HEADER PHOTOSYNTHESIS 05-MAY-12 4F0U
TITLE X-RAY CRYSTAL STRUCTURE OF ALLOPHYCOCYANIN FROM SYNECHOCOCCUS
TITLE 2 ELONGATUS PCC 7942
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALLOPHYCOCYANIN ALPHA CHAIN;
COMPND 3 CHAIN: A, C, E;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: ALLOPHYCOCYANIN, BETA SUBUNIT;
COMPND 6 CHAIN: B, D, F
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS;
SOURCE 3 ORGANISM_TAXID: 1140;
SOURCE 4 STRAIN: PCC 7942;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS;
SOURCE 7 ORGANISM_TAXID: 1140;
SOURCE 8 STRAIN: PCC 7942
KEYWDS COMPONENT OF THE PHYCOBILISOME, PHOTOSYNTHETIC ANTENNA COMPLEX,
KEYWDS 2 PHOTOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MARX,N.ADIR
REVDAT 1 06-MAR-13 4F0U 0
JRNL AUTH A.MARX,N.ADIR
JRNL TITL ALLOPHYCOCYANIN AND PHYCOCYANIN CRYSTAL STRUCTURES REVEAL
JRNL TITL 2 FACETS OF PHYCOBILISOME ASSEMBLY.
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1827 311 2013
JRNL REFN ISSN 0006-3002
JRNL PMID 23201474
JRNL DOI 10.1016/J.BBABIO.2012.11.006
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
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 : 42693
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2152
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 : 7314
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 258
REMARK 3 SOLVENT ATOMS : 186
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) : 0.36
REMARK 3 ESD FROM SIGMAA (A) : 0.40
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.44
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.43
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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: NULL
REMARK 4
REMARK 4 4F0U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-12.
REMARK 100 THE RCSB ID CODE IS RCSB072312.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42702
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 48.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.45500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000; 50MM TRIS PH 8, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 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 75.57500
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 75.57500
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 49.77500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 82.66500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 49.77500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 82.66500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 75.57500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 49.77500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 82.66500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 75.57500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 49.77500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 82.66500
