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HEADER HYDROLASE 27-MAY-11 3AZP
TITLE CRYSTAL STRUCTURE OF PUROMYCIN HYDROLASE S511A MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMINOPEPTIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES MOROOKAENSIS;
SOURCE 3 ORGANISM_TAXID: 1970;
SOURCE 4 STRAIN: JCM4673;
SOURCE 5 GENE: PMH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-21A(+)
KEYWDS POP FAMILY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.MATOBA,M.SUGIYAMA
REVDAT 1 27-JUL-11 3AZP 0
JRNL AUTH Y.MATOBA,A.NAKAYAMA,K.ODA,M.NODA,T.KUMAGAI,M.NISHIMURA,
JRNL AUTH 2 M.SUGIYAMA
JRNL TITL STRUCTURAL EVIDENCE THAT PUROMYCIN HYDROLASE ACTS AS
JRNL TITL 2 AMINOPEPTIDASE WITH POP FAMILY FOLD
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3224286.670
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.2
REMARK 3 NUMBER OF REFLECTIONS : 95702
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) : 0.188
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4814
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.28
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 13751
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 713
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10054
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 1009
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.31000
REMARK 3 B22 (A**2) : 8.74000
REMARK 3 B33 (A**2) : -6.44000
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) : 0.24
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) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.28
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.83
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) : 1.150 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.770 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.930 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.730 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 61.58
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3AZP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JUN-11.
REMARK 100 THE RCSB ID CODE IS RCSB029896.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-DEC-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : VERTICALLY BENT CYLINDER MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU JUPITER 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95945
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.41600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: CNS 1.2
REMARK 200 STARTING MODEL: PDB ENTRY 3AZO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.7M AMMONIUM SULFATE, 0.1M TRIS-HCL
