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HEADER HYDROLASE 31-AUG-09 3IUN
TITLE APPEP_D622N OPENED STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL ENDOPEPTIDASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AEROMONAS PUNCTATA;
SOURCE 3 ORGANISM_COMMON: AEROMONAS CAVIAE;
SOURCE 4 ORGANISM_TAXID: 648;
SOURCE 5 GENE: PROLYL ENDOPEPTIDASE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS PROLYL ENDOPEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.K.CHIU
REVDAT 1 05-MAY-10 3IUN 0
JRNL AUTH M.LI,C.CHEN,D.R.DAVIES,T.K.CHIU
JRNL TITL AN INDUCED-FIT MECHANISM FOR PROLYL ENDOPEPTIDASE
JRNL REF J.BIOL.CHEM. 2010
JRNL REFN ESSN 1083-351X
REMARK 2
REMARK 2 RESOLUTION. 2.40 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1654523.310
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 35888
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) : 0.206
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1879
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.49
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3204
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE : 0.2950
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 173
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5306
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 231
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.74000
REMARK 3 B22 (A**2) : 13.72000
REMARK 3 B33 (A**2) : -12.98000
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) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.25
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) : 0.36
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.29
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) : 24.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.71
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) : 1.440 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.380 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.080 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.060 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 42.87
REMARK 3
REMARK 3 NCS MODEL : NONE
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 : GOL.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : GOL.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3IUN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-SEP-09.
REMARK 100 THE RCSB ID CODE IS RCSB054885.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36350
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.14600
REMARK 200 FOR THE DATA SET : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
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) : 0.46300
