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HEADER HYDROLASE 31-JAN-18 6CAN
TITLE PROLYL OLIGOPEPTIDASE MUTANT S477C FROM PYROCOCCUS FURIOSUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL ENDOPEPTIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 3 ORGANISM_TAXID: 2261;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS PROLYL OLIGOPEPTIDASE, HYPERTHERMOSTABLE, ALPHA/BETA HYDROLASE,
KEYWDS 2 PEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.ELLIS-GUARDIOLA,J.C.LEWIS,N.SUKUMAR
REVDAT 1 06-FEB-19 6CAN 0
JRNL AUTH K.ELLIS-GUARDIOLA,N.SUKUMAR,J.LEWIS
JRNL TITL PROLYL OLIGOPEPTIDASE MUTANT S477C FROM PYROCOCCUS FURIOSUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12_2829)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 3 NUMBER OF REFLECTIONS : 53366
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 932
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 2.3200 - 2.2000 0.76 6037 100 0.2700 0.3400
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.460
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 10268
REMARK 3 ANGLE : 1.235 13862
REMARK 3 CHIRALITY : 0.059 1462
REMARK 3 PLANARITY : 0.004 1776
REMARK 3 DIHEDRAL : 16.915 3874
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6CAN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1000232424.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53493
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.14400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.77200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 2BKL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% W/W PEG 8000 100 MM TRIS PH 9.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 89.38200
REMARK 290 SMTRY3 2 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 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 GLY A 594
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 59 CD CE NZ
REMARK 480 ARG A 89 CG CD NE CZ NH1 NH2
REMARK 480 GLU A 132 CB CG CD OE1 OE2
REMARK 480 ARG A 158 CD NE CZ NH1 NH2
REMARK 480 GLU A 241 CG CD OE1 OE2
REMARK 480 ARG A 289 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 352 CG CD CE NZ
REMARK 480 LYS B 18 CE NZ
REMARK 480 LYS B 138 CG CD CE NZ
REMARK 480 LYS B 148 CB CG CD CE NZ
REMARK 480 ARG B 155 CD NE CZ NH1 NH2
REMARK 480 ARG B 158 CG CD NE CZ NH1 NH2
REMARK 480 LYS B 159 CG CD CE NZ
REMARK 480 GLU B 333 CG CD OE1 OE2
REMARK 480 LYS B 589 CG CD CE NZ
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 LYS A 68 -133.28 45.98
REMARK 500 ILE A 144 108.24 -58.82
REMARK 500 LYS A 148 -128.84 53.55
