HEADER HYDROLASE 01-DEC-06 2O3E
TITLE CRYSTAL STRUCTURE OF ENGINEERED NEUROLYSIN WITH THIMET OLIGOPEPTIDASE
TITLE 2 SPECIFICITY FOR NEUROTENSIN CLEAVAGE SITE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROLYSIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NEUROTENSIN ENDOPEPTIDASE, MITOCHONDRIAL OLIGOPEPTIDASE M,
COMPND 5 MICROSOMAL ENDOPEPTIDASE, MEP;
COMPND 6 EC: 3.4.24.16;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: NLN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TOP10;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBAD
KEYWDS THERMOLYSIN-LIKE DOMAIN, SUBSTRATE-BINDING CHANNEL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.W.RODGERS,E.J.LIM
REVDAT 7 30-AUG-23 2O3E 1 REMARK
REVDAT 6 20-OCT-21 2O3E 1 REMARK SEQADV LINK
REVDAT 5 18-OCT-17 2O3E 1 REMARK
REVDAT 4 24-FEB-09 2O3E 1 VERSN
REVDAT 3 24-APR-07 2O3E 1 JRNL
REVDAT 2 20-FEB-07 2O3E 1 JRNL
REVDAT 1 23-JAN-07 2O3E 0
JRNL AUTH E.J.LIM,S.SAMPATH,J.COLL-RODRIGUEZ,J.SCHMIDT,K.RAY,
JRNL AUTH 2 D.W.RODGERS
JRNL TITL SWAPPING THE SUBSTRATE SPECIFICITIES OF THE NEUROPEPTIDASES
JRNL TITL 2 NEUROLYSIN AND THIMET OLIGOPEPTIDASE.
JRNL REF J.BIOL.CHEM. V. 282 9722 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17251185
JRNL DOI 10.1074/JBC.M609897200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.K.BROWN,K.MADAUSS,W.LIAN,M.R.BECK,W.D.TOLBERT,D.W.RODGERS
REMARK 1 TITL STRUCTURE OF NEUROLYSIN REVEALS A DEEP CHANNEL THAT LIMITS
REMARK 1 TITL 2 SUBSTRATE ACCESS.
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 98 3127 2001
REMARK 1 REFN ISSN 0027-8424
REMARK 1 PMID 11248043
REMARK 1 DOI 10.1073/PNAS.051633198
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2169754.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 41630
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) : 0.219
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4201
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 50
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 702
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 91
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5351
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 209
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.40000
REMARK 3 B22 (A**2) : -0.37000
REMARK 3 B33 (A**2) : -6.04000
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) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.21
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) : 0.30
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.790
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) : 1.310 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.060 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.220 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.240 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.32
REMARK 3 BSOL : 38.88
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: NULL
REMARK 4
REMARK 4 2O3E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-06.
REMARK 100 THE DEPOSITION ID IS D_1000040636.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.5
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) : 0.997
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42607
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 43.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2000
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.41200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1I1I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 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 -X+1/2,Y+1/2,-Z
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 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 -1.000000 0.000000 0.000000 79.77500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.85000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 79.77500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.85000
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 300 REMARK: THE BIOLOGICAL UNIT IS A SINGLE MONOMER.
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 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 MET A 1
