HEADER SIGNALING PROTEIN 25-JUN-10 3NOP
TITLE LIGHT-INDUCED INTERMEDIATE STRUCTURE L1 OF PSEUDOMONAS AERUGINOSA
TITLE 2 BACTERIOPHYTOCHROME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BACTERIOPHYTOCHROME;
COMPND 3 CHAIN: C;
COMPND 4 FRAGMENT: N-TERMINAL PHOTOSENSORY CORE MODULE, UNP RESIDUES 1-499;
COMPND 5 SYNONYM: PHYTOCHROME-LIKE PROTEIN;
COMPND 6 EC: 2.7.13.3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: PA01;
SOURCE 5 GENE: BPHP, PA4117;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLAMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24
KEYWDS INTERMEDIATE STRUCTURE, CHROMOPHORE BINDING POCKET, DIFFERENCE
KEYWDS 2 FOURIER METHOD, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR X.YANG,Z.REN,K.MOFFAT
REVDAT 3 06-SEP-23 3NOP 1 REMARK SEQADV LINK
REVDAT 2 08-NOV-17 3NOP 1 REMARK
REVDAT 1 07-NOV-12 3NOP 0
JRNL AUTH X.YANG,Z.REN,J.KUK,K.MOFFAT
JRNL TITL TEMPERATURE-SCAN CRYOCRYSTALLOGRAPHY REVEALS REACTION
JRNL TITL 2 INTERMEDIATES IN BACTERIOPHYTOCHROME.
JRNL REF NATURE V. 479 428 2011
JRNL REFN ISSN 0028-0836
JRNL PMID 22002602
JRNL DOI 10.1038/NATURE10506
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYNAMIX
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 131216
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : REAL SPACE CORRELATION
REMARK 3 COEFFICIENT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3817
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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 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: THIS CRYO-TRAPPED STRUCTURE WAS
REMARK 3 DETERMINED BASED ON DIFFERENCE FOURIER METHOD. THE L1 (3NOP),
REMARK 3 L2(3NOT) AND L3(3NOU) STRUCTURES WERE REFINED JOINTLY IN REAL
REMARK 3 SPACE AGAINST A SET OF (FLIGHT-FDARK) DIFFERENCE MAPS
REMARK 3 REPRESENTING MIXTURES OF THE L1, L2 AND L3 STRUCTURES IN
REMARK 3 VARIABLE RELATIVE CONCENTRATIONS USING SOFTWARE DYNAMIX. DYNAMIX
REMARK 3 IS A COLLECTION OF SOFTWARE TOOLS FOR ANALYZING DYNAMIC
REMARK 3 CRYSTALLOGRAPHIC DATA DEVELOPED BY ZHONG REN. ALGORITHMS AND
REMARK 3 METHODS ARE DESCRIBED IN REN, Z ET AL. RESOLUTION OF STRUCTURAL
REMARK 3 HETEROGENEITY IN DYNAMIC AND STATIC CRYSTALLOGRAPHY. MANUSCRIPT
REMARK 3 IN PREPARATION.