REMARK 200 FOR SHELL : 4.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: PDB ENTRY 3IUJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8MG/ML PROTEIN IN 20MM HEPES (PH7.5),
REMARK 280 100MM NACL, 5% W/V GLYCEROL, 1MM EDTA, AND 1MM DTT. EQUAL VOLUME
REMARK 280 OF PROTEIN AND PRECIPITANT (20MM MES (PH 6.5), 17% W/V PEG10K)
REMARK 280 WERE EQUILIBRATED BY VAPOR DIFFUSION AT 14C. CRYOSOLUTION IS
REMARK 280 PRECIPITANT PLUS 5% MORE PEG10K AND 20% W/V GLYCEROL., VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 287K
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 31.40500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.44800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.79950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 76.44800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.40500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.79950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: 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 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 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLY A 3
REMARK 465 LYS A 4
REMARK 465 ALA A 5
REMARK 465 ARG A 6
REMARK 465 GLU A 199A
REMARK 465 LEU A 199B
REMARK 465 SER A 199C
REMARK 465 ALA A 655
REMARK 465 GLY A 656
REMARK 465 HIS A 657
REMARK 465 GLY A 658
REMARK 465 ALA A 659
REMARK 465 GLY A 660
REMARK 465 THR A 661
REMARK 465 GLN A 689
REMARK 465 PRO A 690
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 107 -53.53 -19.55
REMARK 500 LYS A 109 -178.54 -58.56
REMARK 500 ASP A 129 -87.42 -112.30
REMARK 500 ALA A 147 -134.22 34.41
REMARK 500 ASP A 194 -99.13 -77.29
REMARK 500 SER A 199 -164.97 -166.16
REMARK 500 ARG A 201 153.21 -35.92
REMARK 500 ASP A 285 -178.58 -178.77
REMARK 500 ALA A 299 90.18 -162.52
REMARK 500 ARG A 302 155.58 71.12
REMARK 500 ASN A 311 71.40 -160.80
REMARK 500 TYR A 354 7.79 -68.63
REMARK 500 PRO A 365 19.27 -61.79
REMARK 500 PRO A 414 59.87 -63.43
REMARK 500 SER A 429 -160.37 -74.26
REMARK 500 TYR A 458 -74.26 -131.63
REMARK 500 ASP A 462 19.71 53.69
REMARK 500 TYR A 494 45.03 -144.00
REMARK 500 GLN A 504 -125.67 38.38
REMARK 500 GLN A 505 22.01 -77.94
REMARK 500 SER A 538 -110.01 64.13
REMARK 500 VAL A 562 45.92 36.45
REMARK 500 ALA A 575 -4.62 66.21
REMARK 500 PRO A 687 -179.86 -50.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 703
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3IUJ RELATED DB: PDB
REMARK 900 APPEP_WT2 OPENED STATE
REMARK 900 RELATED ID: 3IUL RELATED DB: PDB
REMARK 900 APPEP_WT1 OPENED STATE
REMARK 900 RELATED ID: 3IUM RELATED DB: PDB
REMARK 900 APPEP_WTX OPENED STATE
REMARK 900 RELATED ID: 3IUQ RELATED DB: PDB
