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HEADER HYDROLASE 27-MAY-11 3AZQ
TITLE CRYSTAL STRUCTURE OF PUROMYCIN HYDROLASE S511A MUTANT COMPLEXED WITH
TITLE 2 PGG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMINOPEPTIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TRIPEPTIDE PGG;
COMPND 8 CHAIN: C, D;
COMPND 9 ENGINEERED: 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(+);
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: PURCHASED
KEYWDS POP FAMILY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.MATOBA,M.SUGIYAMA
REVDAT 1 27-JUL-11 3AZQ 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. 2.70 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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2399339.730
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 52128
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) : 0.193
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2645
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8128
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE : 0.3670
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 421
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10070
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 510
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 6.87000
REMARK 3 B33 (A**2) : -6.88000
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) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.38
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) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.47
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.90
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) : 1.130 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.900 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.770 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.700 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 22.01
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 3AZQ 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 RCSB029897.
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 : 52360
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.11900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.6000
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) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.40700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.500
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 (%): 62.63
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 42.21500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.15500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 71.34000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.15500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.21500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 71.34000
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 MET A 1
REMARK 465 MET B 1
REMARK 465 GLY C 3
REMARK 465 GLY D 3
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 GLY C 2 CA C O
REMARK 470 GLY D 2 CA C O
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 60.52 -108.39
REMARK 500 ARG A 71 141.74 -173.96
REMARK 500 GLU A 76 -4.15 59.93
REMARK 500 SER A 78 108.33 79.54
REMARK 500 CYS A 146 -172.94 -170.06
REMARK 500 LEU A 237 167.80 174.51
REMARK 500 PRO A 240 0.88 -66.80
REMARK 500 PRO A 251 -19.17 -46.47
REMARK 500 PRO A 272 -7.20 -51.07
REMARK 500 CYS A 281 88.31 -160.00
REMARK 500 GLU A 284 58.10 -93.76
REMARK 500 ALA A 288 -168.91 -162.75
REMARK 500 ALA A 332 -119.88 -92.86
REMARK 500 SER A 413 134.65 -170.83
REMARK 500 ASP A 421 59.08 -96.90
REMARK 500 THR A 435 76.34 -69.38
REMARK 500 ASN A 460 75.02 -101.07
REMARK 500 TYR A 461 174.85 -59.28
REMARK 500 ALA A 511 -120.94 53.93
REMARK 500 TYR A 534 68.63 20.77
REMARK 500 ALA A 653 -77.57 -90.53
REMARK 500 GLU B 45 61.21 -107.01
REMARK 500 PRO B 67 31.54 -93.79
REMARK 500 SER B 78 106.67 81.09
REMARK 500 ASP B 134 70.07 55.96
REMARK 500 LEU B 138 68.41 -117.70
REMARK 500 PRO B 210 46.63 -104.39
REMARK 500 ASP B 252 20.60 -79.94
REMARK 500 PRO B 272 5.01 -63.00
REMARK 500 CYS B 281 75.28 -168.91
REMARK 500 GLU B 284 49.32 -95.76
REMARK 500 GLU B 324 -77.71 -83.72
REMARK 500 ALA B 332 -99.85 -74.71
REMARK 500 ALA B 340 49.05 -82.55
REMARK 500 HIS B 412 140.51 -171.75
REMARK 500 ASP B 421 42.36 -99.37
REMARK 500 THR B 435 82.09 -64.02
REMARK 500 ALA B 440 76.63 -106.46
REMARK 500 VAL B 481 -71.56 -118.37
REMARK 500 ALA B 511 -118.82 51.94
REMARK 500 TYR B 534 64.97 23.50
