HEADER HYDROLASE, LIGASE 24-AUG-09 3IRT
TITLE CRYSTAL STRUCTURE OF THE I93M MUTANT OF UBIQUITIN CARBOXY-TERMINAL
TITLE 2 HYDROLASE L1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: UCH-L1, UBIQUITIN THIOESTERASE L1, NEURON CYTOPLASMIC
COMPND 5 PROTEIN 9.5, PGP 9.5, PGP9.5;
COMPND 6 EC: 3.4.19.12, 6.-.-.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PGP9.5, UCHL1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1
KEYWDS UBIQUITIN HYDROLASE, PARKINSON'S DISEASE MUTANT, CYTOPLASM, DISEASE
KEYWDS 2 MUTATION, GLYCOPROTEIN, HYDROLASE, LIGASE, OXIDATION, POLYMORPHISM,
KEYWDS 3 PROTEASE, THIOL PROTEASE, UBL CONJUGATION PATHWAY
EXPDTA X-RAY DIFFRACTION
AUTHOR C.W.DAVIES,T.K.MAITI,C.DAS
REVDAT 1 09-JUN-10 3IRT 0
JRNL AUTH D.A.BOUDREAUX,T.K.MAITI,C.W.DAVIES,C.DAS
JRNL TITL UBIQUITIN VINYL METHYL ESTER BINDING ORIENTS THE MISALIGNED
JRNL TITL 2 ACTIVE SITE OF THE UBIQUITIN HYDROLASE UCHL1 INTO
JRNL TITL 3 PRODUCTIVE CONFORMATION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 9117 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 20439756
JRNL DOI 10.1073/PNAS.0910870107
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.75
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 11957
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.870
REMARK 3 FREE R VALUE TEST SET COUNT : 582
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 41.7526 - 4.4423 1.00 3101 151 0.1868 0.2189
REMARK 3 2 4.4423 - 3.5265 1.00 2936 147 0.1912 0.2211
REMARK 3 3 3.5265 - 3.0809 0.99 2865 153 0.2455 0.3329
REMARK 3 4 3.0809 - 2.7993 0.85 2473 131 0.3058 0.3634
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 63.02
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 1.090
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.780
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 67.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 9.94330
REMARK 3 B22 (A**2) : 9.94330
REMARK 3 B33 (A**2) : -20.21160
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 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 : 0.003 3544
REMARK 3 ANGLE : 0.641 4772
REMARK 3 CHIRALITY : 0.042 520
REMARK 3 PLANARITY : 0.002 638
REMARK 3 DIHEDRAL : 14.325 1336
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 : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: chain A and (resseq 1:71 or resseq 74:223
REMARK 3 )
REMARK 3 SELECTION : chain B and (resseq 1:71 or resseq 74:223
REMARK 3 )
REMARK 3 ATOM PAIRS NUMBER : 1728
REMARK 3 RMSD : 0.035
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3IRT COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-AUG-09.
REMARK 100 THE RCSB ID CODE IS RCSB054785.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0331
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11988
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 41.750
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.780
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 12.800
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : 0.11100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.9800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : 0.54000
REMARK 200 R SYM FOR SHELL (I) : 0.54000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.780
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: ONE SUBUNIT OF THE ASYMMETRIC UNIT OF 2ETL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M AMMONIUM SULFATE, 0.1 M TRIS
REMARK 280 HYDROCHLORIDE, 0.1 M SODIUM SODIUM MALONATE, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z
REMARK 290 4555 Y+1/2,-X+1/2,Z
REMARK 290 5555 -X+1/2,Y+1/2,-Z
REMARK 290 6555 X+1/2,-Y+1/2,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 54.96900
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 54.96900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 54.96900
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 54.96900
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 54.96900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.96900
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 54.96900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.96900
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 228 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 225 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 225 LIES ON A SPECIAL POSITION.