REMARK 900 APPEP_D622N+PP CLOSED STATE
REMARK 900 RELATED ID: 3IUR RELATED DB: PDB
REMARK 900 APPEP_D266NX+H2H3 OPENED STATE
REMARK 900 RELATED ID: 3IVM RELATED DB: PDB
REMARK 900 APPEP_WT+PP CLOSED STATE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS STATE THAT THESE ARE NOT MUTATIONS, BUT ERROR IN DNA
REMARK 999 SEQUENCING OF THE ORIGINAL DEPOSITED FILE. THEY CONFIRMED THIS WITH
REMARK 999 DNA SEQUENCING
DBREF 3IUN A 1 690 UNP Q9X6R4 Q9X6R4_AERPU 1 690
SEQADV 3IUN GLY A -2 UNP Q9X6R4 EXPRESSION TAG
SEQADV 3IUN SER A -1 UNP Q9X6R4 EXPRESSION TAG
SEQADV 3IUN HIS A 0 UNP Q9X6R4 EXPRESSION TAG
SEQADV 3IUN GLN A 106 UNP Q9X6R4 LYS 106 SEE REMARK 999
SEQADV 3IUN GLN A 325 UNP Q9X6R4 HIS 325 SEE REMARK 999
SEQADV 3IUN GLN A 326 UNP Q9X6R4 ARG 326 SEE REMARK 999
SEQADV 3IUN SER A 334 UNP Q9X6R4 THR 334 SEE REMARK 999
SEQADV 3IUN GLY A 335 UNP Q9X6R4 ALA 335 SEE REMARK 999
SEQADV 3IUN ARG A 348 UNP Q9X6R4 PRO 348 SEE REMARK 999
SEQADV 3IUN THR A 577 UNP Q9X6R4 ALA 577 SEE REMARK 999
SEQADV 3IUN ASN A 622 UNP Q9X6R4 ASP 622 ENGINEERED
SEQRES 1 A 693 GLY SER HIS MET SER GLY LYS ALA ARG LEU HIS TYR PRO
SEQRES 2 A 693 VAL THR ARG GLN GLY GLU GLN VAL ASP HIS TYR PHE GLY
SEQRES 3 A 693 GLN ALA VAL ALA ASP PRO TYR ARG TRP LEU GLU ASP ASP
SEQRES 4 A 693 ARG SER PRO GLU THR GLU ALA TRP VAL LYS ALA GLN ASN
SEQRES 5 A 693 ALA VAL THR GLN ASP TYR LEU ALA GLN ILE PRO TYR ARG
SEQRES 6 A 693 ALA ALA ILE LYS GLU LYS LEU ALA ALA SER TRP ASN TYR
SEQRES 7 A 693 ALA LYS GLU GLY ALA PRO PHE ARG GLU GLY ARG TYR HIS
SEQRES 8 A 693 TYR PHE PHE LYS ASN ASP GLY LEU GLN ASN GLN ASN VAL
SEQRES 9 A 693 LEU TRP ARG GLN GLN GLU GLY LYS PRO ALA GLU VAL PHE
SEQRES 10 A 693 LEU ASP PRO ASN THR LEU SER PRO ASP GLY THR THR ALA
SEQRES 11 A 693 LEU ASP GLN LEU SER PHE SER ARG ASP GLY ARG ILE LEU
SEQRES 12 A 693 ALA TYR SER LEU SER LEU ALA GLY SER ASP TRP ARG GLU
SEQRES 13 A 693 ILE HIS LEU MET ASP VAL GLU SER LYS GLN PRO LEU GLU
SEQRES 14 A 693 THR PRO LEU LYS ASP VAL LYS PHE SER GLY ILE SER TRP
SEQRES 15 A 693 LEU GLY ASN GLU GLY PHE PHE TYR SER SER TYR ASP LYS
SEQRES 16 A 693 PRO ASP GLY SER GLU LEU SER ALA ARG THR ASP GLN HIS
SEQRES 17 A 693 LYS VAL TYR PHE HIS ARG LEU GLY THR ALA GLN GLU ASP
SEQRES 18 A 693 ASP ARG LEU VAL PHE GLY ALA ILE PRO ALA GLN HIS HIS
SEQRES 19 A 693 ARG TYR VAL GLY ALA THR VAL THR GLU ASP ASP ARG PHE
SEQRES 20 A 693 LEU LEU ILE SER ALA ALA ASN SER THR SER GLY ASN ARG
SEQRES 21 A 693 LEU TYR VAL LYS ASP LEU SER GLN GLU ASN ALA PRO LEU
SEQRES 22 A 693 LEU THR VAL GLN GLY ASP LEU ASP ALA ASP VAL SER LEU
SEQRES 23 A 693 VAL ASP ASN LYS GLY SER THR LEU TYR LEU LEU THR ASN
SEQRES 24 A 693 ARG ASP ALA PRO ASN ARG ARG LEU VAL THR VAL ASP ALA
