HEADER BINDING PROTEIN 17-APR-98 1A99
TITLE PUTRESCINE RECEPTOR (POTF) FROM E. COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTRESCINE-BINDING PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: POTF;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: KK313;
SOURCE 5 CELLULAR_LOCATION: PERIPLASM;
SOURCE 6 GENE: PUCPOTF;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: KK313POTF\:\:KM;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMWPOTF;
SOURCE 11 EXPRESSION_SYSTEM_GENE: PUCPOTF
KEYWDS BINDING PROTEIN, TRANSPORT, PERIPLASMIC PUTRESCINE BINDING PROTEIN
KEYWDS 2 (POTF)
EXPDTA X-RAY DIFFRACTION
AUTHOR D.G.VASSYLYEV,H.TOMITORI,K.KASHIWAGI,K.MORIKAWA,K.IGARASHI
REVDAT 4 01-APR-20 1A99 1 REMARK
REVDAT 3 24-FEB-09 1A99 1 VERSN
REVDAT 2 18-NOV-98 1A99 1 SOURCE COMPND REMARK JRNL
REVDAT 2 2 1 KEYWDS HEADER
REVDAT 1 21-OCT-98 1A99 0
JRNL AUTH D.G.VASSYLYEV,H.TOMITORI,K.KASHIWAGI,K.MORIKAWA,K.IGARASHI
JRNL TITL CRYSTAL STRUCTURE AND MUTATIONAL ANALYSIS OF THE ESCHERICHIA
JRNL TITL 2 COLI PUTRESCINE RECEPTOR. STRUCTURAL BASIS FOR SUBSTRATE
JRNL TITL 3 SPECIFICITY.
JRNL REF J.BIOL.CHEM. V. 273 17604 1998
JRNL REFN ISSN 0021-9258
JRNL PMID 9651355
JRNL DOI 10.1074/JBC.273.28.17604
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.G.VASSYLYEV,T.KASHIWAGI,H.TOMITORI,K.KASHIWAGI,K.IGARASHI,
REMARK 1 AUTH 2 K.MORIKAWA
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF THE
REMARK 1 TITL 2 PERIPLASMIC RECEPTOR (POTF) OF THE PUTRESCINE TRANSPORT
REMARK 1 TITL 3 SYSTEM IN ESCHERICHIA COLI
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 54 132 1998
REMARK 1 REFN ISSN 0907-4449
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.PISTOCCHI,K.KASHIWAGI,S.MIYAMOTO,E.NUKUI,Y.SADAKATA,
REMARK 1 AUTH 2 H.KOBAYASHI,K.IGARASHI
REMARK 1 TITL CHARACTERISTICS OF THE OPERON FOR A PUTRESCINE TRANSPORT
REMARK 1 TITL 2 SYSTEM THAT MAPS AT 19 MINUTES ON THE ESCHERICHIA COLI
REMARK 1 TITL 3 CHROMOSOME
REMARK 1 REF J.BIOL.CHEM. V. 268 146 1993
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.0
REMARK 3 NUMBER OF REFLECTIONS : 91992
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) : 0.185
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4618
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.017
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.30
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 47.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6513
REMARK 3 BIN R VALUE (WORKING SET) : 0.3320
REMARK 3 BIN FREE R VALUE : 0.3490
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 344
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10720
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 584
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.20
REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.450
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.852
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 4.300 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 6.000 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 7.100 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 9.000 ; 2.500
REMARK 3
REMARK 3 NCS MODEL : RESTRAINED
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : 1.0 ; 100.0
REMARK 3 GROUP 1 B-FACTOR (A**2) : 6.5 ; 1.0
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1A99 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170552.