REMARK 280 , PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 42.05500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.15000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 71.31000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.15000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.05500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 71.31000
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
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: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 MET B 1
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 A 45 64.06 -110.95
REMARK 500 PHE A 75 14.72 57.97
REMARK 500 GLU A 76 -4.75 60.36
REMARK 500 SER A 78 106.62 86.45
REMARK 500 GLN A 102 14.99 58.98
REMARK 500 CYS A 281 87.49 -165.61
REMARK 500 ALA A 288 -168.08 -161.59
REMARK 500 ALA A 332 -129.29 -103.27
REMARK 500 PRO A 385 -8.51 -59.56
REMARK 500 ASP A 421 30.15 -90.68
REMARK 500 SER A 436 -171.41 -172.89
REMARK 500 ALA A 440 79.30 -103.53
REMARK 500 VAL A 481 -61.42 -123.59
REMARK 500 ALA A 511 -123.45 56.59
REMARK 500 TYR A 534 66.14 22.26
REMARK 500 GLU B 45 58.22 -110.77
REMARK 500 SER B 78 112.31 79.43
REMARK 500 PHE B 80 114.66 -39.93
REMARK 500 PRO B 210 42.44 -101.36
REMARK 500 CYS B 281 74.97 -171.29
REMARK 500 ALA B 288 -169.27 -164.17
REMARK 500 ALA B 332 -116.33 -72.57
REMARK 500 PRO B 385 -9.78 -56.86
REMARK 500 ALA B 440 74.34 -108.76
REMARK 500 ALA B 511 -121.23 58.18
REMARK 500 TYR B 534 70.92 24.57
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 A1890 DISTANCE = 5.18 ANGSTROMS
REMARK 525 HOH B1467 DISTANCE = 5.11 ANGSTROMS
REMARK 525 HOH B1783 DISTANCE = 5.24 ANGSTROMS
REMARK 525 HOH B1885 DISTANCE = 5.23 ANGSTROMS
REMARK 525 HOH B1921 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH B1945 DISTANCE = 5.12 ANGSTROMS
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 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1005
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3AZO RELATED DB: PDB
REMARK 900 RELATED ID: 3AZQ RELATED DB: PDB
DBREF 3AZP A 1 662 UNP Q2HXD9 Q2HXD9_STRMO 1 662
DBREF 3AZP B 1 662 UNP Q2HXD9 Q2HXD9_STRMO 1 662
SEQADV 3AZP ALA A 511 UNP Q2HXD9 SER 511 ENGINEERED MUTATION
SEQADV 3AZP ALA B 511 UNP Q2HXD9 SER 511 ENGINEERED MUTATION
SEQRES 1 A 662 MET VAL SER THR ALA PRO TYR GLY ALA TRP GLN SER PRO
SEQRES 2 A 662 ILE ASP ALA ALA LEU VAL ALA SER ARG SER GLY ARG PRO
SEQRES 3 A 662 ALA CYS VAL GLY ALA VAL GLY ASP GLU VAL TRP TRP VAL
SEQRES 4 A 662 ALA PRO ARG PRO ALA GLU ALA GLY ARG ALA THR LEU VAL