SEQRES 25 A 693 ALA ASN PRO GLY PRO ALA HIS TRP ARG ASP LEU ILE PRO
SEQRES 26 A 693 GLU ARG GLN GLN VAL LEU THR VAL HIS SER GLY SER GLY
SEQRES 27 A 693 TYR LEU PHE ALA GLU TYR MET VAL ASP ALA THR ALA ARG
SEQRES 28 A 693 VAL GLU GLN PHE ASP TYR GLU GLY LYS ARG VAL ARG GLU
SEQRES 29 A 693 VAL ALA LEU PRO GLY LEU GLY SER VAL SER GLY PHE ASN
SEQRES 30 A 693 GLY LYS HIS ASP ASP PRO ALA LEU TYR PHE GLY PHE GLU
SEQRES 31 A 693 ASN TYR ALA GLN PRO PRO THR LEU TYR ARG PHE GLU PRO
SEQRES 32 A 693 LYS SER GLY ALA ILE SER LEU TYR ARG ALA SER ALA ALA
SEQRES 33 A 693 PRO PHE LYS PRO GLU ASP TYR VAL SER GLU GLN ARG PHE
SEQRES 34 A 693 TYR GLN SER LYS ASP GLY THR ARG VAL PRO LEU ILE ILE
SEQRES 35 A 693 SER TYR ARG LYS GLY LEU LYS LEU ASP GLY SER ASN PRO
SEQRES 36 A 693 THR ILE LEU TYR GLY TYR GLY GLY PHE ASP VAL SER LEU
SEQRES 37 A 693 THR PRO SER PHE SER VAL SER VAL ALA ASN TRP LEU ASP
SEQRES 38 A 693 LEU GLY GLY VAL TYR ALA VAL ALA ASN LEU ARG GLY GLY
SEQRES 39 A 693 GLY GLU TYR GLY GLN ALA TRP HIS LEU ALA GLY THR GLN
SEQRES 40 A 693 GLN ASN LYS GLN ASN VAL PHE ASP ASP PHE ILE ALA ALA
SEQRES 41 A 693 ALA GLU TYR LEU LYS ALA GLU GLY TYR THR ARG THR ASP
SEQRES 42 A 693 ARG LEU ALA ILE ARG GLY GLY SER ASN GLY GLY LEU LEU
SEQRES 43 A 693 VAL GLY ALA VAL MET THR GLN ARG PRO ASP LEU MET ARG
SEQRES 44 A 693 VAL ALA LEU PRO ALA VAL GLY VAL LEU ASP MET LEU ARG
SEQRES 45 A 693 TYR HIS THR PHE THR ALA GLY THR GLY TRP ALA TYR ASP
SEQRES 46 A 693 TYR GLY THR SER ALA ASP SER GLU ALA MET PHE ASP TYR
SEQRES 47 A 693 LEU LYS GLY TYR SER PRO LEU HIS ASN VAL ARG PRO GLY
SEQRES 48 A 693 VAL SER TYR PRO SER THR MET VAL THR THR ALA ASP HIS
SEQRES 49 A 693 ASN ASP ARG VAL VAL PRO ALA HIS SER PHE LYS PHE ALA
SEQRES 50 A 693 ALA THR LEU GLN ALA ASP ASN ALA GLY PRO HIS PRO GLN
SEQRES 51 A 693 LEU ILE ARG ILE GLU THR ASN ALA GLY HIS GLY ALA GLY
SEQRES 52 A 693 THR PRO VAL ALA LYS LEU ILE GLU GLN SER ALA ASP ILE
SEQRES 53 A 693 TYR ALA PHE THR LEU TYR GLU MET GLY TYR ARG GLU LEU
SEQRES 54 A 693 PRO ARG GLN PRO
HET GOL A 703 6
HETNAM GOL GLYCEROL
FORMUL 2 GOL C3 H8 O3
FORMUL 3 HOH *231(H2 O)
HELIX 1 1 TYR A 30 ASP A 35 5 6
HELIX 2 2 SER A 38 ALA A 57 1 20
HELIX 3 3 TYR A 61 TRP A 73 1 13
HELIX 4 4 ASP A 116 SER A 121 5 6
HELIX 5 5 ALA A 215 ASP A 219 5 5
HELIX 6 6 ILE A 226 HIS A 230 5 5
HELIX 7 7 GLY A 313 TRP A 317 5 5
HELIX 8 8 LYS A 416 GLU A 418 5 3
HELIX 9 9 SER A 470 ASP A 478 1 9
HELIX 10 10 TYR A 494 ALA A 501 1 8
HELIX 11 11 GLY A 502 ASN A 506 5 5
HELIX 12 12 LYS A 507 GLU A 524 1 18
HELIX 13 13 ARG A 528 ASP A 530 5 3
HELIX 14 14 SER A 538 ARG A 551 1 14
HELIX 15 15 ARG A 569 PHE A 573 5 5
HELIX 16 16 ALA A 575 GLY A 578 5 4
HELIX 17 17 TRP A 579 GLY A 584 1 6