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 : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
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 : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.8
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 2M
REMARK 280 AMMONIUM SULFATE, 6% GLYCEROL, 200MM CACODYLATE BUFFER (PH 5),
REMARK 280 PH 5.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 134.70000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.16500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 134.70000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.16500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 ALA A 27
REMARK 465 GLU A 28
REMARK 465 LYS A 370
REMARK 465 ALA B 27
REMARK 465 GLU B 28
REMARK 465 LYS B 370
REMARK 465 ALA C 27
REMARK 465 GLU C 28
REMARK 465 LYS C 370
REMARK 465 ALA D 27
REMARK 465 GLU D 28
REMARK 465 LYS D 370
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 A 133 -77.02 -115.22
REMARK 500 ALA A 136 -165.19 -164.99
REMARK 500 SER A 227 -39.92 -157.50
REMARK 500 LYS A 344 30.68 -98.55
REMARK 500 TYR B 133 -75.09 -117.63
REMARK 500 ALA B 136 -165.73 -163.75
REMARK 500 PRO B 156 51.17 -69.80
REMARK 500 SER B 227 -35.00 -156.17
REMARK 500 TYR C 133 -74.23 -113.88
REMARK 500 ALA C 136 -165.50 -163.99
REMARK 500 SER C 227 -35.40 -158.86
REMARK 500 TYR D 133 -73.41 -120.74
REMARK 500 ALA D 136 -165.39 -161.50
REMARK 500 SER D 227 -34.39 -156.77
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 B 729 DISTANCE = 7.35 ANGSTROMS
REMARK 525 HOH D 963 DISTANCE = 5.92 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PUT A 371
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PUT B 371
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PUT C 371
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PUT D 371
DBREF 1A99 A 27 370 UNP P31133 POTF_ECOLI 27 370
DBREF 1A99 B 27 370 UNP P31133 POTF_ECOLI 27 370
DBREF 1A99 C 27 370 UNP P31133 POTF_ECOLI 27 370
DBREF 1A99 D 27 370 UNP P31133 POTF_ECOLI 27 370
SEQRES 1 A 344 ALA GLU GLN LYS THR LEU HIS ILE TYR ASN TRP SER ASP
SEQRES 2 A 344 TYR ILE ALA PRO ASP THR VAL ALA ASN PHE GLU LYS GLU
SEQRES 3 A 344 THR GLY ILE LYS VAL VAL TYR ASP VAL PHE ASP SER ASN
SEQRES 4 A 344 GLU VAL LEU GLU GLY LYS LEU MET ALA GLY SER THR GLY
SEQRES 5 A 344 PHE ASP LEU VAL VAL PRO SER ALA SER PHE LEU GLU ARG
SEQRES 6 A 344 GLN LEU THR ALA GLY VAL PHE GLN PRO LEU ASP LYS SER
SEQRES 7 A 344 LYS LEU PRO GLU TRP LYS ASN LEU ASP PRO GLU LEU LEU
SEQRES 8 A 344 LYS LEU VAL ALA LYS HIS ASP PRO ASP ASN LYS PHE ALA