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 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 20350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -209.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 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 GLY F 145 N GLY F 149 2.13
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 TYR B 62 26.53 -169.98
REMARK 500 THR B 77 145.02 83.43
REMARK 500 THR D 77 142.56 65.35
REMARK 500 SER F 59 -57.36 -134.23
REMARK 500 TYR F 62 36.34 36.63
REMARK 500 THR F 77 132.18 88.74
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 CYC A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC E 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC F 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4F0T RELATED DB: PDB
DBREF 4F0U A 3 174 UNP Q31RG0 Q31RG0_SYNE7 2 161
DBREF 4F0U B 1 174 UNP Q31RG1 Q31RG1_SYNE7 1 161
DBREF 4F0U C 3 174 UNP Q31RG0 Q31RG0_SYNE7 2 161
DBREF 4F0U D 1 174 UNP Q31RG1 Q31RG1_SYNE7 1 161
DBREF 4F0U E 3 174 UNP Q31RG0 Q31RG0_SYNE7 2 161
DBREF 4F0U F 1 174 UNP Q31RG1 Q31RG1_SYNE7 1 161
SEQRES 1 A 160 SER ILE VAL SER LYS SER ILE VAL ASN ALA ASP ALA GLU
SEQRES 2 A 160 ALA ARG TYR LEU SER PRO GLY GLU LEU GLU ARG ILE LYS
SEQRES 3 A 160 THR PHE VAL VAL GLY GLY ASP ARG ARG LEU ARG ILE ALA
SEQRES 4 A 160 GLN THR ILE ALA GLU SER ARG GLU ARG ILE VAL LYS GLN
SEQRES 5 A 160 ALA GLY ASN GLN LEU PHE GLN LYS ARG PRO ASP VAL VAL
SEQRES 6 A 160 SER PRO GLY GLY ASN ALA TYR GLY GLU ASP MET THR ALA
SEQRES 7 A 160 THR CYS LEU ARG ASP LEU ASP TYR TYR LEU ARG LEU VAL
SEQRES 8 A 160 THR TYR GLY VAL VAL SER GLY ASP ILE THR PRO ILE GLU
SEQRES 9 A 160 GLU ILE GLY ILE VAL GLY VAL ARG GLU MET TYR LYS SER
SEQRES 10 A 160 LEU GLY THR PRO ILE GLU ALA VAL ALA GLU GLY VAL ARG
SEQRES 11 A 160 GLU LEU LYS SER ALA ALA THR ALA LEU LEU THR GLY GLU
SEQRES 12 A 160 ASP ALA ASP GLU ALA GLY ALA TYR PHE ASP TYR VAL ILE
SEQRES 13 A 160 GLY ALA LEU SER
SEQRES 1 B 161 MET GLN ASP ALA ILE THR ALA VAL ILE ASN ALA SER ASP
SEQRES 2 B 161 VAL GLN GLY LYS TYR LEU ASP SER SER ALA LEU ASP ARG
SEQRES 3 B 161 LEU LYS SER TYR PHE GLN SER GLY GLU LEU ARG VAL ARG
SEQRES 4 B 161 ALA ALA ALA THR ILE SER ALA ASN SER ALA LEU ILE VAL
SEQRES 5 B 161 LYS GLU ALA VAL ALA LYS SER LEU LEU TYR SER ASP ILE
SEQRES 6 B 161 THR ARG PRO GLY GLY MEN MET TYR THR THR ARG ARG TYR
SEQRES 7 B 161 ALA ALA CYS ILE ARG ASP LEU GLU TYR TYR LEU ARG TYR
SEQRES 8 B 161 ALA THR TYR ALA MET LEU ALA GLY ASP THR SER ILE LEU
SEQRES 9 B 161 ASP GLU ARG VAL LEU ASN GLY LEU LYS GLU THR TYR ASN
SEQRES 10 B 161 SER LEU GLY VAL PRO ILE GLY ALA THR VAL GLN ALA ILE
