HEADER ELECTRON TRANSPORT 27-NOV-06 2JAD
TITLE YELLOW FLUORESCENT PROTEIN - GLUTAREDOXIN FUSION PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: YELLOW FLUORESCENT PROTEIN GLUTAREDOXIN FUSION PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: THE MUTATED RESIDUE NUMBER 276 CORRESPONDS TO C30S IN
COMPND 7 GLUTAREDOXIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AEQUOREA VICTORIA, SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_TAXID: 6100, 4932;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS YELLOW FLUORESCENT PROTEIN, ELECTRON TRANSPORT, REDOX- ACTIVE CENTER,
KEYWDS 2 YEAST, GRX1P, TRANSPORT, GLUTAREDOXIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.O.HAKANSSON,J.R.WINTHER
REVDAT 7 13-DEC-23 2JAD 1 REMARK LINK
REVDAT 6 17-JAN-18 2JAD 1 REMARK
REVDAT 5 15-MAR-17 2JAD 1 SOURCE
REVDAT 4 22-OCT-14 2JAD 1 REMARK VERSN HETNAM FORMUL
REVDAT 4 2 1 SHEET
REVDAT 3 24-FEB-09 2JAD 1 VERSN
REVDAT 2 13-MAR-07 2JAD 1 JRNL REMARK
REVDAT 1 20-DEC-06 2JAD 0
JRNL AUTH K.O.HAKANSSON,J.R.WINTHER
JRNL TITL STRUCTURE OF GLUTAREDOXIN GRX1P C30S MUTANT FROM YEAST.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 63 288 2007
JRNL REFN ISSN 0907-4449
JRNL PMID 17327665
JRNL DOI 10.1107/S0907444906051675
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.O.HAKANSSON,J.R.WINTHER
REMARK 1 TITL CRYSTALLISATION OF MUTANT FORMS OF GLUTAREDOXIN GRX1P FROM
REMARK 1 TITL 2 YEAST
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 62 920 2006
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 16946480
REMARK 1 DOI 10.1107/S1744309106031216
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
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) (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 15708
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 SET) : 0.214
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
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 : 2753
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 55
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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.360
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.800
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: RESIDUES 237-241 BUILT AS AAAGG AND
REMARK 3 RESIDUES 242-245 ABSENT DUE TO DISORDER. THE C-TERMINUS WAS ALSO
REMARK 3 DISORDERED
REMARK 4
REMARK 4 2JAD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-NOV-06.
REMARK 100 THE DEPOSITION ID IS D_1290030642.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-OCT-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 10.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.115
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15714
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -10.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1H6R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM BICARBONATE PH 10 1.5-1.75M
REMARK 280 MGSO4, PH 10.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 19.57400
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 39.14800
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 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 19.57400