SEQRES 9 A 344 MET PRO TYR MET TRP ALA THR THR GLY ILE GLY TYR ASN
SEQRES 10 A 344 VAL ASP LYS VAL LYS ALA VAL LEU GLY GLU ASN ALA PRO
SEQRES 11 A 344 VAL ASP SER TRP ASP LEU ILE LEU LYS PRO GLU ASN LEU
SEQRES 12 A 344 GLU LYS LEU LYS SER CYS GLY VAL SER PHE LEU ASP ALA
SEQRES 13 A 344 PRO GLU GLU VAL PHE ALA THR VAL LEU ASN TYR LEU GLY
SEQRES 14 A 344 LYS ASP PRO ASN SER THR LYS ALA ASP ASP TYR THR GLY
SEQRES 15 A 344 PRO ALA THR ASP LEU LEU LEU LYS LEU ARG PRO ASN ILE
SEQRES 16 A 344 ARG TYR PHE HIS SER SER GLN TYR ILE ASN ASP LEU ALA
SEQRES 17 A 344 ASN GLY ASP ILE CYS VAL ALA ILE GLY TRP ALA GLY ASP
SEQRES 18 A 344 VAL TRP GLN ALA SER ASN ARG ALA LYS GLU ALA LYS ASN
SEQRES 19 A 344 GLY VAL ASN VAL SER PHE SER ILE PRO LYS GLU GLY ALA
SEQRES 20 A 344 MET ALA PHE PHE ASP VAL PHE ALA MET PRO ALA ASP ALA
SEQRES 21 A 344 LYS ASN LYS ASP GLU ALA TYR GLN PHE LEU ASN TYR LEU
SEQRES 22 A 344 LEU ARG PRO ASP VAL VAL ALA HIS ILE SER ASP HIS VAL
SEQRES 23 A 344 PHE TYR ALA ASN ALA ASN LYS ALA ALA THR PRO LEU VAL
SEQRES 24 A 344 SER ALA GLU VAL ARG GLU ASN PRO GLY ILE TYR PRO PRO
SEQRES 25 A 344 ALA ASP VAL ARG ALA LYS LEU PHE THR LEU LYS VAL GLN
SEQRES 26 A 344 ASP PRO LYS ILE ASP ARG VAL ARG THR ARG ALA TRP THR
SEQRES 27 A 344 LYS VAL LYS SER GLY LYS
SEQRES 1 B 344 ALA GLU GLN LYS THR LEU HIS ILE TYR ASN TRP SER ASP
SEQRES 2 B 344 TYR ILE ALA PRO ASP THR VAL ALA ASN PHE GLU LYS GLU
SEQRES 3 B 344 THR GLY ILE LYS VAL VAL TYR ASP VAL PHE ASP SER ASN
SEQRES 4 B 344 GLU VAL LEU GLU GLY LYS LEU MET ALA GLY SER THR GLY
SEQRES 5 B 344 PHE ASP LEU VAL VAL PRO SER ALA SER PHE LEU GLU ARG
SEQRES 6 B 344 GLN LEU THR ALA GLY VAL PHE GLN PRO LEU ASP LYS SER
SEQRES 7 B 344 LYS LEU PRO GLU TRP LYS ASN LEU ASP PRO GLU LEU LEU
SEQRES 8 B 344 LYS LEU VAL ALA LYS HIS ASP PRO ASP ASN LYS PHE ALA
SEQRES 9 B 344 MET PRO TYR MET TRP ALA THR THR GLY ILE GLY TYR ASN
SEQRES 10 B 344 VAL ASP LYS VAL LYS ALA VAL LEU GLY GLU ASN ALA PRO
SEQRES 11 B 344 VAL ASP SER TRP ASP LEU ILE LEU LYS PRO GLU ASN LEU
SEQRES 12 B 344 GLU LYS LEU LYS SER CYS GLY VAL SER PHE LEU ASP ALA
SEQRES 13 B 344 PRO GLU GLU VAL PHE ALA THR VAL LEU ASN TYR LEU GLY
SEQRES 14 B 344 LYS ASP PRO ASN SER THR LYS ALA ASP ASP TYR THR GLY
SEQRES 15 B 344 PRO ALA THR ASP LEU LEU LEU LYS LEU ARG PRO ASN ILE
SEQRES 16 B 344 ARG TYR PHE HIS SER SER GLN TYR ILE ASN ASP LEU ALA
SEQRES 17 B 344 ASN GLY ASP ILE CYS VAL ALA ILE GLY TRP ALA GLY ASP
SEQRES 18 B 344 VAL TRP GLN ALA SER ASN ARG ALA LYS GLU ALA LYS ASN
SEQRES 19 B 344 GLY VAL ASN VAL SER PHE SER ILE PRO LYS GLU GLY ALA