SEQRES 11 B 161 GLN ALA ILE LYS GLU VAL THR ALA SER LEU VAL GLY PRO
SEQRES 12 B 161 ASP ALA GLY ARG GLU MET GLY VAL TYR LEU ASP TYR ILE
SEQRES 13 B 161 SER SER GLY LEU SER
SEQRES 1 C 160 SER ILE VAL SER LYS SER ILE VAL ASN ALA ASP ALA GLU
SEQRES 2 C 160 ALA ARG TYR LEU SER PRO GLY GLU LEU GLU ARG ILE LYS
SEQRES 3 C 160 THR PHE VAL VAL GLY GLY ASP ARG ARG LEU ARG ILE ALA
SEQRES 4 C 160 GLN THR ILE ALA GLU SER ARG GLU ARG ILE VAL LYS GLN
SEQRES 5 C 160 ALA GLY ASN GLN LEU PHE GLN LYS ARG PRO ASP VAL VAL
SEQRES 6 C 160 SER PRO GLY GLY ASN ALA TYR GLY GLU ASP MET THR ALA
SEQRES 7 C 160 THR CYS LEU ARG ASP LEU ASP TYR TYR LEU ARG LEU VAL
SEQRES 8 C 160 THR TYR GLY VAL VAL SER GLY ASP ILE THR PRO ILE GLU
SEQRES 9 C 160 GLU ILE GLY ILE VAL GLY VAL ARG GLU MET TYR LYS SER
SEQRES 10 C 160 LEU GLY THR PRO ILE GLU ALA VAL ALA GLU GLY VAL ARG
SEQRES 11 C 160 GLU LEU LYS SER ALA ALA THR ALA LEU LEU THR GLY GLU
SEQRES 12 C 160 ASP ALA ASP GLU ALA GLY ALA TYR PHE ASP TYR VAL ILE
SEQRES 13 C 160 GLY ALA LEU SER
SEQRES 1 D 161 MET GLN ASP ALA ILE THR ALA VAL ILE ASN ALA SER ASP
SEQRES 2 D 161 VAL GLN GLY LYS TYR LEU ASP SER SER ALA LEU ASP ARG
SEQRES 3 D 161 LEU LYS SER TYR PHE GLN SER GLY GLU LEU ARG VAL ARG
SEQRES 4 D 161 ALA ALA ALA THR ILE SER ALA ASN SER ALA LEU ILE VAL
SEQRES 5 D 161 LYS GLU ALA VAL ALA LYS SER LEU LEU TYR SER ASP ILE
SEQRES 6 D 161 THR ARG PRO GLY GLY MEN MET TYR THR THR ARG ARG TYR
SEQRES 7 D 161 ALA ALA CYS ILE ARG ASP LEU GLU TYR TYR LEU ARG TYR
SEQRES 8 D 161 ALA THR TYR ALA MET LEU ALA GLY ASP THR SER ILE LEU
SEQRES 9 D 161 ASP GLU ARG VAL LEU ASN GLY LEU LYS GLU THR TYR ASN
SEQRES 10 D 161 SER LEU GLY VAL PRO ILE GLY ALA THR VAL GLN ALA ILE
SEQRES 11 D 161 GLN ALA ILE LYS GLU VAL THR ALA SER LEU VAL GLY PRO
SEQRES 12 D 161 ASP ALA GLY ARG GLU MET GLY VAL TYR LEU ASP TYR ILE
SEQRES 13 D 161 SER SER GLY LEU SER
SEQRES 1 E 160 SER ILE VAL SER LYS SER ILE VAL ASN ALA ASP ALA GLU
SEQRES 2 E 160 ALA ARG TYR LEU SER PRO GLY GLU LEU GLU ARG ILE LYS
SEQRES 3 E 160 THR PHE VAL VAL GLY GLY ASP ARG ARG LEU ARG ILE ALA
SEQRES 4 E 160 GLN THR ILE ALA GLU SER ARG GLU ARG ILE VAL LYS GLN
SEQRES 5 E 160 ALA GLY ASN GLN LEU PHE GLN LYS ARG PRO ASP VAL VAL
SEQRES 6 E 160 SER PRO GLY GLY ASN ALA TYR GLY GLU ASP MET THR ALA
SEQRES 7 E 160 THR CYS LEU ARG ASP LEU ASP TYR TYR LEU ARG LEU VAL
SEQRES 8 E 160 THR TYR GLY VAL VAL SER GLY ASP ILE THR PRO ILE GLU
SEQRES 9 E 160 GLU ILE GLY ILE VAL GLY VAL ARG GLU MET TYR LYS SER
SEQRES 10 E 160 LEU GLY THR PRO ILE GLU ALA VAL ALA GLU GLY VAL ARG
SEQRES 11 E 160 GLU LEU LYS SER ALA ALA THR ALA LEU LEU THR GLY GLU
SEQRES 12 E 160 ASP ALA ASP GLU ALA GLY ALA TYR PHE ASP TYR VAL ILE
SEQRES 13 E 160 GLY ALA LEU SER
SEQRES 1 F 161 MET GLN ASP ALA ILE THR ALA VAL ILE ASN ALA SER ASP