REMARK 4
REMARK 4 3NOP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000060090.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
REMARK 200 MONOCHROMATOR : C(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 131216
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 82.8
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: DIFFERENCE FOURIER METHOD
REMARK 200 SOFTWARE USED: DIFFERENCE FOURIER METHOD USING CCP4
REMARK 200 STARTING MODEL: PDB ENTRY 3NHQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10MG/ML PROTEIN, 0.1M TRIS HCL BUFFER,
REMARK 280 0.45M AMMONIUM PHOSPHATE, PH 7.7, VAPOR DIFFUSION, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 218.04900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 218.04900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 77.19000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 81.48950
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 77.19000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 81.48950
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 218.04900
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 77.19000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 81.48950
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 218.04900
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 77.19000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 81.48950
REMARK 290 SMTRY3 8 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 C 1
REMARK 465 THR C 2
REMARK 465 SER C 3
REMARK 465 PRO C 396
REMARK 465 GLN C 397
REMARK 465 PRO C 398
REMARK 465 SER C 399
REMARK 465 GLU C 400
REMARK 465 ASP C 401
REMARK 465 SER C 402
REMARK 465 PRO C 403
REMARK 465 ASP C 404
REMARK 465 GLY C 405
REMARK 465 ALA C 497
REMARK 465 LEU C 498
REMARK 465 GLU C 499
REMARK 465 HIS C 500
REMARK 465 HIS C 501
REMARK 465 HIS C 502
REMARK 465 HIS C 503
REMARK 465 HIS C 504
REMARK 465 HIS C 505
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 ILE C 4 CG1 CG2 CD1
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 C 43 1.41 -63.22
REMARK 500 GLU C 62 41.32 36.42
REMARK 500 PRO C 81 97.59 -32.43
REMARK 500 VAL C 97 78.40 -113.60
REMARK 500 LYS C 103 -121.29 60.61
REMARK 500 ARG C 166 -169.41 -72.59
REMARK 500 LEU C 235 33.44 -89.44
REMARK 500 MET C 260 117.57 -170.01
REMARK 500 ASP C 333 -6.95 78.24
REMARK 500 ARG C 367 28.64 80.42
REMARK 500 ASP C 407 -6.60 -143.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU C 62 GLN C 63 139.39
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 BLA C 900
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NHQ RELATED DB: PDB
REMARK 900 DARK-ADAPTED GROUND STATE
REMARK 900 RELATED ID: 3NOT RELATED DB: PDB
REMARK 900 LIGHT-INDUCED STRUCTURE L2
REMARK 900 RELATED ID: 3NOU RELATED DB: PDB
REMARK 900 LIGHT-INDUCED STRUCTURE L3
DBREF 3NOP C 1 499 UNP Q9HWR3 BPHY_PSEAE 1 499
SEQADV 3NOP HIS C 500 UNP Q9HWR3 EXPRESSION TAG
SEQADV 3NOP HIS C 501 UNP Q9HWR3 EXPRESSION TAG
SEQADV 3NOP HIS C 502 UNP Q9HWR3 EXPRESSION TAG
SEQADV 3NOP HIS C 503 UNP Q9HWR3 EXPRESSION TAG