REMARK 500 TYR A 151 147.42 -179.56
REMARK 500 LEU A 189 106.76 -59.83
REMARK 500 ASN A 215 -21.30 -142.25
REMARK 500 LYS A 352 -59.37 -134.13
REMARK 500 TYR A 401 -79.32 -133.52
REMARK 500 ASN A 405 19.96 59.10
REMARK 500 ARG A 447 -121.67 51.97
REMARK 500 CYS A 477 -120.54 60.25
REMARK 500 TYR A 501 58.60 27.34
REMARK 500 TYR A 513 -133.58 53.76
REMARK 500 SER A 590 -154.56 -91.86
REMARK 500 ASP B 3 114.05 -165.21
REMARK 500 LYS B 68 -122.25 52.09
REMARK 500 GLN B 98 -66.50 -100.86
REMARK 500 LYS B 148 -129.06 45.39
REMARK 500 ARG B 289 -120.51 59.18
REMARK 500 ASP B 331 -161.14 -129.74
REMARK 500 LYS B 352 -81.20 -107.30
REMARK 500 TYR B 401 -72.59 -128.21
REMARK 500 ASN B 405 19.69 55.86
REMARK 500 ARG B 447 -125.51 49.98
REMARK 500 CYS B 477 -123.75 61.95
REMARK 500 TYR B 501 59.05 24.40
REMARK 500 ILE B 504 -43.30 -136.25
REMARK 500 TYR B 513 -127.26 56.28
REMARK 500 SER B 538 109.48 -45.18
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 A1221 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH A1222 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH A1223 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH A1224 DISTANCE = 6.69 ANGSTROMS
REMARK 525 HOH A1225 DISTANCE = 6.74 ANGSTROMS
REMARK 525 HOH A1226 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH A1227 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH A1228 DISTANCE = 6.97 ANGSTROMS
REMARK 525 HOH A1229 DISTANCE = 6.98 ANGSTROMS
REMARK 525 HOH A1230 DISTANCE = 7.24 ANGSTROMS
REMARK 525 HOH A1231 DISTANCE = 7.52 ANGSTROMS
REMARK 525 HOH A1232 DISTANCE = 7.57 ANGSTROMS
REMARK 525 HOH A1233 DISTANCE = 7.91 ANGSTROMS
REMARK 525 HOH A1234 DISTANCE = 8.16 ANGSTROMS
REMARK 525 HOH A1235 DISTANCE = 8.34 ANGSTROMS
REMARK 525 HOH B1198 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH B1199 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH B1200 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH B1201 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH B1202 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH B1203 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH B1204 DISTANCE = 6.87 ANGSTROMS
REMARK 525 HOH B1205 DISTANCE = 7.02 ANGSTROMS
REMARK 525 HOH B1206 DISTANCE = 7.11 ANGSTROMS
REMARK 525 HOH B1207 DISTANCE = 7.54 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 703
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5T88 RELATED DB: PDB
REMARK 900 PROLYL OLIGOPEPTIDASE FROM PYROCOCCUS FURIOSUS
DBREF 6CAN A 1 616 UNP Q51714 Q51714_9EURY 1 616
DBREF 6CAN B 1 616 UNP Q51714 Q51714_9EURY 1 616