SEQRES 5 A 662 ARG ARG ARG ALA ASP GLY ALA GLU GLU SER ALA LEU PRO
SEQRES 6 A 662 ALA PRO TRP ASN VAL ARG ASN ARG VAL PHE GLU TYR SER
SEQRES 7 A 662 GLY PHE PRO TRP ALA GLY VAL PRO ARG PRO ALA GLY GLY
SEQRES 8 A 662 PRO LEU LEU VAL PHE THR HIS PHE GLY ASP GLN ARG LEU
SEQRES 9 A 662 TYR ALA PHE GLU PRO ASP ALA PRO GLY GLY ALA VAL PRO
SEQRES 10 A 662 ARG PRO LEU THR PRO VAL SER ALA VAL GLY GLY GLY LEU
SEQRES 11 A 662 ARG TRP ALA ASP PRO VAL LEU LEU PRO GLU ARG GLY GLU
SEQRES 12 A 662 VAL TRP CYS MET ALA GLU GLU PHE THR GLY GLU GLY PRO
SEQRES 13 A 662 SER ASP VAL ARG ARG PHE LEU ALA ALA VAL PRO LEU ASP
SEQRES 14 A 662 GLY SER ALA ALA ALA ASP ARG SER ALA VAL ARG GLU LEU
SEQRES 15 A 662 SER ASP ASP ALA HIS ARG PHE VAL THR GLY PRO ARG LEU
SEQRES 16 A 662 SER PRO ASP GLY ARG GLN ALA VAL TRP LEU ALA TRP ASP
SEQRES 17 A 662 HIS PRO ARG MET PRO TRP GLU GLY THR GLU LEU LYS THR
SEQRES 18 A 662 ALA ARG VAL THR GLU ASP GLY ARG PHE ALA ASP THR ARG
SEQRES 19 A 662 THR LEU LEU GLY GLY PRO GLU GLU ALA ILE ALA GLN ALA
SEQRES 20 A 662 GLU TRP ALA PRO ASP GLY SER LEU ILE VAL ALA THR ASP
SEQRES 21 A 662 ARG THR GLY TRP TRP ASN LEU HIS ARG VAL ASP PRO ALA
SEQRES 22 A 662 THR GLY ALA ALA THR GLN LEU CYS ARG ARG GLU GLU GLU
SEQRES 23 A 662 PHE ALA GLY PRO LEU TRP THR PRO GLY MET ARG TRP PHE
SEQRES 24 A 662 ALA PRO LEU ALA ASN GLY LEU ILE ALA VAL VAL HIS GLY
SEQRES 25 A 662 LYS GLY ALA ALA VAL LEU GLY ILE LEU ASP PRO GLU SER
SEQRES 26 A 662 GLY GLU LEU VAL ASP ALA ALA GLY PRO TRP THR GLU TRP
SEQRES 27 A 662 ALA ALA THR LEU THR VAL SER GLY THR ARG ALA VAL GLY
SEQRES 28 A 662 VAL ALA ALA SER PRO ARG THR ALA TYR GLU VAL VAL GLU
SEQRES 29 A 662 LEU ASP THR VAL THR GLY ARG ALA ARG THR ILE GLY ALA
SEQRES 30 A 662 ARG HIS THR ASP PRO VAL ASP PRO ALA TYR TYR PRO GLU
SEQRES 31 A 662 PRO GLN ILE ARG THR PHE THR ALA PRO ASP GLY ARG GLU
SEQRES 32 A 662 ILE HIS ALA HIS ILE TYR PRO PRO HIS SER PRO ASP PHE
SEQRES 33 A 662 THR GLY PRO ALA ASP GLU LEU PRO PRO TYR VAL VAL MET
SEQRES 34 A 662 ALA HIS GLY GLY PRO THR SER ARG VAL PRO ALA VAL LEU
SEQRES 35 A 662 ASP LEU ASP VAL ALA TYR PHE THR SER ARG GLY ILE GLY
SEQRES 36 A 662 VAL ALA ASP VAL ASN TYR GLY GLY SER THR GLY TYR GLY
SEQRES 37 A 662 ARG ALA TYR ARG GLU ARG LEU ARG GLY ARG TRP GLY VAL
SEQRES 38 A 662 VAL ASP VAL GLU ASP CYS ALA ALA VAL ALA THR ALA LEU
SEQRES 39 A 662 ALA GLU GLU GLY THR ALA ASP ARG ALA ARG LEU ALA VAL
SEQRES 40 A 662 ARG GLY GLY ALA ALA GLY GLY TRP THR ALA ALA SER SER
SEQRES 41 A 662 LEU VAL SER THR ASP VAL TYR ALA CYS GLY THR VAL LEU
SEQRES 42 A 662 TYR PRO VAL LEU ASP LEU LEU GLY TRP ALA ASP GLY GLY
SEQRES 43 A 662 THR HIS ASP PHE GLU SER ARG TYR LEU ASP PHE LEU ILE