SEQRES 2 F 161 VAL GLN GLY LYS TYR LEU ASP SER SER ALA LEU ASP ARG
SEQRES 3 F 161 LEU LYS SER TYR PHE GLN SER GLY GLU LEU ARG VAL ARG
SEQRES 4 F 161 ALA ALA ALA THR ILE SER ALA ASN SER ALA LEU ILE VAL
SEQRES 5 F 161 LYS GLU ALA VAL ALA LYS SER LEU LEU TYR SER ASP ILE
SEQRES 6 F 161 THR ARG PRO GLY GLY MEN MET TYR THR THR ARG ARG TYR
SEQRES 7 F 161 ALA ALA CYS ILE ARG ASP LEU GLU TYR TYR LEU ARG TYR
SEQRES 8 F 161 ALA THR TYR ALA MET LEU ALA GLY ASP THR SER ILE LEU
SEQRES 9 F 161 ASP GLU ARG VAL LEU ASN GLY LEU LYS GLU THR TYR ASN
SEQRES 10 F 161 SER LEU GLY VAL PRO ILE GLY ALA THR VAL GLN ALA ILE
SEQRES 11 F 161 GLN ALA ILE LYS GLU VAL THR ALA SER LEU VAL GLY PRO
SEQRES 12 F 161 ASP ALA GLY ARG GLU MET GLY VAL TYR LEU ASP TYR ILE
SEQRES 13 F 161 SER SER GLY LEU SER
MODRES 4F0U MEN B 72 ASN N-METHYL ASPARAGINE
MODRES 4F0U MEN D 72 ASN N-METHYL ASPARAGINE
MODRES 4F0U MEN F 72 ASN N-METHYL ASPARAGINE
HET MEN B 72 9
HET MEN D 72 9
HET MEN F 72 9
HET CYC A 201 43
HET CYC B 201 43
HET CYC C 201 43
HET CYC D 201 43
HET CYC E 201 43
HET CYC F 201 43
HETNAM MEN N-METHYL ASPARAGINE
HETNAM CYC PHYCOCYANOBILIN
FORMUL 2 MEN 3(C5 H10 N2 O3)
FORMUL 7 CYC 6(C33 H40 N4 O6)
FORMUL 13 HOH *186(H2 O)
HELIX 1 1 VAL A 5 GLU A 15 1 11
HELIX 2 2 SER A 20 GLY A 33 1 14
HELIX 3 3 GLY A 33 SER A 47 1 15
HELIX 4 4 SER A 47 ARG A 63 1 17
HELIX 5 5 GLY A 77 GLY A 102 1 26
HELIX 6 6 ILE A 104 ILE A 112 1 9
HELIX 7 7 GLY A 114 GLY A 123 1 10
HELIX 8 8 PRO A 125 ALA A 142 1 18
HELIX 9 9 LEU A 143 THR A 145 5 3
HELIX 10 10 GLY A 146 SER A 174 1 19
HELIX 11 11 ASP B 3 VAL B 14 1 12
HELIX 12 12 ASP B 20 SER B 33 1 14
HELIX 13 13 SER B 33 ASN B 47 1 15
HELIX 14 14 ASN B 47 LEU B 60 1 14
HELIX 15 15 SER B 64 ARG B 68 5 5
HELIX 16 16 THR B 77 GLY B 102 1 26
HELIX 17 17 THR B 104 VAL B 111 1 8
HELIX 18 18 GLY B 114 SER B 121 1 8
HELIX 19 19 PRO B 125 GLY B 145 1 21
HELIX 20 20 GLY B 145 SER B 174 1 20
HELIX 21 21 ILE C 4 GLU C 15 1 12
HELIX 22 22 SER C 20 GLY C 33 1 14
HELIX 23 23 GLY C 33 SER C 47 1 15
HELIX 24 24 SER C 47 ARG C 63 1 17
HELIX 25 25 GLY C 77 GLY C 102 1 26
HELIX 26 26 ILE C 104 ILE C 112 1 9
HELIX 27 27 GLY C 114 GLY C 123 1 10
HELIX 28 28 PRO C 125 ALA C 142 1 18
HELIX 29 29 LEU C 143 THR C 145 5 3
HELIX 30 30 GLY C 146 LEU C 173 1 18
HELIX 31 31 ASP D 3 VAL D 14 1 12
HELIX 32 32 ASP D 20 SER D 33 1 14
HELIX 33 33 SER D 33 LYS D 58 1 26
HELIX 34 34 TYR D 76 GLY D 102 1 27
HELIX 35 35 THR D 104 VAL D 111 1 8
HELIX 36 36 GLY D 114 SER D 121 1 8
HELIX 37 37 PRO D 125 GLY D 145 1 21
HELIX 38 38 GLY D 145 GLY D 172 1 18
HELIX 39 39 ILE E 4 GLU E 15 1 12
HELIX 40 40 SER E 20 GLY E 33 1 14
HELIX 41 41 GLY E 33 SER E 47 1 15
HELIX 42 42 SER E 47 ARG E 63 1 17
HELIX 43 43 GLY E 77 GLY E 102 1 26
HELIX 44 44 ILE E 104 ILE E 112 1 9