SEQADV 6CAN LEU A 464 UNP Q51714 ARG 464 VARIANT
SEQADV 6CAN CYS A 477 UNP Q51714 SER 477 ENGINEERED MUTATION
SEQADV 6CAN LEU B 464 UNP Q51714 ARG 464 VARIANT
SEQADV 6CAN CYS B 477 UNP Q51714 SER 477 ENGINEERED MUTATION
SEQRES 1 A 616 MET GLU ASP PRO TYR ILE TRP MET GLU ASN LEU GLU ASP
SEQRES 2 A 616 GLU ARG VAL LEU LYS ILE ILE GLU GLU GLU ASN LYS ARG
SEQRES 3 A 616 PHE ARG GLU PHE ILE GLY GLU LEU SER ASP LYS LEU PHE
SEQRES 4 A 616 PRO GLU VAL TRP GLU GLN PHE SER GLN PRO THR ILE GLY
SEQRES 5 A 616 MET ALA ARG ILE THR LYS LYS GLY ILE ILE ALA SER TYR
SEQRES 6 A 616 SER GLU LYS ASP ARG VAL VAL ILE LYS TRP PHE ASN GLY
SEQRES 7 A 616 ASP VAL ILE VAL ASP SER LYS GLU LEU GLU ARG GLU VAL
SEQRES 8 A 616 GLY ASP GLU VAL LEU LEU GLN GLY PHE THR THR ASP GLU
SEQRES 9 A 616 GLU GLY GLU LYS LEU ALA TYR SER PHE SER ILE GLY GLY
SEQRES 10 A 616 ALA ASP GLU GLY ILE THR ARG ILE ILE ASP LEU LYS THR
SEQRES 11 A 616 GLY GLU VAL ILE GLU GLU ILE LYS PRO SER ILE TRP ASN
SEQRES 12 A 616 ILE THR PHE LEU LYS ASP GLY TYR TYR PHE THR ARG PHE
SEQRES 13 A 616 TYR ARG LYS GLU LYS THR PRO ASP GLY VAL ASN PRO PRO
SEQRES 14 A 616 ALA ALA ARG MET PHE TRP LYS ASP ARG GLU GLY GLU ARG
SEQRES 15 A 616 MET VAL PHE GLY GLU GLY LEU THR SER GLY TYR PHE MET
SEQRES 16 A 616 SER ILE ARG LYS SER SER ASP GLY LYS PHE ALA ILE VAL
SEQRES 17 A 616 THR LEU THR TYR GLY TRP ASN GLN GLY GLU VAL TYR ILE
SEQRES 18 A 616 GLY PRO ILE ASP ASN PRO GLN GLU TRP LYS LYS VAL TYR
SEQRES 19 A 616 SER ALA SER VAL PRO VAL GLU ALA ILE ASP VAL VAL ASN
SEQRES 20 A 616 GLY LYS LEU TYR ILE LEU THR LYS GLU GLY LYS GLY LEU
SEQRES 21 A 616 GLY LYS ILE ILE ALA ILE LYS ASN GLY LYS ILE ASP GLU
SEQRES 22 A 616 VAL ILE PRO GLU GLY GLU PHE PRO LEU GLU TRP ALA VAL
SEQRES 23 A 616 ILE VAL ARG ASP LYS ILE LEU ALA GLY ARG LEU VAL HIS
SEQRES 24 A 616 ALA SER TYR LYS LEU GLU VAL TYR THR LEU ASN GLY GLU
SEQRES 25 A 616 LYS ILE LYS GLU ILE THR PHE ASP VAL PRO GLY SER LEU
SEQRES 26 A 616 TYR PRO LEU ASP LYS ASP GLU GLU ARG VAL LEU LEU ARG
SEQRES 27 A 616 TYR THR SER PHE THR ILE PRO TYR ARG LEU TYR GLU PHE
SEQRES 28 A 616 LYS ASP ASP LEU ARG LEU ILE GLU GLU ARG LYS VAL GLU
SEQRES 29 A 616 GLY GLU PHE ARG VAL GLU GLU ASP PHE ALA THR SER LYS
SEQRES 30 A 616 ASP GLY THR LYS VAL HIS TYR PHE ILE VAL LYS GLY GLU
SEQRES 31 A 616 ARG ASP GLU LYS ARG ALA TRP VAL PHE GLY TYR GLY GLY
SEQRES 32 A 616 PHE ASN ILE ALA LEU THR PRO MET PHE PHE PRO GLN VAL
SEQRES 33 A 616 ILE PRO PHE LEU LYS ARG GLY GLY THR PHE ILE MET ALA
SEQRES 34 A 616 ASN LEU ARG GLY GLY SER GLU TYR GLY GLU GLU TRP HIS
SEQRES 35 A 616 ARG ALA GLY MET ARG GLU ASN LYS GLN ASN VAL PHE ASP