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 -4
REMARK 465 PRO A -3
REMARK 465 LEU A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 GLY B -4
REMARK 465 PRO B -3
REMARK 465 LEU B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 153 NE - CZ - NH1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG A 153 NE - CZ - NH2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG B 153 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG B 153 NE - CZ - NH2 ANGL. DEV. = -5.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 LEU A 34 76.22 -110.57
REMARK 500 GLU A 36 -70.73 -38.43
REMARK 500 SER A 38 -25.98 71.00
REMARK 500 PRO A 43 157.81 -48.23
REMARK 500 ASN A 88 -2.73 69.62
REMARK 500 ASN A 102 30.29 -148.40
REMARK 500 LYS A 123 70.84 -111.14
REMARK 500 CYS A 152 -160.13 -109.56
REMARK 500 ARG A 153 -100.11 -146.52
REMARK 500 VAL A 154 113.21 65.62
REMARK 500 ASP A 155 75.78 -163.33
REMARK 500 GLU A 190 28.06 -75.88
REMARK 500 ASP A 191 -27.50 -142.69
REMARK 500 GLU A 208 67.35 -116.88
REMARK 500 GLN A 209 36.67 -69.86
REMARK 500 LEU B 34 76.52 -110.97
REMARK 500 GLU B 36 -70.39 -38.21
REMARK 500 SER B 38 -26.09 71.16
REMARK 500 PRO B 43 157.61 -48.62
REMARK 500 LYS B 71 -127.89 -66.11
REMARK 500 GLN B 73 -68.47 -146.98
REMARK 500 GLU B 74 -17.84 -159.76
REMARK 500 ASN B 88 -2.82 69.77
REMARK 500 ASN B 102 30.44 -148.70
REMARK 500 LYS B 123 70.68 -111.38
REMARK 500 CYS B 152 -160.39 -110.14
REMARK 500 ARG B 153 -99.19 -146.24
REMARK 500 VAL B 154 113.64 65.80
REMARK 500 ASP B 155 75.63 -163.52
REMARK 500 GLU B 190 28.46 -75.83
REMARK 500 ASP B 191 -27.68 -143.04
REMARK 500 GLU B 208 66.89 -117.10
REMARK 500 GLN B 209 36.49 -69.13
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 CL A 224
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 224
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ETL RELATED DB: PDB
REMARK 900 ISOLEUCINE 93 TO METHIONINE MUTANT
DBREF 3IRT A 1 223 UNP P09936 UCHL1_HUMAN 1 223
DBREF 3IRT B 1 223 UNP P09936 UCHL1_HUMAN 1 223
SEQADV 3IRT GLY A -4 UNP P09936 EXPRESSION TAG
SEQADV 3IRT PRO A -3 UNP P09936 EXPRESSION TAG
SEQADV 3IRT LEU A -2 UNP P09936 EXPRESSION TAG
SEQADV 3IRT GLY A -1 UNP P09936 EXPRESSION TAG
SEQADV 3IRT SER A 0 UNP P09936 EXPRESSION TAG
SEQADV 3IRT MET A 93 UNP P09936 ILE 93 ENGINEERED
SEQADV 3IRT GLY B -4 UNP P09936 EXPRESSION TAG
SEQADV 3IRT PRO B -3 UNP P09936 EXPRESSION TAG
SEQADV 3IRT LEU B -2 UNP P09936 EXPRESSION TAG
SEQADV 3IRT GLY B -1 UNP P09936 EXPRESSION TAG
SEQADV 3IRT SER B 0 UNP P09936 EXPRESSION TAG
SEQADV 3IRT MET B 93 UNP P09936 ILE 93 ENGINEERED
SEQRES 1 A 228 GLY PRO LEU GLY SER MET GLN LEU LYS PRO MET GLU ILE
SEQRES 2 A 228 ASN PRO GLU MET LEU ASN LYS VAL LEU SER ARG LEU GLY
SEQRES 3 A 228 VAL ALA GLY GLN TRP ARG PHE VAL ASP VAL LEU GLY LEU
SEQRES 4 A 228 GLU GLU GLU SER LEU GLY SER VAL PRO ALA PRO ALA CYS
SEQRES 5 A 228 ALA LEU LEU LEU LEU PHE PRO LEU THR ALA GLN HIS GLU
SEQRES 6 A 228 ASN PHE ARG LYS LYS GLN ILE GLU GLU LEU LYS GLY GLN
SEQRES 7 A 228 GLU VAL SER PRO LYS VAL TYR PHE MET LYS GLN THR ILE
SEQRES 8 A 228 GLY ASN SER CYS GLY THR MET GLY LEU ILE HIS ALA VAL
SEQRES 9 A 228 ALA ASN ASN GLN ASP LYS LEU GLY PHE GLU ASP GLY SER
SEQRES 10 A 228 VAL LEU LYS GLN PHE LEU SER GLU THR GLU LYS MET SER
SEQRES 11 A 228 PRO GLU ASP ARG ALA LYS CYS PHE GLU LYS ASN GLU ALA