HELIX 45 45 GLY E 114 GLY E 123 1 10
HELIX 46 46 PRO E 125 ALA E 142 1 18
HELIX 47 47 THR E 145 LEU E 173 1 19
HELIX 48 48 ASP F 3 VAL F 14 1 12
HELIX 49 49 ASP F 20 SER F 33 1 14
HELIX 50 50 SER F 33 ASN F 47 1 15
HELIX 51 51 ASN F 47 LYS F 58 1 12
HELIX 52 52 SER F 64 ARG F 68 5 5
HELIX 53 53 THR F 77 GLY F 102 1 26
HELIX 54 54 THR F 104 VAL F 111 1 8
HELIX 55 55 GLY F 114 GLY F 123 1 10
HELIX 56 56 PRO F 125 GLY F 145 1 21
HELIX 57 57 GLY F 145 GLY F 172 1 18
LINK C GLY B 71 N MEN B 72 1555 1555 1.32
LINK C MEN B 72 N MET B 75 1555 1555 1.33
LINK C GLY D 71 N MEN D 72 1555 1555 1.32
LINK C MEN D 72 N MET D 75 1555 1555 1.33
LINK C GLY F 71 N MEN F 72 1555 1555 1.33
LINK C MEN F 72 N MET F 75 1555 1555 1.33
LINK SG CYS A 84 CAC CYC A 201 1555 1555 1.82
LINK SG CYS B 84 CAC CYC B 201 1555 1555 1.81
LINK SG CYS C 84 CAC CYC C 201 1555 1555 1.92
LINK SG CYS D 84 CAC CYC D 201 1555 1555 1.83
LINK SG CYS E 84 CAC CYC E 201 1555 1555 1.81
LINK SG CYS F 84 CAC CYC F 201 1555 1555 1.82
SITE 1 AC1 23 LEU A 59 VAL A 66 ASN A 72 ALA A 75
SITE 2 AC1 23 MET A 80 THR A 83 CYS A 84 ARG A 86
SITE 3 AC1 23 ASP A 87 LEU A 88 TYR A 91 ILE A 110
SITE 4 AC1 23 GLY A 111 MET A 118 LEU A 122 THR A 124
SITE 5 AC1 23 ALA A 128 LEU F 61 TYR F 62 THR F 67
SITE 6 AC1 23 TYR F 76 THR F 77 THR F 78
SITE 1 AC2 18 ILE B 66 MEN B 72 MET B 75 ARG B 79
SITE 2 AC2 18 ARG B 80 CYS B 84 ARG B 86 ASP B 87
SITE 3 AC2 18 LEU B 88 TYR B 90 ARG B 110 VAL B 111
SITE 4 AC2 18 LEU B 122 VAL B 124 PRO B 125 ALA B 128
SITE 5 AC2 18 THR B 129 HOH B 330
SITE 1 AC3 20 THR B 67 TYR B 76 THR B 77 THR B 78
SITE 2 AC3 20 VAL C 66 ASN C 72 ALA C 75 THR C 83
SITE 3 AC3 20 CYS C 84 ARG C 86 ASP C 87 LEU C 88
SITE 4 AC3 20 TYR C 90 TYR C 91 ILE C 110 MET C 118
SITE 5 AC3 20 LEU C 122 THR C 124 ALA C 128 SER F 22
SITE 1 AC4 14 MEN D 72 MET D 75 ARG D 79 ARG D 80
SITE 2 AC4 14 CYS D 84 ARG D 86 ASP D 87 LEU D 88
SITE 3 AC4 14 TYR D 90 TYR D 94 ARG D 110 TYR D 119
SITE 4 AC4 14 THR D 129 HOH D 309
SITE 1 AC5 20 LEU D 61 TYR D 62 THR D 67 TYR D 76
SITE 2 AC5 20 THR D 77 VAL E 66 ASN E 72 ALA E 75
SITE 3 AC5 20 MET E 80 THR E 83 CYS E 84 ARG E 86
SITE 4 AC5 20 ASP E 87 LEU E 88 TYR E 90 TYR E 91
SITE 5 AC5 20 ILE E 110 MET E 118 ALA E 128 HOH E 321
SITE 1 AC6 15 LEU F 60 ILE F 66 MEN F 72 MET F 75
SITE 2 AC6 15 ARG F 80 ALA F 83 CYS F 84 ARG F 86
SITE 3 AC6 15 ASP F 87 ARG F 110 VAL F 124 PRO F 125
SITE 4 AC6 15 ALA F 128 THR F 129 HOH F 312
CRYST1 99.550 165.330 151.150 90.00 90.00 90.00 C 2 2 21 24
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 0.010045 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006049 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006616 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