SEQRES 36 A 616 ASP PHE ILE ALA VAL LEU GLU LYS LEU LYS LYS GLU GLY
SEQRES 37 A 616 TYR LYS VAL ALA ALA TRP GLY ARG CYS ASN GLY GLY LEU
SEQRES 38 A 616 LEU VAL SER ALA THR LEU THR GLN ARG PRO ASP VAL MET
SEQRES 39 A 616 ASP SER ALA LEU ILE GLY TYR PRO VAL ILE ASP MET LEU
SEQRES 40 A 616 ARG PHE HIS LYS LEU TYR ILE GLY SER VAL TRP ILE PRO
SEQRES 41 A 616 GLU TYR GLY ASN PRO GLU ASP PRO LYS ASP ARG GLU PHE
SEQRES 42 A 616 LEU LEU LYS TYR SER PRO TYR HIS ASN VAL ASP PRO LYS
SEQRES 43 A 616 LYS LYS TYR PRO PRO THR LEU ILE TYR THR GLY LEU HIS
SEQRES 44 A 616 ASP ASP ARG VAL HIS PRO ALA HIS ALA LEU LYS PHE PHE
SEQRES 45 A 616 MET LYS LEU LYS GLU ILE GLY ALA PRO VAL TYR LEU ARG
SEQRES 46 A 616 VAL GLU THR LYS SER GLY HIS MET GLY ALA SER PRO GLU
SEQRES 47 A 616 THR ARG ALA ARG GLU LEU THR ASP LEU LEU ALA PHE VAL
SEQRES 48 A 616 LEU LYS THR LEU SER
SEQRES 1 B 616 MET GLU ASP PRO TYR ILE TRP MET GLU ASN LEU GLU ASP
SEQRES 2 B 616 GLU ARG VAL LEU LYS ILE ILE GLU GLU GLU ASN LYS ARG
SEQRES 3 B 616 PHE ARG GLU PHE ILE GLY GLU LEU SER ASP LYS LEU PHE
SEQRES 4 B 616 PRO GLU VAL TRP GLU GLN PHE SER GLN PRO THR ILE GLY
SEQRES 5 B 616 MET ALA ARG ILE THR LYS LYS GLY ILE ILE ALA SER TYR
SEQRES 6 B 616 SER GLU LYS ASP ARG VAL VAL ILE LYS TRP PHE ASN GLY
SEQRES 7 B 616 ASP VAL ILE VAL ASP SER LYS GLU LEU GLU ARG GLU VAL
SEQRES 8 B 616 GLY ASP GLU VAL LEU LEU GLN GLY PHE THR THR ASP GLU
SEQRES 9 B 616 GLU GLY GLU LYS LEU ALA TYR SER PHE SER ILE GLY GLY
SEQRES 10 B 616 ALA ASP GLU GLY ILE THR ARG ILE ILE ASP LEU LYS THR
SEQRES 11 B 616 GLY GLU VAL ILE GLU GLU ILE LYS PRO SER ILE TRP ASN
SEQRES 12 B 616 ILE THR PHE LEU LYS ASP GLY TYR TYR PHE THR ARG PHE
SEQRES 13 B 616 TYR ARG LYS GLU LYS THR PRO ASP GLY VAL ASN PRO PRO
SEQRES 14 B 616 ALA ALA ARG MET PHE TRP LYS ASP ARG GLU GLY GLU ARG
SEQRES 15 B 616 MET VAL PHE GLY GLU GLY LEU THR SER GLY TYR PHE MET
SEQRES 16 B 616 SER ILE ARG LYS SER SER ASP GLY LYS PHE ALA ILE VAL
SEQRES 17 B 616 THR LEU THR TYR GLY TRP ASN GLN GLY GLU VAL TYR ILE
SEQRES 18 B 616 GLY PRO ILE ASP ASN PRO GLN GLU TRP LYS LYS VAL TYR
SEQRES 19 B 616 SER ALA SER VAL PRO VAL GLU ALA ILE ASP VAL VAL ASN
SEQRES 20 B 616 GLY LYS LEU TYR ILE LEU THR LYS GLU GLY LYS GLY LEU
SEQRES 21 B 616 GLY LYS ILE ILE ALA ILE LYS ASN GLY LYS ILE ASP GLU
SEQRES 22 B 616 VAL ILE PRO GLU GLY GLU PHE PRO LEU GLU TRP ALA VAL
SEQRES 23 B 616 ILE VAL ARG ASP LYS ILE LEU ALA GLY ARG LEU VAL HIS
SEQRES 24 B 616 ALA SER TYR LYS LEU GLU VAL TYR THR LEU ASN GLY GLU
SEQRES 25 B 616 LYS ILE LYS GLU ILE THR PHE ASP VAL PRO GLY SER LEU