SEQRES 44 A 662 GLY SER PHE GLU GLU PHE PRO GLU ARG TYR ARG ASP ARG
SEQRES 45 A 662 ALA PRO LEU THR ARG ALA ASP ARG VAL ARG VAL PRO PHE
SEQRES 46 A 662 LEU LEU LEU GLN GLY LEU GLU ASP PRO VAL CYS PRO PRO
SEQRES 47 A 662 GLU GLN CYS ASP ARG PHE LEU GLU ALA VAL ALA GLY CYS
SEQRES 48 A 662 GLY VAL PRO HIS ALA TYR LEU SER PHE GLU GLY GLU GLY
SEQRES 49 A 662 HIS GLY PHE ARG ARG LYS GLU THR MET VAL ARG ALA LEU
SEQRES 50 A 662 GLU ALA GLU LEU SER LEU TYR ALA GLN VAL PHE GLY VAL
SEQRES 51 A 662 GLU VAL ALA GLY VAL PRO LEU LEU LYS LEU GLY GLU
SEQRES 1 B 662 MET VAL SER THR ALA PRO TYR GLY ALA TRP GLN SER PRO
SEQRES 2 B 662 ILE ASP ALA ALA LEU VAL ALA SER ARG SER GLY ARG PRO
SEQRES 3 B 662 ALA CYS VAL GLY ALA VAL GLY ASP GLU VAL TRP TRP VAL
SEQRES 4 B 662 ALA PRO ARG PRO ALA GLU ALA GLY ARG ALA THR LEU VAL
SEQRES 5 B 662 ARG ARG ARG ALA ASP GLY ALA GLU GLU SER ALA LEU PRO
SEQRES 6 B 662 ALA PRO TRP ASN VAL ARG ASN ARG VAL PHE GLU TYR SER
SEQRES 7 B 662 GLY PHE PRO TRP ALA GLY VAL PRO ARG PRO ALA GLY GLY
SEQRES 8 B 662 PRO LEU LEU VAL PHE THR HIS PHE GLY ASP GLN ARG LEU
SEQRES 9 B 662 TYR ALA PHE GLU PRO ASP ALA PRO GLY GLY ALA VAL PRO
SEQRES 10 B 662 ARG PRO LEU THR PRO VAL SER ALA VAL GLY GLY GLY LEU
SEQRES 11 B 662 ARG TRP ALA ASP PRO VAL LEU LEU PRO GLU ARG GLY GLU
SEQRES 12 B 662 VAL TRP CYS MET ALA GLU GLU PHE THR GLY GLU GLY PRO
SEQRES 13 B 662 SER ASP VAL ARG ARG PHE LEU ALA ALA VAL PRO LEU ASP
SEQRES 14 B 662 GLY SER ALA ALA ALA ASP ARG SER ALA VAL ARG GLU LEU
SEQRES 15 B 662 SER ASP ASP ALA HIS ARG PHE VAL THR GLY PRO ARG LEU
SEQRES 16 B 662 SER PRO ASP GLY ARG GLN ALA VAL TRP LEU ALA TRP ASP
SEQRES 17 B 662 HIS PRO ARG MET PRO TRP GLU GLY THR GLU LEU LYS THR
SEQRES 18 B 662 ALA ARG VAL THR GLU ASP GLY ARG PHE ALA ASP THR ARG
SEQRES 19 B 662 THR LEU LEU GLY GLY PRO GLU GLU ALA ILE ALA GLN ALA
SEQRES 20 B 662 GLU TRP ALA PRO ASP GLY SER LEU ILE VAL ALA THR ASP
SEQRES 21 B 662 ARG THR GLY TRP TRP ASN LEU HIS ARG VAL ASP PRO ALA
SEQRES 22 B 662 THR GLY ALA ALA THR GLN LEU CYS ARG ARG GLU GLU GLU
SEQRES 23 B 662 PHE ALA GLY PRO LEU TRP THR PRO GLY MET ARG TRP PHE
SEQRES 24 B 662 ALA PRO LEU ALA ASN GLY LEU ILE ALA VAL VAL HIS GLY
SEQRES 25 B 662 LYS GLY ALA ALA VAL LEU GLY ILE LEU ASP PRO GLU SER
SEQRES 26 B 662 GLY GLU LEU VAL ASP ALA ALA GLY PRO TRP THR GLU TRP
SEQRES 27 B 662 ALA ALA THR LEU THR VAL SER GLY THR ARG ALA VAL GLY
SEQRES 28 B 662 VAL ALA ALA SER PRO ARG THR ALA TYR GLU VAL VAL GLU
SEQRES 29 B 662 LEU ASP THR VAL THR GLY ARG ALA ARG THR ILE GLY ALA
SEQRES 30 B 662 ARG HIS THR ASP PRO VAL ASP PRO ALA TYR TYR PRO GLU