SEQRES 12 A 228 ILE GLN ALA ALA HIS ASP ALA VAL ALA GLN GLU GLY GLN
SEQRES 13 A 228 CYS ARG VAL ASP ASP LYS VAL ASN PHE HIS PHE ILE LEU
SEQRES 14 A 228 PHE ASN ASN VAL ASP GLY HIS LEU TYR GLU LEU ASP GLY
SEQRES 15 A 228 ARG MET PRO PHE PRO VAL ASN HIS GLY ALA SER SER GLU
SEQRES 16 A 228 ASP THR LEU LEU LYS ASP ALA ALA LYS VAL CYS ARG GLU
SEQRES 17 A 228 PHE THR GLU ARG GLU GLN GLY GLU VAL ARG PHE SER ALA
SEQRES 18 A 228 VAL ALA LEU CYS LYS ALA ALA
SEQRES 1 B 228 GLY PRO LEU GLY SER MET GLN LEU LYS PRO MET GLU ILE
SEQRES 2 B 228 ASN PRO GLU MET LEU ASN LYS VAL LEU SER ARG LEU GLY
SEQRES 3 B 228 VAL ALA GLY GLN TRP ARG PHE VAL ASP VAL LEU GLY LEU
SEQRES 4 B 228 GLU GLU GLU SER LEU GLY SER VAL PRO ALA PRO ALA CYS
SEQRES 5 B 228 ALA LEU LEU LEU LEU PHE PRO LEU THR ALA GLN HIS GLU
SEQRES 6 B 228 ASN PHE ARG LYS LYS GLN ILE GLU GLU LEU LYS GLY GLN
SEQRES 7 B 228 GLU VAL SER PRO LYS VAL TYR PHE MET LYS GLN THR ILE
SEQRES 8 B 228 GLY ASN SER CYS GLY THR MET GLY LEU ILE HIS ALA VAL
SEQRES 9 B 228 ALA ASN ASN GLN ASP LYS LEU GLY PHE GLU ASP GLY SER
SEQRES 10 B 228 VAL LEU LYS GLN PHE LEU SER GLU THR GLU LYS MET SER
SEQRES 11 B 228 PRO GLU ASP ARG ALA LYS CYS PHE GLU LYS ASN GLU ALA
SEQRES 12 B 228 ILE GLN ALA ALA HIS ASP ALA VAL ALA GLN GLU GLY GLN
SEQRES 13 B 228 CYS ARG VAL ASP ASP LYS VAL ASN PHE HIS PHE ILE LEU
SEQRES 14 B 228 PHE ASN ASN VAL ASP GLY HIS LEU TYR GLU LEU ASP GLY
SEQRES 15 B 228 ARG MET PRO PHE PRO VAL ASN HIS GLY ALA SER SER GLU
SEQRES 16 B 228 ASP THR LEU LEU LYS ASP ALA ALA LYS VAL CYS ARG GLU
SEQRES 17 B 228 PHE THR GLU ARG GLU GLN GLY GLU VAL ARG PHE SER ALA
SEQRES 18 B 228 VAL ALA LEU CYS LYS ALA ALA
HET CL A 224 1
HET CL B 224 1
HETNAM CL CHLORIDE ION
FORMUL 3 CL 2(CL 1-)
FORMUL 5 HOH *35(H2 O)
HELIX 1 1 ASN A 9 LEU A 20 1 12
HELIX 2 2 GLU A 35 GLY A 40 1 6
HELIX 3 3 THR A 56 LEU A 70 1 15
HELIX 4 4 SER A 89 ASN A 101 1 13
HELIX 5 5 SER A 112 THR A 121 1 10
HELIX 6 6 SER A 125 ASN A 136 1 12
HELIX 7 7 ASN A 136 GLN A 148 1 13
HELIX 8 8 THR A 192 GLU A 206 1 15
HELIX 9 9 ASN B 9 LEU B 20 1 12
HELIX 10 10 GLU B 35 GLY B 40 1 6
HELIX 11 11 THR B 56 LEU B 70 1 15
HELIX 12 12 SER B 89 ASN B 101 1 13
HELIX 13 13 SER B 112 THR B 121 1 10
HELIX 14 14 SER B 125 ASN B 136 1 12
HELIX 15 15 ASN B 136 GLN B 148 1 13
HELIX 16 16 THR B 192 GLU B 206 1 15
SHEET 1 A 6 TRP A 26 VAL A 31 0
SHEET 2 A 6 SER A 215 LYS A 221 -1 O ALA A 218 N VAL A 29
SHEET 3 A 6 ALA A 46 PRO A 54 -1 N LEU A 52 O SER A 215
SHEET 4 A 6 PHE A 160 ASN A 167 -1 O ILE A 163 N LEU A 51
SHEET 5 A 6 HIS A 171 LEU A 175 -1 O LEU A 175 N LEU A 164
SHEET 6 A 6 VAL A 183 ALA A 187 -1 O HIS A 185 N LEU A 172
SHEET 1 B 6 TRP B 26 VAL B 31 0
SHEET 2 B 6 SER B 215 LYS B 221 -1 O ALA B 218 N VAL B 29
SHEET 3 B 6 ALA B 46 PRO B 54 -1 N LEU B 52 O SER B 215
SHEET 4 B 6 PHE B 160 ASN B 167 -1 O ILE B 163 N LEU B 51
SHEET 5 B 6 HIS B 171 LEU B 175 -1 O LEU B 175 N LEU B 164
SHEET 6 B 6 VAL B 183 ALA B 187 -1 O HIS B 185 N LEU B 172
CISPEP 1 ALA A 44 PRO A 45 0 -2.72
CISPEP 2 ALA B 44 PRO B 45 0 -2.48
SITE 1 AC1 2 GLN A 84 CYS A 90
SITE 1 AC2 3 GLN B 84 ASN B 88 CYS B 90
CRYST1 109.938 109.938 79.040 90.00 90.00 90.00 P 4 21 2 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009096 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009096 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012652 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