SEQRES 26 B 616 TYR PRO LEU ASP LYS ASP GLU GLU ARG VAL LEU LEU ARG
SEQRES 27 B 616 TYR THR SER PHE THR ILE PRO TYR ARG LEU TYR GLU PHE
SEQRES 28 B 616 LYS ASP ASP LEU ARG LEU ILE GLU GLU ARG LYS VAL GLU
SEQRES 29 B 616 GLY GLU PHE ARG VAL GLU GLU ASP PHE ALA THR SER LYS
SEQRES 30 B 616 ASP GLY THR LYS VAL HIS TYR PHE ILE VAL LYS GLY GLU
SEQRES 31 B 616 ARG ASP GLU LYS ARG ALA TRP VAL PHE GLY TYR GLY GLY
SEQRES 32 B 616 PHE ASN ILE ALA LEU THR PRO MET PHE PHE PRO GLN VAL
SEQRES 33 B 616 ILE PRO PHE LEU LYS ARG GLY GLY THR PHE ILE MET ALA
SEQRES 34 B 616 ASN LEU ARG GLY GLY SER GLU TYR GLY GLU GLU TRP HIS
SEQRES 35 B 616 ARG ALA GLY MET ARG GLU ASN LYS GLN ASN VAL PHE ASP
SEQRES 36 B 616 ASP PHE ILE ALA VAL LEU GLU LYS LEU LYS LYS GLU GLY
SEQRES 37 B 616 TYR LYS VAL ALA ALA TRP GLY ARG CYS ASN GLY GLY LEU
SEQRES 38 B 616 LEU VAL SER ALA THR LEU THR GLN ARG PRO ASP VAL MET
SEQRES 39 B 616 ASP SER ALA LEU ILE GLY TYR PRO VAL ILE ASP MET LEU
SEQRES 40 B 616 ARG PHE HIS LYS LEU TYR ILE GLY SER VAL TRP ILE PRO
SEQRES 41 B 616 GLU TYR GLY ASN PRO GLU ASP PRO LYS ASP ARG GLU PHE
SEQRES 42 B 616 LEU LEU LYS TYR SER PRO TYR HIS ASN VAL ASP PRO LYS
SEQRES 43 B 616 LYS LYS TYR PRO PRO THR LEU ILE TYR THR GLY LEU HIS
SEQRES 44 B 616 ASP ASP ARG VAL HIS PRO ALA HIS ALA LEU LYS PHE PHE
SEQRES 45 B 616 MET LYS LEU LYS GLU ILE GLY ALA PRO VAL TYR LEU ARG
SEQRES 46 B 616 VAL GLU THR LYS SER GLY HIS MET GLY ALA SER PRO GLU
SEQRES 47 B 616 THR ARG ALA ARG GLU LEU THR ASP LEU LEU ALA PHE VAL
SEQRES 48 B 616 LEU LYS THR LEU SER
HET CL A 701 1
HET CL A 702 1
HET CL A 703 1
HET CL B 701 1
HET CL B 702 1
HET CL B 703 1
HETNAM CL CHLORIDE ION
FORMUL 3 CL 6(CL 1-)
FORMUL 9 HOH *842(H2 O)
HELIX 1 AA1 TYR A 5 ASN A 10 5 6
HELIX 2 AA2 ASP A 13 SER A 47 1 35
HELIX 3 AA3 GLU A 86 GLU A 90 5 5
HELIX 4 AA4 ASN A 226 TRP A 230 5 5
HELIX 5 AA5 PHE A 413 GLN A 415 5 3
HELIX 6 AA6 VAL A 416 ARG A 422 1 7
HELIX 7 AA7 GLY A 438 ALA A 444 1 7
HELIX 8 AA8 GLY A 445 GLU A 448 5 4
HELIX 9 AA9 ASN A 449 GLU A 467 1 19
HELIX 10 AB1 CYS A 477 ARG A 490 1 14
HELIX 11 AB2 PRO A 491 MET A 494 5 4
HELIX 12 AB3 ARG A 508 LEU A 512 5 5
HELIX 13 AB4 ILE A 514 VAL A 517 5 4
HELIX 14 AB5 TRP A 518 GLY A 523 1 6
HELIX 15 AB6 ASP A 527 SER A 538 1 12
HELIX 16 AB7 PRO A 539 ASN A 542 5 4
HELIX 17 AB8 PRO A 565 ILE A 578 1 14
HELIX 18 AB9 SER A 596 SER A 616 1 21
HELIX 19 AC1 TYR B 5 ASN B 10 5 6
HELIX 20 AC2 ASP B 13 GLN B 48 1 36
HELIX 21 AC3 ASN B 226 TRP B 230 5 5
HELIX 22 AC4 PHE B 413 GLN B 415 5 3
HELIX 23 AC5 VAL B 416 LYS B 421 1 6
HELIX 24 AC6 GLY B 438 ALA B 444 1 7
HELIX 25 AC7 GLY B 445 GLU B 448 5 4