SEQRES 20 B 344 MET ALA PHE PHE ASP VAL PHE ALA MET PRO ALA ASP ALA
SEQRES 21 B 344 LYS ASN LYS ASP GLU ALA TYR GLN PHE LEU ASN TYR LEU
SEQRES 22 B 344 LEU ARG PRO ASP VAL VAL ALA HIS ILE SER ASP HIS VAL
SEQRES 23 B 344 PHE TYR ALA ASN ALA ASN LYS ALA ALA THR PRO LEU VAL
SEQRES 24 B 344 SER ALA GLU VAL ARG GLU ASN PRO GLY ILE TYR PRO PRO
SEQRES 25 B 344 ALA ASP VAL ARG ALA LYS LEU PHE THR LEU LYS VAL GLN
SEQRES 26 B 344 ASP PRO LYS ILE ASP ARG VAL ARG THR ARG ALA TRP THR
SEQRES 27 B 344 LYS VAL LYS SER GLY LYS
SEQRES 1 C 344 ALA GLU GLN LYS THR LEU HIS ILE TYR ASN TRP SER ASP
SEQRES 2 C 344 TYR ILE ALA PRO ASP THR VAL ALA ASN PHE GLU LYS GLU
SEQRES 3 C 344 THR GLY ILE LYS VAL VAL TYR ASP VAL PHE ASP SER ASN
SEQRES 4 C 344 GLU VAL LEU GLU GLY LYS LEU MET ALA GLY SER THR GLY
SEQRES 5 C 344 PHE ASP LEU VAL VAL PRO SER ALA SER PHE LEU GLU ARG
SEQRES 6 C 344 GLN LEU THR ALA GLY VAL PHE GLN PRO LEU ASP LYS SER
SEQRES 7 C 344 LYS LEU PRO GLU TRP LYS ASN LEU ASP PRO GLU LEU LEU
SEQRES 8 C 344 LYS LEU VAL ALA LYS HIS ASP PRO ASP ASN LYS PHE ALA
SEQRES 9 C 344 MET PRO TYR MET TRP ALA THR THR GLY ILE GLY TYR ASN
SEQRES 10 C 344 VAL ASP LYS VAL LYS ALA VAL LEU GLY GLU ASN ALA PRO
SEQRES 11 C 344 VAL ASP SER TRP ASP LEU ILE LEU LYS PRO GLU ASN LEU
SEQRES 12 C 344 GLU LYS LEU LYS SER CYS GLY VAL SER PHE LEU ASP ALA
SEQRES 13 C 344 PRO GLU GLU VAL PHE ALA THR VAL LEU ASN TYR LEU GLY
SEQRES 14 C 344 LYS ASP PRO ASN SER THR LYS ALA ASP ASP TYR THR GLY
SEQRES 15 C 344 PRO ALA THR ASP LEU LEU LEU LYS LEU ARG PRO ASN ILE
SEQRES 16 C 344 ARG TYR PHE HIS SER SER GLN TYR ILE ASN ASP LEU ALA
SEQRES 17 C 344 ASN GLY ASP ILE CYS VAL ALA ILE GLY TRP ALA GLY ASP
SEQRES 18 C 344 VAL TRP GLN ALA SER ASN ARG ALA LYS GLU ALA LYS ASN
SEQRES 19 C 344 GLY VAL ASN VAL SER PHE SER ILE PRO LYS GLU GLY ALA
SEQRES 20 C 344 MET ALA PHE PHE ASP VAL PHE ALA MET PRO ALA ASP ALA
SEQRES 21 C 344 LYS ASN LYS ASP GLU ALA TYR GLN PHE LEU ASN TYR LEU
SEQRES 22 C 344 LEU ARG PRO ASP VAL VAL ALA HIS ILE SER ASP HIS VAL
SEQRES 23 C 344 PHE TYR ALA ASN ALA ASN LYS ALA ALA THR PRO LEU VAL
SEQRES 24 C 344 SER ALA GLU VAL ARG GLU ASN PRO GLY ILE TYR PRO PRO
SEQRES 25 C 344 ALA ASP VAL ARG ALA LYS LEU PHE THR LEU LYS VAL GLN
SEQRES 26 C 344 ASP PRO LYS ILE ASP ARG VAL ARG THR ARG ALA TRP THR
SEQRES 27 C 344 LYS VAL LYS SER GLY LYS
SEQRES 1 D 344 ALA GLU GLN LYS THR LEU HIS ILE TYR ASN TRP SER ASP
SEQRES 2 D 344 TYR ILE ALA PRO ASP THR VAL ALA ASN PHE GLU LYS GLU
SEQRES 3 D 344 THR GLY ILE LYS VAL VAL TYR ASP VAL PHE ASP SER ASN