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 A1277 DISTANCE = 5.22 ANGSTROMS
REMARK 525 HOH B1326 DISTANCE = 5.16 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 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1009
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1007
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1010
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3AZO RELATED DB: PDB
REMARK 900 RELATED ID: 3AZP RELATED DB: PDB
DBREF 3AZQ A 1 662 UNP Q2HXD9 Q2HXD9_STRMO 1 662
DBREF 3AZQ B 1 662 UNP Q2HXD9 Q2HXD9_STRMO 1 662
DBREF 3AZQ C 1 3 PDB 3AZQ 3AZQ 1 3
DBREF 3AZQ D 1 3 PDB 3AZQ 3AZQ 1 3
SEQADV 3AZQ ALA A 511 UNP Q2HXD9 SER 511 ENGINEERED MUTATION
SEQADV 3AZQ 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
SEQRES 1 C 3 PRO GLY GLY
SEQRES 1 D 3 PRO GLY GLY
HET SO4 A1001 5
HET SO4 A1003 5
HET SO4 A1004 5
HET SO4 A1006 5
HET SO4 A1008 5
HET SO4 A1009 5
HET SO4 B1002 5
HET SO4 B1005 5
HET SO4 B1007 5
HET SO4 B1010 5
HETNAM SO4 SULFATE ION
FORMUL 5 SO4 10(O4 S 2-)
FORMUL 15 HOH *510(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 PRO A 139 ARG A 141 5 3
HELIX 4 4 ASP A 175 VAL A 179 5 5
HELIX 5 5 ASP A 384 TYR A 388 5 5
HELIX 6 6 ASP A 443 SER A 451 1 9
HELIX 7 7 GLY A 468 ARG A 474 1 7
HELIX 8 8 VAL A 481 GLU A 497 1 17
HELIX 9 9 ALA A 511 SER A 523 1 13
HELIX 10 10 ASP A 538 ASP A 544 1 7
HELIX 11 11 HIS A 548 ARG A 553 5 6
HELIX 12 12 TYR A 554 ILE A 559 1 6
HELIX 13 13 GLU A 567 ARG A 572 1 6
HELIX 14 14 PRO A 574 VAL A 581 5 8
HELIX 15 15 PRO A 598 ALA A 609 1 12
HELIX 16 16 ARG A 629 PHE A 648 1 20
HELIX 17 17 ASP B 15 ARG B 22 1 8
HELIX 18 18 ARG B 73 TYR B 77 5 5
HELIX 19 19 PRO B 139 ARG B 141 5 3
HELIX 20 20 ASP B 175 VAL B 179 5 5
HELIX 21 21 ASP B 384 TYR B 388 5 5
HELIX 22 22 ASP B 443 SER B 451 1 9
HELIX 23 23 GLY B 468 ARG B 474 1 7
HELIX 24 24 VAL B 481 GLU B 497 1 17
HELIX 25 25 ALA B 511 THR B 524 1 14
HELIX 26 26 ASP B 538 ASP B 544 1 7
HELIX 27 27 HIS B 548 SER B 552 5 5
HELIX 28 28 ARG B 553 GLY B 560 1 8
HELIX 29 29 GLU B 567 ARG B 572 1 6
HELIX 30 30 ALA B 573 VAL B 581 5 9
HELIX 31 31 PRO B 598 ALA B 609 1 12
HELIX 32 32 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 VAL A 52 N TRP A 38
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 GLU A 143 N LEU A 138
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 GLU A 218 VAL A 224 -1 O LYS A 220 N TRP A 204
SHEET 4 F 4 PHE A 230 GLY A 238 -1 O LEU A 236 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 GLY A 319 N VAL A 309
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 ALA A 354 -1 O VAL A 352 N ALA A 339
SHEET 3 I 4 GLU A 361 ASP A 366 -1 O GLU A 361 N ALA A 353
SHEET 4 I 4 ALA A 372 GLY A 376 -1 O ILE A 375 N VAL A 362
SHEET 1 J 8 GLN A 392 THR A 397 0
SHEET 2 J 8 GLU A 403 TYR A 409 -1 O ILE A 404 N PHE A 396
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 ALA A 457
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 LEU A 618 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 149 N ARG B 131
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 THR B 217 VAL B 224 -1 O LYS B 220 N TRP B 204
SHEET 4 P 4 PHE B 230 GLY B 239 -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 LEU B 321 -1 O LEU B 321 N ILE B 307
SHEET 4 R 4 LEU B 328 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 352 N ALA B 339
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 ILE B 375 N VAL B 362
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 -0.15
CISPEP 2 HIS A 209 PRO A 210 0 -0.04
CISPEP 3 GLY A 433 PRO A 434 0 0.33
CISPEP 4 ALA B 66 PRO B 67 0 0.06
CISPEP 5 HIS B 209 PRO B 210 0 -0.50
CISPEP 6 GLY B 433 PRO B 434 0 0.11
SITE 1 AC1 4 ARG A 188 HIS A 209 HOH A1127 HOH A1185
SITE 1 AC2 4 ARG A 261 GLY A 275 ALA A 276 ALA A 277
SITE 1 AC3 4 ARG A 223 THR A 225 GLU A 226 HOH A1199
SITE 1 AC4 4 HIS A 407 ARG A 437 ASN A 460 TYR A 467
SITE 1 AC5 6 LEU A 18 SER A 21 ARG A 22 ARG A 402
SITE 2 AC5 6 GLU A 403 ARG A 474
SITE 1 AC6 5 ARG A 25 ALA A 27 CYS A 28 ALA A 340
SITE 2 AC6 5 THR A 341
SITE 1 AC7 2 THR B 262 ARG B 282
SITE 1 AC8 3 ARG B 188 HIS B 209 HOH B1177
SITE 1 AC9 4 ARG A 371 ARG B 223 THR B 225 GLU B 226
SITE 1 BC1 1 ARG B 553
CRYST1 84.430 142.680 156.310 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 0.011844 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007009 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006398 0.00000
TER 5028 GLU A 662
TER 10056 GLU B 662
TER 10065 GLY C 2
TER 10074 GLY D 2
MASTER 357 0 10 32 82 0 12 610630 4 50 104
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