HELIX 26 AC8 ASN B 449 GLU B 467 1 19
HELIX 27 AC9 CYS B 477 ARG B 490 1 14
HELIX 28 AD1 PRO B 491 MET B 494 5 4
HELIX 29 AD2 ARG B 508 LEU B 512 5 5
HELIX 30 AD3 ILE B 514 VAL B 517 5 4
HELIX 31 AD4 TRP B 518 GLY B 523 1 6
HELIX 32 AD5 ASP B 527 SER B 538 1 12
HELIX 33 AD6 PRO B 539 ASN B 542 5 4
HELIX 34 AD7 PRO B 565 ILE B 578 1 14
HELIX 35 AD8 SER B 596 LEU B 615 1 20
SHEET 1 AA1 4 THR A 50 THR A 57 0
SHEET 2 AA1 4 GLY A 60 GLU A 67 -1 O SER A 66 N THR A 50
SHEET 3 AA1 4 ARG A 70 TRP A 75 -1 O ARG A 70 N GLU A 67
SHEET 4 AA1 4 VAL A 80 VAL A 82 -1 O VAL A 82 N ILE A 73
SHEET 1 AA2 4 VAL A 95 THR A 102 0
SHEET 2 AA2 4 LYS A 108 ILE A 115 -1 O SER A 112 N GLN A 98
SHEET 3 AA2 4 ILE A 122 ASP A 127 -1 O ILE A 126 N LEU A 109
SHEET 4 AA2 4 VAL A 133 ILE A 137 -1 O ILE A 137 N THR A 123
SHEET 1 AA3 4 TRP A 142 LEU A 147 0
SHEET 2 AA3 4 GLY A 150 TYR A 157 -1 O THR A 154 N TRP A 142
SHEET 3 AA3 4 ALA A 170 LYS A 176 -1 O ALA A 170 N TYR A 157
SHEET 4 AA3 4 GLU A 181 PHE A 185 -1 O PHE A 185 N MET A 173
SHEET 1 AA4 4 TYR A 193 LYS A 199 0
SHEET 2 AA4 4 PHE A 205 TYR A 212 -1 O THR A 211 N PHE A 194
SHEET 3 AA4 4 GLN A 216 PRO A 223 -1 O GLY A 222 N ALA A 206
SHEET 4 AA4 4 LYS A 231 SER A 235 -1 O TYR A 234 N VAL A 219
SHEET 1 AA5 4 VAL A 240 VAL A 246 0
SHEET 2 AA5 4 LYS A 249 THR A 254 -1 O TYR A 251 N ILE A 243
SHEET 3 AA5 4 LYS A 262 LYS A 267 -1 O ILE A 264 N ILE A 252
SHEET 4 AA5 4 LYS A 270 ILE A 275 -1 O ASP A 272 N ALA A 265
SHEET 1 AA6 4 LEU A 282 ILE A 287 0
SHEET 2 AA6 4 LYS A 291 VAL A 298 -1 O LEU A 293 N VAL A 286
SHEET 3 AA6 4 SER A 301 THR A 308 -1 O TYR A 307 N ILE A 292
SHEET 4 AA6 4 LYS A 313 ILE A 317 -1 O ILE A 317 N LEU A 304
SHEET 1 AA7 4 SER A 324 LYS A 330 0
SHEET 2 AA7 4 VAL A 335 SER A 341 -1 O LEU A 336 N LEU A 328
SHEET 3 AA7 4 ILE A 344 PHE A 351 -1 O TYR A 349 N LEU A 337
SHEET 4 AA7 4 LEU A 355 ARG A 361 -1 O ARG A 361 N TYR A 346
SHEET 1 AA8 8 ARG A 368 THR A 375 0
SHEET 2 AA8 8 LYS A 381 LYS A 388 -1 O VAL A 382 N ALA A 374
SHEET 3 AA8 8 THR A 425 ALA A 429 -1 O PHE A 426 N VAL A 387
SHEET 4 AA8 8 ARG A 395 PHE A 399 1 N PHE A 399 O ILE A 427
SHEET 5 AA8 8 LYS A 470 ARG A 476 1 O LYS A 470 N ALA A 396
SHEET 6 AA8 8 SER A 496 GLY A 500 1 O LEU A 498 N ALA A 473
SHEET 7 AA8 8 THR A 552 GLY A 557 1 O LEU A 553 N ILE A 499
SHEET 8 AA8 8 VAL A 582 GLU A 587 1 O GLU A 587 N THR A 556
SHEET 1 AA9 4 THR B 50 THR B 57 0
SHEET 2 AA9 4 GLY B 60 GLU B 67 -1 O ILE B 62 N ARG B 55
SHEET 3 AA9 4 ARG B 70 TRP B 75 -1 O ARG B 70 N GLU B 67
SHEET 4 AA9 4 VAL B 80 ASP B 83 -1 O ILE B 81 N ILE B 73