SEQRES 4 D 344 GLU VAL LEU GLU GLY LYS LEU MET ALA GLY SER THR GLY
SEQRES 5 D 344 PHE ASP LEU VAL VAL PRO SER ALA SER PHE LEU GLU ARG
SEQRES 6 D 344 GLN LEU THR ALA GLY VAL PHE GLN PRO LEU ASP LYS SER
SEQRES 7 D 344 LYS LEU PRO GLU TRP LYS ASN LEU ASP PRO GLU LEU LEU
SEQRES 8 D 344 LYS LEU VAL ALA LYS HIS ASP PRO ASP ASN LYS PHE ALA
SEQRES 9 D 344 MET PRO TYR MET TRP ALA THR THR GLY ILE GLY TYR ASN
SEQRES 10 D 344 VAL ASP LYS VAL LYS ALA VAL LEU GLY GLU ASN ALA PRO
SEQRES 11 D 344 VAL ASP SER TRP ASP LEU ILE LEU LYS PRO GLU ASN LEU
SEQRES 12 D 344 GLU LYS LEU LYS SER CYS GLY VAL SER PHE LEU ASP ALA
SEQRES 13 D 344 PRO GLU GLU VAL PHE ALA THR VAL LEU ASN TYR LEU GLY
SEQRES 14 D 344 LYS ASP PRO ASN SER THR LYS ALA ASP ASP TYR THR GLY
SEQRES 15 D 344 PRO ALA THR ASP LEU LEU LEU LYS LEU ARG PRO ASN ILE
SEQRES 16 D 344 ARG TYR PHE HIS SER SER GLN TYR ILE ASN ASP LEU ALA
SEQRES 17 D 344 ASN GLY ASP ILE CYS VAL ALA ILE GLY TRP ALA GLY ASP
SEQRES 18 D 344 VAL TRP GLN ALA SER ASN ARG ALA LYS GLU ALA LYS ASN
SEQRES 19 D 344 GLY VAL ASN VAL SER PHE SER ILE PRO LYS GLU GLY ALA
SEQRES 20 D 344 MET ALA PHE PHE ASP VAL PHE ALA MET PRO ALA ASP ALA
SEQRES 21 D 344 LYS ASN LYS ASP GLU ALA TYR GLN PHE LEU ASN TYR LEU
SEQRES 22 D 344 LEU ARG PRO ASP VAL VAL ALA HIS ILE SER ASP HIS VAL
SEQRES 23 D 344 PHE TYR ALA ASN ALA ASN LYS ALA ALA THR PRO LEU VAL
SEQRES 24 D 344 SER ALA GLU VAL ARG GLU ASN PRO GLY ILE TYR PRO PRO
SEQRES 25 D 344 ALA ASP VAL ARG ALA LYS LEU PHE THR LEU LYS VAL GLN
SEQRES 26 D 344 ASP PRO LYS ILE ASP ARG VAL ARG THR ARG ALA TRP THR
SEQRES 27 D 344 LYS VAL LYS SER GLY LYS
HET PUT A 371 6
HET PUT B 371 6
HET PUT C 371 6
HET PUT D 371 6
HETNAM PUT 1,4-DIAMINOBUTANE
HETSYN PUT PUTRESCINE
FORMUL 5 PUT 4(C4 H12 N2)
FORMUL 9 HOH *584(H2 O)
HELIX 1 1 THR A 45 THR A 53 1 9
HELIX 2 2 ASN A 65 ALA A 74 1 10
HELIX 3 3 ALA A 86 THR A 94 1 9
HELIX 4 4 LYS A 103 LYS A 105 5 3
HELIX 5 5 PRO A 107 ASN A 111 5 5
HELIX 6 6 PRO A 114 LYS A 122 1 9
HELIX 7 7 PRO A 125 ASN A 127 5 3
HELIX 8 8 VAL A 144 LEU A 151 1 8
HELIX 9 9 TRP A 160 LEU A 164 5 5
HELIX 10 10 PRO A 166 CYS A 175 1 10
HELIX 11 11 PRO A 183 TYR A 193 1 11
HELIX 12 12 ALA A 203 THR A 207 1 5
HELIX 13 13 PRO A 209 ASN A 220 1 12
HELIX 14 14 GLN A 228 ALA A 234 1 7
HELIX 15 15 ALA A 245 ALA A 258 1 14
HELIX 16 16 LYS A 289 LEU A 300 1 12
HELIX 17 17 PRO A 302 VAL A 312 1 11
HELIX 18 18 THR A 322 LEU A 324 5 3
HELIX 19 19 ALA A 327 ARG A 330 1 4
HELIX 20 20 ALA A 339 LYS A 344 1 6
HELIX 21 21 PRO A 353 LYS A 367 1 15
HELIX 22 22 THR B 45 THR B 53 1 9