SEQRES 31 B 662 PRO GLN ILE ARG THR PHE THR ALA PRO ASP GLY ARG GLU
SEQRES 32 B 662 ILE HIS ALA HIS ILE TYR PRO PRO HIS SER PRO ASP PHE
SEQRES 33 B 662 THR GLY PRO ALA ASP GLU LEU PRO PRO TYR VAL VAL MET
SEQRES 34 B 662 ALA HIS GLY GLY PRO THR SER ARG VAL PRO ALA VAL LEU
SEQRES 35 B 662 ASP LEU ASP VAL ALA TYR PHE THR SER ARG GLY ILE GLY
SEQRES 36 B 662 VAL ALA ASP VAL ASN TYR GLY GLY SER THR GLY TYR GLY
SEQRES 37 B 662 ARG ALA TYR ARG GLU ARG LEU ARG GLY ARG TRP GLY VAL
SEQRES 38 B 662 VAL ASP VAL GLU ASP CYS ALA ALA VAL ALA THR ALA LEU
SEQRES 39 B 662 ALA GLU GLU GLY THR ALA ASP ARG ALA ARG LEU ALA VAL
SEQRES 40 B 662 ARG GLY GLY ALA ALA GLY GLY TRP THR ALA ALA SER SER
SEQRES 41 B 662 LEU VAL SER THR ASP VAL TYR ALA CYS GLY THR VAL LEU
SEQRES 42 B 662 TYR PRO VAL LEU ASP LEU LEU GLY TRP ALA ASP GLY GLY
SEQRES 43 B 662 THR HIS ASP PHE GLU SER ARG TYR LEU ASP PHE LEU ILE
SEQRES 44 B 662 GLY SER PHE GLU GLU PHE PRO GLU ARG TYR ARG ASP ARG
SEQRES 45 B 662 ALA PRO LEU THR ARG ALA ASP ARG VAL ARG VAL PRO PHE
SEQRES 46 B 662 LEU LEU LEU GLN GLY LEU GLU ASP PRO VAL CYS PRO PRO
SEQRES 47 B 662 GLU GLN CYS ASP ARG PHE LEU GLU ALA VAL ALA GLY CYS
SEQRES 48 B 662 GLY VAL PRO HIS ALA TYR LEU SER PHE GLU GLY GLU GLY
SEQRES 49 B 662 HIS GLY PHE ARG ARG LYS GLU THR MET VAL ARG ALA LEU
SEQRES 50 B 662 GLU ALA GLU LEU SER LEU TYR ALA GLN VAL PHE GLY VAL
SEQRES 51 B 662 GLU VAL ALA GLY VAL PRO LEU LEU LYS LEU GLY GLU
HET SO4 A1001 5
HET SO4 A1002 5
HET SO4 A1003 5
HET SO4 B1004 5
HET SO4 B1005 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 5(O4 S 2-)
FORMUL 8 HOH *1009(H2 O)
HELIX 1 1 ASP A 15 ARG A 22 1 8
HELIX 2 2 ARG A 73 TYR A 77 5 5
HELIX 3 3 ASP A 175 VAL A 179 5 5
HELIX 4 4 ASP A 384 TYR A 388 5 5
HELIX 5 5 ASP A 443 SER A 451 1 9
HELIX 6 6 GLY A 468 ARG A 474 1 7
HELIX 7 7 VAL A 481 GLU A 497 1 17
HELIX 8 8 ALA A 511 THR A 524 1 14
HELIX 9 9 ASP A 538 ASP A 544 1 7
HELIX 10 10 HIS A 548 ARG A 553 5 6
HELIX 11 11 TYR A 554 ILE A 559 1 6
HELIX 12 12 GLU A 567 ARG A 572 1 6
HELIX 13 13 ALA A 573 VAL A 581 5 9
HELIX 14 14 PRO A 598 ALA A 609 1 12
HELIX 15 15 ARG A 629 PHE A 648 1 20
HELIX 16 16 ASP B 15 ARG B 22 1 8
HELIX 17 17 ARG B 73 TYR B 77 5 5
HELIX 18 18 PRO B 139 ARG B 141 5 3
HELIX 19 19 ASP B 175 VAL B 179 5 5
HELIX 20 20 ASP B 384 TYR B 388 5 5
HELIX 21 21 ASP B 443 SER B 451 1 9
HELIX 22 22 GLY B 468 ARG B 474 1 7
HELIX 23 23 VAL B 481 GLU B 497 1 17
HELIX 24 24 ALA B 511 THR B 524 1 14
HELIX 25 25 ASP B 538 ASP B 544 1 7
HELIX 26 26 HIS B 548 SER B 552 5 5
HELIX 27 27 ARG B 553 ILE B 559 1 7
HELIX 28 28 GLU B 567 ARG B 572 1 6