SHEET 1 AB1 4 VAL B 95 THR B 102 0
SHEET 2 AB1 4 LYS B 108 ILE B 115 -1 O ALA B 110 N THR B 101
SHEET 3 AB1 4 ILE B 122 ASP B 127 -1 O ILE B 126 N LEU B 109
SHEET 4 AB1 4 GLU B 135 ILE B 137 -1 O ILE B 137 N THR B 123
SHEET 1 AB2 4 TRP B 142 LEU B 147 0
SHEET 2 AB2 4 GLY B 150 TYR B 157 -1 O GLY B 150 N LEU B 147
SHEET 3 AB2 4 ALA B 170 LYS B 176 -1 O PHE B 174 N PHE B 153
SHEET 4 AB2 4 ARG B 182 PHE B 185 -1 O VAL B 184 N MET B 173
SHEET 1 AB3 4 TYR B 193 LYS B 199 0
SHEET 2 AB3 4 PHE B 205 TYR B 212 -1 O THR B 211 N PHE B 194
SHEET 3 AB3 4 GLY B 217 PRO B 223 -1 O GLY B 222 N ALA B 206
SHEET 4 AB3 4 LYS B 231 ALA B 236 -1 O VAL B 233 N VAL B 219
SHEET 1 AB4 4 GLU B 241 VAL B 246 0
SHEET 2 AB4 4 LYS B 249 THR B 254 -1 O TYR B 251 N ILE B 243
SHEET 3 AB4 4 LYS B 262 LYS B 267 -1 O LYS B 262 N THR B 254
SHEET 4 AB4 4 LYS B 270 ILE B 275 -1 O ASP B 272 N ALA B 265
SHEET 1 AB5 4 LEU B 282 VAL B 288 0
SHEET 2 AB5 4 LYS B 291 VAL B 298 -1 O LEU B 293 N VAL B 286
SHEET 3 AB5 4 SER B 301 THR B 308 -1 O TYR B 307 N ILE B 292
SHEET 4 AB5 4 LYS B 313 ILE B 317 -1 O ILE B 314 N VAL B 306
SHEET 1 AB6 4 SER B 324 LYS B 330 0
SHEET 2 AB6 4 VAL B 335 THR B 340 -1 O ARG B 338 N TYR B 326
SHEET 3 AB6 4 TYR B 346 PHE B 351 -1 O ARG B 347 N TYR B 339
SHEET 4 AB6 4 LEU B 355 ARG B 361 -1 O GLU B 359 N LEU B 348
SHEET 1 AB7 8 ARG B 368 THR B 375 0
SHEET 2 AB7 8 LYS B 381 LYS B 388 -1 O ILE B 386 N GLU B 370
SHEET 3 AB7 8 GLY B 424 ALA B 429 -1 O MET B 428 N PHE B 385
SHEET 4 AB7 8 ARG B 395 PHE B 399 1 N ARG B 395 O THR B 425
SHEET 5 AB7 8 LYS B 470 ARG B 476 1 O TRP B 474 N VAL B 398
SHEET 6 AB7 8 SER B 496 GLY B 500 1 O LEU B 498 N ALA B 473
SHEET 7 AB7 8 THR B 552 GLY B 557 1 O LEU B 553 N ILE B 499
SHEET 8 AB7 8 VAL B 582 GLU B 587 1 O TYR B 583 N THR B 552
CISPEP 1 LYS A 138 PRO A 139 0 1.93
CISPEP 2 PRO A 168 PRO A 169 0 -3.13
CISPEP 3 LYS B 138 PRO B 139 0 1.02
CISPEP 4 PRO B 168 PRO B 169 0 -0.03
SITE 1 AC1 3 ARG A 476 TYR A 555 ARG A 600
SITE 1 AC2 3 TYR A 401 PHE A 404 HOH A 811
SITE 1 AC3 4 ARG A 476 TYR A 501 MET A 593 GLU A 603
SITE 1 AC4 3 ARG B 476 TYR B 555 ARG B 600
SITE 1 AC5 2 CYS B 477 HOH B1076
SITE 1 AC6 5 ARG B 476 TYR B 501 ARG B 600 GLU B 603
SITE 2 AC6 5 HOH B1044
CRYST1 56.292 178.764 59.293 90.00 104.35 90.00 P 1 21 1 4
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 0.017765 0.000000 0.004545 0.00000
SCALE2 0.000000 0.005594 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017409 0.00000
TER 5010 SER A 616
TER 10020 SER B 616
MASTER 332 0 6 35 72 0 7 610866 2 0 96
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