HELIX 23 23 ASN B 65 ALA B 74 1 10
HELIX 24 24 ALA B 86 THR B 94 1 9
HELIX 25 25 LYS B 103 LYS B 105 5 3
HELIX 26 26 PRO B 107 ASN B 111 5 5
HELIX 27 27 PRO B 114 LYS B 122 1 9
HELIX 28 28 PRO B 125 ASN B 127 5 3
HELIX 29 29 VAL B 144 LEU B 151 1 8
HELIX 30 30 TRP B 160 LEU B 164 5 5
HELIX 31 31 PRO B 166 CYS B 175 1 10
HELIX 32 32 PRO B 183 TYR B 193 1 11
HELIX 33 33 ALA B 203 THR B 207 1 5
HELIX 34 34 PRO B 209 ASN B 220 1 12
HELIX 35 35 GLN B 228 ASN B 235 1 8
HELIX 36 36 ALA B 245 ALA B 258 1 14
HELIX 37 37 LYS B 289 LEU B 300 1 12
HELIX 38 38 PRO B 302 VAL B 312 1 11
HELIX 39 39 THR B 322 LEU B 324 5 3
HELIX 40 40 ALA B 327 ARG B 330 1 4
HELIX 41 41 ALA B 339 LYS B 344 1 6
HELIX 42 42 PRO B 353 LYS B 367 1 15
HELIX 43 43 THR C 45 THR C 53 1 9
HELIX 44 44 ASN C 65 ALA C 74 1 10
HELIX 45 45 ALA C 86 THR C 94 1 9
HELIX 46 46 LYS C 103 LYS C 105 5 3
HELIX 47 47 PRO C 107 ASN C 111 5 5
HELIX 48 48 PRO C 114 LYS C 122 1 9
HELIX 49 49 PRO C 125 ASN C 127 5 3
HELIX 50 50 VAL C 144 LEU C 151 1 8
HELIX 51 51 TRP C 160 LEU C 164 5 5
HELIX 52 52 PRO C 166 CYS C 175 1 10
HELIX 53 53 PRO C 183 TYR C 193 1 11
HELIX 54 54 ALA C 203 THR C 207 1 5
HELIX 55 55 PRO C 209 ASN C 220 1 12
HELIX 56 56 GLN C 228 ALA C 234 1 7
HELIX 57 57 ALA C 245 ALA C 258 1 14
HELIX 58 58 LYS C 289 LEU C 300 1 12
HELIX 59 59 PRO C 302 VAL C 312 1 11
HELIX 60 60 THR C 322 LEU C 324 5 3
HELIX 61 61 ALA C 327 ARG C 330 1 4
HELIX 62 62 ALA C 339 LYS C 344 1 6
HELIX 63 63 PRO C 353 LYS C 367 1 15
HELIX 64 64 THR D 45 THR D 53 1 9
HELIX 65 65 ASN D 65 ALA D 74 1 10
HELIX 66 66 ALA D 86 THR D 94 1 9
HELIX 67 67 LYS D 103 LYS D 105 5 3
HELIX 68 68 PRO D 107 ASN D 111 5 5
HELIX 69 69 PRO D 114 LYS D 122 1 9
HELIX 70 70 PRO D 125 ASN D 127 5 3
HELIX 71 71 VAL D 144 LEU D 151 1 8
HELIX 72 72 TRP D 160 LEU D 164 5 5
HELIX 73 73 PRO D 166 LEU D 172 1 7
HELIX 74 74 PRO D 183 TYR D 193 1 11
HELIX 75 75 ALA D 203 THR D 207 1 5
HELIX 76 76 PRO D 209 ASN D 220 1 12
HELIX 77 77 GLN D 228 ASN D 235 1 8
HELIX 78 78 ALA D 245 ALA D 258 1 14
HELIX 79 79 LYS D 289 LEU D 300 1 12
HELIX 80 80 PRO D 302 VAL D 312 1 11
HELIX 81 81 THR D 322 LEU D 324 5 3
HELIX 82 82 ALA D 327 ARG D 330 1 4
HELIX 83 83 ALA D 339 LYS D 344 1 6
HELIX 84 84 PRO D 353 LYS D 367 1 15
SHEET 1 A 2 THR A 31 TRP A 37 0
SHEET 2 A 2 LYS A 56 PHE A 62 1 N LYS A 56 O LEU A 32
SHEET 1 B 3 VAL A 240 TRP A 244 0
SHEET 2 B 3 THR A 138 ASN A 143 -1 N GLY A 141 O ALA A 241
SHEET 3 B 3 VAL A 264 SER A 267 -1 N SER A 267 O ILE A 140
SHEET 1 C 2 ALA A 130 THR A 138 0