SEQADV 3NOP HIS C 504 UNP Q9HWR3 EXPRESSION TAG
SEQADV 3NOP HIS C 505 UNP Q9HWR3 EXPRESSION TAG
SEQRES 1 C 505 MET THR SER ILE THR PRO VAL THR LEU ALA ASN CYS GLU
SEQRES 2 C 505 ASP GLU PRO ILE HIS VAL PRO GLY ALA ILE GLN PRO HIS
SEQRES 3 C 505 GLY ALA LEU VAL THR LEU ARG ALA ASP GLY MET VAL LEU
SEQRES 4 C 505 ALA ALA SER GLU ASN ILE GLN ALA LEU LEU GLY PHE VAL
SEQRES 5 C 505 ALA SER PRO GLY SER TYR LEU THR GLN GLU GLN VAL GLY
SEQRES 6 C 505 PRO GLU VAL LEU ARG MET LEU GLU GLU GLY LEU THR GLY
SEQRES 7 C 505 ASN GLY PRO TRP SER ASN SER VAL GLU THR ARG ILE GLY
SEQRES 8 C 505 GLU HIS LEU PHE ASP VAL ILE GLY HIS SER TYR LYS GLU
SEQRES 9 C 505 VAL PHE TYR LEU GLU PHE GLU ILE ARG THR ALA ASP THR
SEQRES 10 C 505 LEU SER ILE THR SER PHE THR LEU ASN ALA GLN ARG ILE
SEQRES 11 C 505 ILE ALA GLN VAL GLN LEU HIS ASN ASP THR ALA SER LEU
SEQRES 12 C 505 LEU SER ASN VAL THR ASP GLU LEU ARG ARG MET THR GLY
SEQRES 13 C 505 TYR ASP ARG VAL MET ALA TYR ARG PHE ARG HIS ASP ASP
SEQRES 14 C 505 SER GLY GLU VAL VAL ALA GLU SER ARG ARG GLU ASP LEU
SEQRES 15 C 505 GLU SER TYR LEU GLY GLN ARG TYR PRO ALA SER ASP ILE
SEQRES 16 C 505 PRO ALA GLN ALA ARG ARG LEU TYR ILE GLN ASN PRO ILE
SEQRES 17 C 505 ARG LEU ILE ALA ASP VAL ALA TYR THR PRO MET ARG VAL
SEQRES 18 C 505 PHE PRO ALA LEU ASN PRO GLU THR ASN GLU SER PHE ASP
SEQRES 19 C 505 LEU SER TYR SER VAL LEU ARG SER VAL SER PRO ILE HIS
SEQRES 20 C 505 CYS GLU TYR LEU THR ASN MET GLY VAL ARG ALA SER MET
SEQRES 21 C 505 SER ILE SER ILE VAL VAL GLY GLY LYS LEU TRP GLY LEU
SEQRES 22 C 505 PHE SER CYS HIS HIS MET SER PRO LYS LEU ILE PRO TYR
SEQRES 23 C 505 PRO VAL ARG MET SER PHE GLN ILE PHE SER GLN VAL CYS
SEQRES 24 C 505 SER ALA ILE VAL GLU ARG LEU GLU GLN GLY ARG ILE ALA
SEQRES 25 C 505 GLU LEU LEU ARG VAL SER THR GLU ARG ARG LEU ALA LEU
SEQRES 26 C 505 ALA ARG ARG ALA ARG ASP ALA ASP ASP LEU PHE GLY ALA
SEQRES 27 C 505 LEU ALA HIS PRO ASP ASP GLY ILE ALA ALA LEU ILE PRO
SEQRES 28 C 505 CYS ASP GLY ALA LEU VAL MET LEU GLY GLY ARG THR LEU
SEQRES 29 C 505 SER ILE ARG GLY ASP PHE GLU ARG GLN ALA GLY ASN VAL
SEQRES 30 C 505 LEU GLN ARG LEU GLN ARG ASP PRO GLU ARG ASP ILE TYR
SEQRES 31 C 505 HIS THR ASP ASN TRP PRO GLN PRO SER GLU ASP SER PRO
SEQRES 32 C 505 ASP GLY GLY ASP CYS CYS GLY VAL LEU ALA ILE ARG PHE
SEQRES 33 C 505 HIS ARG GLN GLU SER GLY TRP ILE PHE TRP PHE ARG HIS
SEQRES 34 C 505 GLU GLU VAL HIS ARG ILE ARG TRP GLY GLY LYS PRO GLU
SEQRES 35 C 505 LYS LEU LEU THR ILE GLY PRO SER GLY PRO ARG LEU THR
SEQRES 36 C 505 PRO ARG GLY SER PHE GLU ALA TRP GLU GLU VAL VAL ARG
SEQRES 37 C 505 GLY HIS SER THR PRO TRP SER GLU THR ASP LEU ALA ILE
SEQRES 38 C 505 ALA GLU LYS LEU ARG LEU ASP LEU MET GLU LEU CYS LEU
SEQRES 39 C 505 ASN HIS ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET BLA C 900 43
HETNAM BLA BILIVERDINE IX ALPHA
FORMUL 2 BLA C33 H34 N4 O6
HELIX 1 1 ASN C 11 GLU C 15 5 5
HELIX 2 2 ASN C 44 LEU C 49 1 6
HELIX 3 3 GLY C 65 THR C 77 1 13
HELIX 4 4 LEU C 118 ALA C 132 1 15
HELIX 5 5 GLN C 133 GLN C 135 5 3