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 39.14800
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: PQS
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 GLY A 242
REMARK 465 SER A 243
REMARK 465 GLY A 244
REMARK 465 SER A 245
REMARK 465 ALA A 355
REMARK 465 ASN A 356
REMARK 465 LEU A 357
REMARK 465 GLU A 358
REMARK 465 HIS A 359
REMARK 465 HIS A 360
REMARK 465 HIS A 361
REMARK 465 HIS A 362
REMARK 465 HIS A 363
REMARK 465 HIS A 364
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 TYR A 237 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 238 CG CD CE NZ
REMARK 470 SER A 239 OG
REMARK 470 SER A 241 CB OG
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 ASP A 103 -161.89 -165.52
REMARK 500 ILE A 136 -74.64 -74.68
REMARK 500 HIS A 148 169.99 178.25
REMARK 500 SER A 175 -156.36 -82.35
REMARK 500 PRO A 211 -9.80 -58.34
REMARK 500 HIS A 231 95.62 -62.75
REMARK 500 GLU A 285 -68.79 -100.85
REMARK 500 LYS A 288 57.82 30.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 12-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 13-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1355
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1356
DBREF 2JAD A 1 238 UNP P42212 GFP_AEQVI 1 238
DBREF 2JAD A 247 356 UNP P25373 GLRX1_YEAST 1 110
SEQADV 2JAD LEU A 68 UNP P42212 VAL 68 CONFLICT
SEQADV 2JAD HIS A 234 UNP P42212 ASP 234 CONFLICT
SEQADV 2JAD SER A 239 UNP P42212 LINKER
SEQADV 2JAD GLY A 240 UNP P42212 LINKER
SEQADV 2JAD SER A 241 UNP P42212 LINKER
SEQADV 2JAD GLY A 242 UNP P42212 LINKER
SEQADV 2JAD SER A 243 UNP P42212 LINKER
SEQADV 2JAD GLY A 244 UNP P42212 LINKER
SEQADV 2JAD SER A 245 UNP P42212 LINKER
SEQADV 2JAD GLY A 246 UNP P42212 LINKER
SEQADV 2JAD SER A 276 UNP P25373 CYS 30 ENGINEERED MUTATION
SEQADV 2JAD LEU A 357 UNP P42212 EXPRESSION TAG
SEQADV 2JAD GLU A 358 UNP P42212 EXPRESSION TAG
SEQADV 2JAD HIS A 359 UNP P42212 EXPRESSION TAG
SEQADV 2JAD HIS A 360 UNP P42212 EXPRESSION TAG
SEQADV 2JAD HIS A 361 UNP P42212 EXPRESSION TAG
SEQADV 2JAD HIS A 362 UNP P42212 EXPRESSION TAG
SEQADV 2JAD HIS A 363 UNP P42212 EXPRESSION TAG
SEQADV 2JAD HIS A 364 UNP P42212 EXPRESSION TAG
SEQRES 1 A 362 MET SER LYS GLY GLU GLU LEU PHE THR GLY VAL VAL PRO
SEQRES 2 A 362 ILE LEU VAL GLU LEU ASP GLY ASP VAL ASN GLY HIS LYS
SEQRES 3 A 362 PHE SER VAL SER GLY GLU GLY GLU GLY ASP ALA THR TYR
SEQRES 4 A 362 GLY LYS LEU THR LEU LYS PHE ILE VAL THR THR GLY LYS
SEQRES 5 A 362 LEU PRO VAL PRO TRP PRO THR LEU VAL THR THR PHE PIA
SEQRES 6 A 362 LEU GLN CYS PHE ALA ARG TYR PRO ASP HIS MET LYS ARG
SEQRES 7 A 362 HIS ASP PHE PHE LYS SER ALA MET PRO GLU GLY TYR VAL
SEQRES 8 A 362 GLN GLU ARG THR ILE PHE PHE LYS ASP ASP GLY ASN TYR
SEQRES 9 A 362 LYS THR ARG ALA GLU VAL LYS PHE GLU GLY ASP THR LEU
SEQRES 10 A 362 VAL ASN ARG ILE GLU LEU LYS GLY ILE ASP PHE LYS GLU
SEQRES 11 A 362 ASP GLY ASN ILE LEU GLY HIS LYS LEU GLU TYR ASN TYR
SEQRES 12 A 362 ASN SER HIS CYS VAL TYR ILE VAL ALA ASP LYS GLN LYS
SEQRES 13 A 362 ASN GLY ILE LYS VAL ASN PHE LYS ILE ARG HIS ASN ILE
SEQRES 14 A 362 GLU ASP GLY SER VAL GLN LEU ALA ASP HIS TYR GLN GLN
SEQRES 15 A 362 ASN THR PRO ILE GLY ASP GLY PRO VAL LEU LEU PRO ASP