HELIX 29 29 ALA B 573 VAL B 581 5 9
HELIX 30 30 PRO B 598 ALA B 609 1 12
HELIX 31 31 ARG B 629 GLY B 649 1 21
SHEET 1 A 2 SER A 3 THR A 4 0
SHEET 2 A 2 PHE A 416 THR A 417 1 O THR A 417 N SER A 3
SHEET 1 B 4 ALA A 27 VAL A 32 0
SHEET 2 B 4 GLU A 35 ARG A 42 -1 O VAL A 39 N ALA A 27
SHEET 3 B 4 ARG A 48 ARG A 54 -1 O THR A 50 N ALA A 40
SHEET 4 B 4 GLU A 60 SER A 62 -1 O GLU A 61 N ARG A 53
SHEET 1 C 4 TRP A 82 VAL A 85 0
SHEET 2 C 4 LEU A 93 THR A 97 -1 O LEU A 93 N VAL A 85
SHEET 3 C 4 LEU A 104 PHE A 107 -1 O TYR A 105 N PHE A 96
SHEET 4 C 4 ARG A 118 PRO A 119 -1 O ARG A 118 N ALA A 106
SHEET 1 D 4 LEU A 130 LEU A 138 0
SHEET 2 D 4 GLU A 143 PHE A 151 -1 O TRP A 145 N VAL A 136
SHEET 3 D 4 VAL A 159 PRO A 167 -1 O ALA A 164 N CYS A 146
SHEET 4 D 4 ARG A 180 GLU A 181 -1 O ARG A 180 N ALA A 165
SHEET 1 E 3 PHE A 189 VAL A 190 0
SHEET 2 E 3 GLN A 201 TRP A 207 -1 O TRP A 207 N PHE A 189
SHEET 3 E 3 ARG A 194 LEU A 195 -1 N ARG A 194 O VAL A 203
SHEET 1 F 4 PHE A 189 VAL A 190 0
SHEET 2 F 4 GLN A 201 TRP A 207 -1 O TRP A 207 N PHE A 189
SHEET 3 F 4 THR A 217 VAL A 224 -1 O LYS A 220 N TRP A 204
SHEET 4 F 4 PHE A 230 GLY A 239 -1 O LEU A 237 N LEU A 219
SHEET 1 G 4 ILE A 244 TRP A 249 0
SHEET 2 G 4 LEU A 255 THR A 259 -1 O ILE A 256 N GLU A 248
SHEET 3 G 4 ASN A 266 VAL A 270 -1 O VAL A 270 N LEU A 255
SHEET 4 G 4 ALA A 277 GLN A 279 -1 O THR A 278 N ARG A 269
SHEET 1 H 4 PHE A 299 PRO A 301 0
SHEET 2 H 4 ILE A 307 HIS A 311 -1 O ALA A 308 N ALA A 300
SHEET 3 H 4 VAL A 317 LEU A 321 -1 O LEU A 321 N ILE A 307
SHEET 4 H 4 LEU A 328 ASP A 330 -1 O VAL A 329 N ILE A 320
SHEET 1 I 4 GLU A 337 SER A 345 0
SHEET 2 I 4 ARG A 348 SER A 355 -1 O VAL A 350 N THR A 343
SHEET 3 I 4 THR A 358 ASP A 366 -1 O LEU A 365 N ALA A 349
SHEET 4 I 4 ALA A 372 GLY A 376 -1 O ARG A 373 N GLU A 364
SHEET 1 J 8 GLN A 392 THR A 397 0
SHEET 2 J 8 GLU A 403 TYR A 409 -1 O ALA A 406 N ARG A 394
SHEET 3 J 8 GLY A 455 ASN A 460 -1 O VAL A 456 N TYR A 409
SHEET 4 J 8 TYR A 426 ALA A 430 1 N VAL A 427 O GLY A 455
SHEET 5 J 8 LEU A 505 GLY A 510 1 O ALA A 506 N VAL A 428
SHEET 6 J 8 CYS A 529 LEU A 533 1 O LEU A 533 N GLY A 509
SHEET 7 J 8 PHE A 585 GLY A 590 1 O LEU A 586 N VAL A 532
SHEET 8 J 8 HIS A 615 PHE A 620 1 O ALA A 616 N LEU A 587
SHEET 1 K 2 SER B 3 THR B 4 0
SHEET 2 K 2 PHE B 416 THR B 417 1 O THR B 417 N SER B 3
SHEET 1 L 4 ALA B 27 VAL B 32 0
SHEET 2 L 4 GLU B 35 ARG B 42 -1 O VAL B 39 N ALA B 27
SHEET 3 L 4 ARG B 48 ARG B 54 -1 O VAL B 52 N TRP B 38
SHEET 4 L 4 GLU B 60 SER B 62 -1 O GLU B 61 N ARG B 53
SHEET 1 M 4 TRP B 82 VAL B 85 0
SHEET 2 M 4 LEU B 93 THR B 97 -1 O LEU B 93 N VAL B 85