SHEET 2 C 2 MET A 274 ALA A 281 -1 N PHE A 280 O MET A 131
SHEET 1 D 2 THR B 31 TRP B 37 0
SHEET 2 D 2 LYS B 56 PHE B 62 1 N LYS B 56 O LEU B 32
SHEET 1 E 3 VAL B 240 TRP B 244 0
SHEET 2 E 3 THR B 138 ASN B 143 -1 N GLY B 141 O ALA B 241
SHEET 3 E 3 VAL B 264 SER B 267 -1 N SER B 267 O ILE B 140
SHEET 1 F 2 ALA B 130 THR B 138 0
SHEET 2 F 2 MET B 274 ALA B 281 -1 N PHE B 280 O MET B 131
SHEET 1 G 2 THR C 31 TRP C 37 0
SHEET 2 G 2 LYS C 56 PHE C 62 1 N LYS C 56 O LEU C 32
SHEET 1 H 3 VAL C 240 TRP C 244 0
SHEET 2 H 3 THR C 138 ASN C 143 -1 N GLY C 141 O ALA C 241
SHEET 3 H 3 VAL C 264 SER C 267 -1 N SER C 267 O ILE C 140
SHEET 1 I 2 ALA C 130 THR C 138 0
SHEET 2 I 2 MET C 274 ALA C 281 -1 N PHE C 280 O MET C 131
SHEET 1 J 2 THR D 31 TRP D 37 0
SHEET 2 J 2 LYS D 56 PHE D 62 1 N LYS D 56 O LEU D 32
SHEET 1 K 3 VAL D 240 TRP D 244 0
SHEET 2 K 3 THR D 138 ASN D 143 -1 N GLY D 141 O ALA D 241
SHEET 3 K 3 VAL D 264 SER D 267 -1 N SER D 267 O ILE D 140
SHEET 1 L 2 ALA D 130 THR D 138 0
SHEET 2 L 2 MET D 274 ALA D 281 -1 N PHE D 280 O MET D 131
SSBOND 1 CYS A 175 CYS A 239 1555 1555 2.04
SSBOND 2 CYS B 175 CYS B 239 1555 1555 2.04
SSBOND 3 CYS C 175 CYS C 239 1555 1555 2.04
SSBOND 4 CYS D 175 CYS D 239 1555 1555 2.04
SITE 1 AC1 11 TRP A 37 SER A 38 ASP A 39 TYR A 40
SITE 2 AC1 11 TRP A 244 ASP A 247 PHE A 276 ASP A 278
SITE 3 AC1 11 TYR A 314 HOH A 471 HOH A 968
SITE 1 AC2 11 TRP B 37 SER B 38 ASP B 39 TYR B 40
SITE 2 AC2 11 TRP B 244 ASP B 247 PHE B 276 ASP B 278
SITE 3 AC2 11 TYR B 314 HOH B 743 HOH B 858
SITE 1 AC3 11 TRP C 37 SER C 38 ASP C 39 TYR C 40
SITE 2 AC3 11 TRP C 244 ASP C 247 PHE C 276 ASP C 278
SITE 3 AC3 11 TYR C 314 HOH C 897 HOH C 962
SITE 1 AC4 11 TRP D 37 SER D 38 ASP D 39 TYR D 40
SITE 2 AC4 11 TRP D 244 ASP D 247 PHE D 276 ASP D 278
SITE 3 AC4 11 TYR D 314 HOH D 412 HOH D 456
CRYST1 269.400 82.330 93.740 90.00 90.00 90.00 P 21 21 2 16
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 0.003712 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012146 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010668 0.00000
MTRIX1 1 -0.794200 0.596650 -0.115100 289.24081 1
MTRIX2 1 0.464340 0.473720 -0.748320 -14.83522 1
MTRIX3 1 -0.391960 -0.647770 -0.653280 190.97041 1
MTRIX1 2 0.939690 0.138750 -0.312610 31.41611 1
MTRIX2 2 0.119350 -0.989590 -0.080450 65.41694 1
MTRIX3 2 -0.320520 0.038280 -0.946470 155.36401 1
MTRIX1 3 -0.877840 0.475720 0.055580 297.77582 1
MTRIX2 3 -0.272430 -0.591380 0.758980 60.40127 1
MTRIX3 3 0.393930 0.651120 0.648740 -92.03163 1
(ATOM LINES ARE NOT SHOWN.)
END