SEQRES 16 A 362 ASN HIS TYR LEU CYS TYR GLN SER ALA LEU SER LYS ASP
SEQRES 17 A 362 PRO ASN GLU LYS ARG ASP HIS MET VAL LEU LEU GLU PHE
SEQRES 18 A 362 VAL THR ALA ALA GLY ILE THR HIS GLY MET HIS GLU LEU
SEQRES 19 A 362 TYR LYS SER GLY SER GLY SER GLY SER GLY MET VAL SER
SEQRES 20 A 362 GLN GLU THR ILE LYS HIS VAL LYS ASP LEU ILE ALA GLU
SEQRES 21 A 362 ASN GLU ILE PHE VAL ALA SER LYS THR TYR CYS PRO TYR
SEQRES 22 A 362 SER HIS ALA ALA LEU ASN THR LEU PHE GLU LYS LEU LYS
SEQRES 23 A 362 VAL PRO ARG SER LYS VAL LEU VAL LEU GLN LEU ASN ASP
SEQRES 24 A 362 MET LYS GLU GLY ALA ASP ILE GLN ALA ALA LEU TYR GLU
SEQRES 25 A 362 ILE ASN GLY GLN ARG THR VAL PRO ASN ILE TYR ILE ASN
SEQRES 26 A 362 GLY LYS HIS ILE GLY GLY ASN ASP ASP LEU GLN GLU LEU
SEQRES 27 A 362 ARG GLU THR GLY GLU LEU GLU GLU LEU LEU GLU PRO ILE
SEQRES 28 A 362 LEU ALA ASN LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 2JAD PIA A 66 ALA
MODRES 2JAD PIA A 66 TYR
MODRES 2JAD PIA A 66 GLY
HET PIA A 66 20
HET SO4 A1355 5
HET SO4 A1356 5
HETNAM PIA [(4Z)-2-[(1S)-1-AMINOETHYL]-4-(4-HYDROXYBENZYLIDENE)-5-
HETNAM 2 PIA OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC ACID
HETNAM SO4 SULFATE ION
FORMUL 1 PIA C14 H15 N3 O4
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 HOH *55(H2 O)
HELIX 1 1 LYS A 3 THR A 9 5 7
HELIX 2 2 PRO A 56 VAL A 61 5 6
HELIX 3 3 LEU A 68 ALA A 72 5 5
HELIX 4 4 MET A 78 HIS A 81 5 4
HELIX 5 5 ASP A 82 ALA A 87 1 6
HELIX 6 6 HIS A 231 SER A 239 1 9
HELIX 7 7 SER A 249 GLU A 262 1 14
HELIX 8 8 CYS A 273 GLU A 285 1 13
HELIX 9 9 ASN A 300 MET A 302 5 3
HELIX 10 10 GLU A 304 GLY A 317 1 14
HELIX 11 11 GLY A 333 THR A 343 1 11
HELIX 12 12 GLY A 344 LEU A 354 1 11
SHEET 1 AA13 VAL A 12 VAL A 22 0
SHEET 2 AA13 HIS A 25 ASP A 36 -1 O HIS A 25 N VAL A 22
SHEET 3 AA13 LYS A 41 VAL A 48 -1 O LYS A 41 N ASP A 36
SHEET 4 AA13 HIS A 217 ALA A 227 -1 O MET A 218 N PHE A 46
SHEET 5 AA13 HIS A 199 SER A 208 -1 O TYR A 200 N ALA A 227
SHEET 6 AA13 HIS A 148 ASP A 155 -1 O HIS A 148 N TYR A 203
SHEET 7 AA13 GLY A 160 ASN A 170 -1 O GLY A 160 N ASP A 155
SHEET 8 AA13 VAL A 176 PRO A 187 -1 O GLN A 177 N HIS A 169
SHEET 9 AA13 TYR A 92 PHE A 100 -1 O VAL A 93 N THR A 186
SHEET 10 AA13 ASN A 105 GLU A 115 -1 O TYR A 106 N ILE A 98
SHEET 11 AA13 THR A 118 ILE A 128 -1 O THR A 118 N GLU A 115
SHEET 12 AA13 VAL A 12 VAL A 22 1 O PRO A 13 N LEU A 119
SHEET 13 AA13 VAL A 12 VAL A 22 0
SHEET 1 AB 4 VAL A 294 GLN A 298 0
SHEET 2 AB 4 ILE A 265 SER A 269 1 O ILE A 265 N LEU A 295
SHEET 3 AB 4 ASN A 323 ILE A 326 -1 O ASN A 323 N ALA A 268
SHEET 4 AB 4 LYS A 329 GLY A 332 -1 O LYS A 329 N ILE A 326
SSBOND 1 CYS A 149 CYS A 202 1555 1555 2.05
LINK C PHE A 64 N1 PIA A 66 1555 1555 1.34
LINK C3 PIA A 66 N LEU A 68 1555 1555 1.34
CISPEP 1 MET A 88 PRO A 89 0 0.14
CISPEP 2 VAL A 321 PRO A 322 0 -0.08
SITE 1 AC1 4 PRO A 290 ARG A 291 HOH A2053 HOH A2054
SITE 1 AC2 3 ARG A 80 HIS A 81 HOH A2055
CRYST1 132.111 132.111 58.722 90.00 90.00 120.00 P 64 6
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 0.007569 0.004370 0.000000 0.00000
SCALE2 0.000000 0.008740 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017029 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