HELIX 6 6 ASP C 139 GLY C 156 1 18
HELIX 7 7 PRO C 191 ILE C 195 5 5
HELIX 8 8 PRO C 196 ASN C 206 1 11
HELIX 9 9 SER C 244 GLY C 255 1 12
HELIX 10 10 PRO C 285 ASP C 333 1 49
HELIX 11 11 ASP C 334 ALA C 340 1 7
HELIX 12 12 GLY C 345 ILE C 350 1 6
HELIX 13 13 PHE C 370 LEU C 381 1 12
HELIX 14 14 GLN C 382 ASP C 384 5 3
HELIX 15 15 GLY C 451 LEU C 454 5 4
HELIX 16 16 THR C 455 ARG C 468 1 14
HELIX 17 17 SER C 475 HIS C 496 1 22
SHEET 1 A 7 ALA C 22 ILE C 23 0
SHEET 2 A 7 MET C 219 PHE C 222 -1 O MET C 219 N ILE C 23
SHEET 3 A 7 VAL C 38 SER C 42 -1 N ALA C 41 O PHE C 222
SHEET 4 A 7 GLY C 27 LEU C 32 -1 N THR C 31 O LEU C 39
SHEET 5 A 7 VAL C 105 ILE C 112 -1 O PHE C 106 N LEU C 32
SHEET 6 A 7 HIS C 93 TYR C 102 -1 N HIS C 100 O TYR C 107
SHEET 7 A 7 SER C 83 ILE C 90 -1 N THR C 88 O PHE C 95
SHEET 1 B 6 ARG C 189 TYR C 190 0
SHEET 2 B 6 GLY C 171 ARG C 178 -1 N GLY C 171 O TYR C 190
SHEET 3 B 6 ARG C 159 PHE C 165 -1 N ALA C 162 O VAL C 174
SHEET 4 B 6 LYS C 269 HIS C 278 -1 O HIS C 277 N ARG C 159
SHEET 5 B 6 ALA C 258 VAL C 266 -1 N ILE C 262 O PHE C 274
SHEET 6 B 6 ILE C 208 ILE C 211 -1 N ILE C 211 O SER C 259
SHEET 1 C 5 ARG C 362 ILE C 366 0
SHEET 2 C 5 GLY C 354 LEU C 359 -1 N VAL C 357 O LEU C 364
SHEET 3 C 5 GLY C 422 ARG C 428 -1 O TRP C 423 N MET C 358
SHEET 4 C 5 GLY C 410 HIS C 417 -1 N HIS C 417 O GLY C 422
SHEET 5 C 5 ILE C 389 THR C 392 -1 N TYR C 390 O ALA C 413
LINK SG CYS C 12 CBC BLA C 900 1555 1555 1.66
CISPEP 1 PHE C 222 PRO C 223 0 -0.43
SITE 1 AC1 15 CYS C 12 ILE C 17 TYR C 163 TYR C 185
SITE 2 AC1 15 ASP C 194 PRO C 196 TYR C 203 ARG C 209
SITE 3 AC1 15 HIS C 247 TYR C 250 MET C 254 SER C 275
SITE 4 AC1 15 HIS C 277 ARG C 453 LEU C 454
CRYST1 154.380 162.979 436.098 90.00 90.00 90.00 C 2 2 21 64
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 0.006478 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006136 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002293 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 0.950180 -0.181630 -0.253320 49.36829
MTRIX2 2 0.102240 0.949330 -0.297170 -15.39839
MTRIX3 2 0.294460 0.256470 0.920610 34.53864
MTRIX1 3 -0.606380 -0.189510 -0.772260 -2.77281
MTRIX2 3 -0.169080 -0.918250 0.358100 16.08975
MTRIX3 3 -0.776990 0.347720 0.524760 -3.47570
MTRIX1 4 -0.821800 -0.238360 -0.517520 -56.34828
MTRIX2 4 -0.179920 -0.753250 0.632640 32.87178
MTRIX3 4 -0.540620 0.613020 0.576140 -30.58517
MTRIX1 5 0.153830 0.969490 -0.190880 -88.86876
MTRIX2 5 0.971320 -0.183820 -0.150840 121.50987
MTRIX3 5 -0.181320 -0.162200 -0.969960 77.39897
MTRIX1 6 -0.278190 -0.883930 0.375880 -61.45194
MTRIX2 6 -0.672770 -0.099990 -0.733070 64.60500
MTRIX3 6 0.685560 -0.456810 -0.566860 113.99367
MTRIX1 7 0.024870 0.994750 0.099320 -77.39406
MTRIX2 7 0.994380 -0.034840 0.099990 68.65884
MTRIX3 7 0.102920 0.096270 -0.990020 109.27385
MTRIX1 8 -0.256930 -0.690270 0.676400 -49.73023
MTRIX2 8 -0.864510 -0.148690 -0.480120 8.51341
MTRIX3 8 0.431980 -0.708110 -0.558540 136.80702
(ATOM LINES ARE NOT SHOWN.)
END
