PRO LEU TYR LEU GLY GLY
SEQRES 2 A 319 PRO GLU ILE THR THR GLU ASN CYS GLU ARG GLU PRO ILE
SEQRES 3 A 319 HIS ILE PRO GLY SER ILE GLN PRO HIS GLY ALA LEU LEU
SEQRES 4 A 319 THR ALA ASP GLY HIS SER GLY GLU VAL LEU GLN MET SER
SEQRES 5 A 319 LEU ASN ALA ALA THR PHE LEU GLY GLN GLU PRO THR VAL
SEQRES 6 A 319 LEU ARG GLY GLN THR LEU ALA ALA LEU LEU PRO GLU GLN
SEQRES 7 A 319 TRP PRO ALA LEU GLN ALA ALA LEU PRO PRO GLY CYS PRO
SEQRES 8 A 319 ASP ALA LEU GLN TYR ARG ALA THR LEU ASP TRP PRO ALA
SEQRES 9 A 319 ALA GLY HIS LEU SER LEU THR VAL HIS ARG VAL GLY GLU
SEQRES 10 A 319 LEU LEU ILE LEU GLU PHE GLU PRO THR GLU ALA TRP ASP
SEQRES 11 A 319 SER THR GLY PRO HIS ALA LEU ARG ASN ALA MET PHE ALA
SEQRES 12 A 319 LEU GLU SER ALA PRO ASN LEU ARG ALA LEU ALA GLU VAL
SEQRES 13 A 319 ALA THR GLN THR VAL ARG GLU LEU THR GLY PHE ASP ARG
SEQRES 14 A 319 VAL MET LEU TYR LYS PHE ALA PRO ASP ALA THR GLY GLU
SEQRES 15 A 319 VAL ILE ALA GLU ALA ARG ARG GLU GLY LEU HIS ALA PHE
SEQRES 16 A 319 LEU GLY HIS ARG PHE PRO ALA SER ASP ILE PRO ALA GLN
SEQRES 17 A 319 ALA ARG ALA LEU TYR THR ARG HIS LEU LEU ARG LEU THR
SEQRES 18 A 319 ALA ASP THR ARG ALA ALA ALA VAL PRO LEU ASP PRO VAL
SEQRES 19 A 319 LEU ASN PRO GLN THR ASN ALA PRO THR PRO LEU GLY GLY
SEQRES 20 A 319 ALA VAL LEU ARG ALA THR SER PRO MET HIS MET GLN TYR
SEQRES 21 A 319 LEU ARG ASN MET GLY VAL GLY SER SER LEU SER VAL SER
SEQRES 22 A 319 VAL VAL VAL GLY GLY GLN LEU TRP GLY LEU ILE ALA CYS
SEQRES 23 A 319 HIS HIS GLN THR PRO TYR VAL LEU PRO PRO ASP LEU ARG
SEQRES 24 A 319 THR THR LEU GLU SER LEU GLY ARG LEU LEU SER LEU GLN
SEQRES 25 A 319 VAL GLN VAL LYS GLU ALA HIS
HET LBV A 401 43
HETNAM LBV 3-[2-[(Z)-[3-(2-CARBOXYETHYL)-5-[(Z)-(4-ETHENYL-3-
HETNAM 2 LBV METHYL-5-OXIDANYLIDENE-PYRROL-2-YLIDENE)METHYL]-4-
HETNAM 3 LBV METHYL-PYRROL-1-IUM -2-YLIDENE]METHYL]-5-[(Z)-[(3E)-3-
HETNAM 4 LBV ETHYLIDENE-4-METHYL-5-OXIDANYLIDENE-PYRROLIDIN-2-
HETNAM 5 LBV YLIDENE]METHYL]-4-METHYL-1H-PYRROL-3- YL]PROPANOIC
HETNAM 6 LBV ACID
HETSYN LBV 2(R),3(E)- PHYTOCHROMOBILIN
FORMUL 2 LBV C33 H37 N4 O6 1+
FORMUL 3 HOH *156(H2 O)
HELIX 1 AA1 PRO A 11 GLY A 15 5 5
HELIX 2 AA2 ASN A 23 GLU A 27 5 5
HELIX 3 AA3 ASN A 57 GLY A 63 1 7
HELIX 4 AA4 GLU A 65 ARG A 70 1 6
HELIX 5 AA5 THR A 73 LEU A 78 1 6
HELIX 6 AA6 GLN A 81 LEU A 89 1 9
HELIX 7 AA7 GLU A 130 SER A 134 5 5
HELIX 8 AA8 PRO A 137 ALA A 150 1 14
HELIX 9 AA9 ASN A 152 GLY A 169 1 18
HELIX 10 AB1 PRO A 204 ILE A 208 5 5
HELIX 11 AB2 PRO A 209 HIS A 219 1 11
HELIX 12 AB3 SER A 257 MET A 267 1 11
HELIX 13 AB4 PRO A 298 ALA A 321 1 24
SHEET 1 AA1 7 SER A 34 ILE A 35 0
SHEET 2 AA1 7 VAL A 232 ASP A 235 -1 O VAL A 232 N ILE A 35
SHEET 3 AA1 7 VAL A 51 SER A 55 -1 N MET A 54 O ASP A 235
SHEET 4 AA1 7 ALA A 40 ASP A 45 -1 N LEU A 41 O SER A 55
SHEET 5 AA1 7 LEU A 121 THR A 129 -1 O LEU A 124 N LEU A 42
SHEET 6 AA1 7 HIS A 110 VAL A 118 -1 N HIS A 110 O THR A 129
SHEET 7 AA1 7 TYR A 99 LEU A 103 -1 N LEU A 103 O LEU A 111
SHEET 1 AA2 6 ARG A 202 PHE A 203 0
SHEET 2 AA2 6 GLY A 184 ARG A 191 -1 N GLY A 184 O PHE A 203
SHEET 3 AA2 6 ARG A 172 PHE A 178 -1 N VAL A 173 O ALA A 190
SHEET 4 AA2 6 GLN A 282 HIS A 291 -1 O LEU A 286 N TYR A 176
SHEET 5 AA2 6 SER A 271 VAL A 279 -1 N LEU A 273 O CYS A 289
SHEET 6 AA2 6 LEU A 221 THR A 224 -1 N THR A 224 O SER A 272
LINK SG CYS A 24 CBA LBV A 401 1555 1555 1.64
CISPEP 1 ASP A 235 PRO A 236 0 -10.47
SITE 1 AC1 25 CYS A 24 MET A 174 TYR A 176 PHE A 203
SITE 2 AC1 25 SER A 206 ASP A 207 ILE A 208 PRO A 209
SITE 3 AC1 25 TYR A 216 ARG A 254 THR A 256 SER A 257
SITE 4 AC1 25 MET A 259 HIS A 260 TYR A 263 MET A 267
SITE 5 AC1 25 SER A 272 SER A 274 HIS A 290 HOH A 549
SITE 6 AC1 25 HOH A 554 HOH A 557 HOH A 562 HOH A 564
SITE 7 AC1 25 HOH A 629
CRYST1 89.274 51.803 80.272 90.00 116.22 90.00 C 1 2 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 0.011201 0.000000 0.005517 0.00000
SCALE2 0.000000 0.019304 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013887 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