SHEET 3 M 4 LEU B 104 PHE B 107 -1 O TYR B 105 N PHE B 96
SHEET 4 M 4 ARG B 118 PRO B 119 -1 O ARG B 118 N ALA B 106
SHEET 1 N 4 LEU B 130 LEU B 138 0
SHEET 2 N 4 GLU B 143 PHE B 151 -1 O GLU B 143 N LEU B 138
SHEET 3 N 4 VAL B 159 PRO B 167 -1 O ALA B 164 N CYS B 146
SHEET 4 N 4 ARG B 180 GLU B 181 -1 O ARG B 180 N ALA B 165
SHEET 1 O 3 PHE B 189 VAL B 190 0
SHEET 2 O 3 GLN B 201 TRP B 207 -1 O TRP B 207 N PHE B 189
SHEET 3 O 3 ARG B 194 LEU B 195 -1 N ARG B 194 O VAL B 203
SHEET 1 P 4 PHE B 189 VAL B 190 0
SHEET 2 P 4 GLN B 201 TRP B 207 -1 O TRP B 207 N PHE B 189
SHEET 3 P 4 GLU B 218 VAL B 224 -1 O LYS B 220 N TRP B 204
SHEET 4 P 4 PHE B 230 GLY B 238 -1 O LEU B 237 N LEU B 219
SHEET 1 Q 4 ILE B 244 TRP B 249 0
SHEET 2 Q 4 LEU B 255 THR B 259 -1 O ILE B 256 N GLU B 248
SHEET 3 Q 4 ASN B 266 VAL B 270 -1 O VAL B 270 N LEU B 255
SHEET 4 Q 4 ALA B 277 GLN B 279 -1 O THR B 278 N ARG B 269
SHEET 1 R 4 PHE B 299 PRO B 301 0
SHEET 2 R 4 ILE B 307 HIS B 311 -1 O ALA B 308 N ALA B 300
SHEET 3 R 4 VAL B 317 ASP B 322 -1 O LEU B 321 N ILE B 307
SHEET 4 R 4 GLU B 327 ASP B 330 -1 O VAL B 329 N ILE B 320
SHEET 1 S 4 GLU B 337 SER B 345 0
SHEET 2 S 4 ARG B 348 SER B 355 -1 O VAL B 350 N THR B 343
SHEET 3 S 4 THR B 358 ASP B 366 -1 O LEU B 365 N ALA B 349
SHEET 4 S 4 ALA B 372 GLY B 376 -1 O ARG B 373 N GLU B 364
SHEET 1 T 8 GLN B 392 THR B 397 0
SHEET 2 T 8 GLU B 403 TYR B 409 -1 O ILE B 404 N PHE B 396
SHEET 3 T 8 GLY B 455 ASN B 460 -1 O VAL B 456 N TYR B 409
SHEET 4 T 8 TYR B 426 ALA B 430 1 N MET B 429 O ALA B 457
SHEET 5 T 8 LEU B 505 GLY B 510 1 O ALA B 506 N VAL B 428
SHEET 6 T 8 CYS B 529 LEU B 533 1 O LEU B 533 N GLY B 509
SHEET 7 T 8 PHE B 585 GLY B 590 1 O LEU B 586 N VAL B 532
SHEET 8 T 8 HIS B 615 PHE B 620 1 O LEU B 618 N LEU B 587
CISPEP 1 ALA A 66 PRO A 67 0 0.03
CISPEP 2 HIS A 209 PRO A 210 0 -0.13
CISPEP 3 GLY A 433 PRO A 434 0 0.14
CISPEP 4 ALA B 66 PRO B 67 0 -0.07
CISPEP 5 HIS B 209 PRO B 210 0 -0.19
CISPEP 6 GLY B 433 PRO B 434 0 0.34
SITE 1 AC1 4 ARG A 188 HIS A 209 HOH A1092 HOH A1234
SITE 1 AC2 3 ARG A 261 ALA A 276 ALA A 277
SITE 1 AC3 3 ARG A 223 THR A 225 GLU A 226
SITE 1 AC4 5 ARG B 188 HIS B 209 HOH B1249 HOH B1478
SITE 2 AC4 5 HOH B1781
SITE 1 AC5 4 ARG A 371 ARG B 223 THR B 225 GLU B 226
CRYST1 84.110 142.620 156.300 90.00 90.00 90.00 P 21 21 21 8
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 0.011889 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007012 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006398 0.00000
TER 5028 GLU A 662
TER 10056 GLU B 662
MASTER 320 0 5 31 82 0 6 611088 2 25 102
END |