HELIX 18 18 SER A 589 SER A 600 1 12
HELIX 19 19 SER A 600 VAL A 605 1 6
HELIX 20 20 PRO A 627 ASN A 641 1 15
HELIX 21 21 PRO A 662 MET A 681 1 20
SHEET 1 A 2 VAL A 18 TYR A 21 0
SHEET 2 A 2 GLN A 24 ALA A 27 -1 O VAL A 26 N ASP A 19
SHEET 1 B 3 LYS A 77 GLU A 78 0
SHEET 2 B 3 TYR A 87 ASN A 93 -1 O ASN A 93 N LYS A 77
SHEET 3 B 3 PHE A 82 GLU A 84 -1 N PHE A 82 O TYR A 89
SHEET 1 C 4 LYS A 77 GLU A 78 0
SHEET 2 C 4 TYR A 87 ASN A 93 -1 O ASN A 93 N LYS A 77
SHEET 3 C 4 VAL A 101 GLN A 105 -1 O VAL A 101 N LYS A 92
SHEET 4 C 4 GLU A 112 LEU A 115 -1 O GLU A 112 N ARG A 104
SHEET 1 D 4 ALA A 127 PHE A 133 0
SHEET 2 D 4 ILE A 139 SER A 145 -1 O SER A 143 N ASP A 129
SHEET 3 D 4 TRP A 151 ASP A 158 -1 O HIS A 155 N TYR A 142
SHEET 4 D 4 PRO A 164 LYS A 173 -1 O LEU A 165 N LEU A 156
SHEET 1 E 4 SER A 178 LEU A 180 0
SHEET 2 E 4 GLY A 184 SER A 189 -1 O PHE A 186 N SER A 178
SHEET 3 E 4 LYS A 206 ARG A 211 -1 O HIS A 210 N PHE A 185
SHEET 4 E 4 ARG A 220 PHE A 223 -1 O VAL A 222 N VAL A 207
SHEET 1 F 4 TYR A 233 VAL A 238 0
SHEET 2 F 4 PHE A 244 ALA A 250 -1 O LEU A 246 N THR A 237
SHEET 3 F 4 ARG A 257 ASP A 262 -1 O ARG A 257 N ALA A 249
SHEET 4 F 4 LEU A 271 GLN A 274 -1 O LEU A 271 N VAL A 260
SHEET 1 G 4 VAL A 281 LYS A 287 0
SHEET 2 G 4 THR A 290 THR A 295 -1 O TYR A 292 N VAL A 284
SHEET 3 G 4 ARG A 303 ASP A 308 -1 O VAL A 305 N LEU A 293
SHEET 4 G 4 ARG A 318 ILE A 321 -1 O LEU A 320 N LEU A 304
SHEET 1 H 4 THR A 329 GLY A 333 0
SHEET 2 H 4 TYR A 336 VAL A 343 -1 O PHE A 338 N HIS A 331
SHEET 3 H 4 THR A 346 PHE A 352 -1 O THR A 346 N VAL A 343
SHEET 4 H 4 ARG A 358 VAL A 362 -1 O VAL A 359 N GLN A 351
SHEET 1 I 4 SER A 369 GLY A 372 0
SHEET 2 I 4 LEU A 382 ASN A 388 -1 O GLU A 387 N SER A 369
SHEET 3 I 4 GLN A 391 PHE A 398 -1 O PHE A 398 N LEU A 382
SHEET 4 I 4 ILE A 405 ARG A 409 -1 O SER A 406 N ARG A 397
SHEET 1 J 8 TYR A 420 GLN A 428 0
SHEET 2 J 8 ARG A 434 ARG A 442 -1 O TYR A 441 N VAL A 421
SHEET 3 J 8 VAL A 482 ALA A 486 -1 O VAL A 485 N ILE A 438
SHEET 4 J 8 THR A 453 TYR A 456 1 N TYR A 456 O ALA A 484
SHEET 5 J 8 LEU A 532 GLY A 537 1 O ALA A 533 N LEU A 455
SHEET 6 J 8 VAL A 557 ALA A 561 1 O ALA A 561 N GLY A 536
SHEET 7 J 8 SER A 613 ALA A 619 1 O SER A 613 N ALA A 558
SHEET 8 J 8 GLN A 647 GLU A 652 1 O ARG A 650 N VAL A 616
SITE 1 AC1 4 ARG A 13 TYR A 354 GLU A 355 HOH A1019
CRYST1 62.810 93.599 152.896 90.00 90.00 90.00 P 21 21 21 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 0.015921 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010684 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006540 0.00000
TER 5307 ARG A 688
MASTER 311 0 1 21 41 0 1 6 5543 1 6 54
END |