REMARK 465 THR A 2
REMARK 465 LEU A 3
REMARK 465 GLY A 4
REMARK 465 LYS A 5
REMARK 465 GLU A 6
REMARK 465 LEU A 7
REMARK 465 ALA A 8
REMARK 465 SER A 9
REMARK 465 PRO A 10
REMARK 465 LEU A 11
REMARK 465 GLN A 12
REMARK 465 ALA A 13
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 132 -28.58 -34.57
REMARK 500 SER A 167 -2.36 -54.99
REMARK 500 ASP A 186 135.63 -38.87
REMARK 500 ALA A 199 -15.17 86.26
REMARK 500 ASP A 214 37.35 -78.02
REMARK 500 CYS A 249 27.65 45.32
REMARK 500 LYS A 287 -41.47 55.48
REMARK 500 SER A 351 73.85 37.01
REMARK 500 PHE A 361 64.88 -116.82
REMARK 500 PRO A 386 -87.06 -37.73
REMARK 500 ASP A 387 75.97 -106.28
REMARK 500 LYS A 524 126.52 -176.84
REMARK 500 LYS A 527 -88.23 -78.35
REMARK 500 ALA A 569 31.25 -79.53
REMARK 500 ALA A 603 -94.15 -51.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 679 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 474 NE2
REMARK 620 2 HIS A 478 NE2 100.7
REMARK 620 3 GLU A 503 OE1 89.5 91.5
REMARK 620 4 GLU A 503 OE2 141.0 89.1 52.3
REMARK 620 5 HOH A 888 O 98.5 111.6 153.5 113.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 679
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1I1I RELATED DB: PDB
REMARK 900 NEUROLYSIN (ENDOPEPTIDASE 24.16) CRYSTAL STRUCTURE
DBREF 2O3E A 1 678 UNP P42676 NEUL_RAT 24 701
SEQADV 2O3E GLU A 470 UNP P42676 ARG 493 ENGINEERED MUTATION
SEQADV 2O3E ARG A 499 UNP P42676 THR 522 ENGINEERED MUTATION
SEQRES 1 A 678 MET THR LEU GLY LYS GLU LEU ALA SER PRO LEU GLN ALA
SEQRES 2 A 678 MET SER SER TYR THR ALA ALA GLY ARG ASN VAL LEU ARG
SEQRES 3 A 678 TRP ASP LEU SER PRO GLU GLN ILE LYS THR ARG THR GLU
SEQRES 4 A 678 GLN LEU ILE ALA GLN THR LYS GLN VAL TYR ASP THR VAL
SEQRES 5 A 678 GLY THR ILE ALA LEU LYS GLU VAL THR TYR GLU ASN CYS
SEQRES 6 A 678 LEU GLN VAL LEU ALA ASP ILE GLU VAL THR TYR ILE VAL
SEQRES 7 A 678 GLU ARG THR MET LEU ASP PHE PRO GLN HIS VAL SER SER
SEQRES 8 A 678 ASP ARG GLU VAL ARG ALA ALA SER THR GLU ALA ASP LYS
SEQRES 9 A 678 LYS LEU SER ARG PHE ASP ILE GLU MET SER MET ARG GLU
SEQRES 10 A 678 ASP VAL PHE GLN ARG ILE VAL HIS LEU GLN GLU THR CYS
SEQRES 11 A 678 ASP LEU GLU LYS ILE LYS PRO GLU ALA ARG ARG TYR LEU
SEQRES 12 A 678 GLU LYS SER ILE LYS MET GLY LYS ARG ASN GLY LEU HIS
SEQRES 13 A 678 LEU SER GLU HIS ILE ARG ASN GLU ILE LYS SER MET LYS
SEQRES 14 A 678 LYS ARG MET SER GLU LEU CYS ILE ASP PHE ASN LYS ASN
SEQRES 15 A 678 LEU ASN GLU ASP ASP THR SER LEU VAL PHE SER LYS ALA
SEQRES 16 A 678 GLU LEU GLY ALA LEU PRO ASP ASP PHE ILE ASP SER LEU
SEQRES 17 A 678 GLU LYS THR ASP GLU ASP LYS TYR LYS VAL THR LEU LYS
SEQRES 18 A 678 TYR PRO HIS TYR PHE PRO VAL MET LYS LYS CYS CYS VAL
SEQRES 19 A 678 PRO GLU THR ARG ARG LYS MET GLU MET ALA PHE HIS THR
SEQRES 20 A 678 ARG CYS LYS GLN GLU ASN THR ALA ILE LEU GLN GLN LEU
SEQRES 21 A 678 LEU PRO LEU ARG ALA GLN VAL ALA LYS LEU LEU GLY TYR
SEQRES 22 A 678 ASN THR HIS ALA ASP PHE VAL LEU GLU LEU ASN THR ALA
SEQRES 23 A 678 LYS SER THR SER ARG VAL ALA ALA PHE LEU ASP ASP LEU
SEQRES 24 A 678 SER GLN LYS LEU LYS PRO LEU GLY GLU ALA GLU ARG GLU
SEQRES 25 A 678 PHE ILE LEU SER LEU LYS LYS LYS GLU CYS GLU GLU ARG
SEQRES 26 A 678 GLY PHE GLU TYR ASP GLY LYS ILE ASN ALA TRP ASP LEU
SEQRES 27 A 678 HIS TYR TYR MET THR GLN THR GLU GLU LEU LYS TYR SER
SEQRES 28 A 678 VAL ASP GLN GLU SER LEU LYS GLU TYR PHE PRO ILE GLU
SEQRES 29 A 678 VAL VAL THR GLU GLY LEU LEU SER ILE TYR GLN GLU LEU
SEQRES 30 A 678 LEU GLY LEU SER PHE GLU GLN VAL PRO ASP ALA HIS VAL
SEQRES 31 A 678 TRP ASN LYS SER VAL SER LEU TYR THR VAL LYS ASP LYS
SEQRES 32 A 678 ALA THR GLY GLU VAL LEU GLY GLN PHE TYR LEU ASP LEU
SEQRES 33 A 678 TYR PRO ARG GLU GLY LYS TYR ASN HIS ALA ALA CYS PHE
SEQRES 34 A 678 GLY LEU GLN PRO GLY CYS LEU LEU PRO ASP GLY SER ARG
SEQRES 35 A 678 MET MET SER VAL ALA ALA LEU VAL VAL ASN PHE SER GLN
SEQRES 36 A 678 PRO VAL ALA GLY ARG PRO SER LEU LEU ARG HIS ASP GLU
SEQRES 37 A 678 VAL GLU THR TYR PHE HIS GLU PHE GLY HIS VAL MET HIS
SEQRES 38 A 678 GLN ILE CYS ALA GLN THR ASP PHE ALA ARG PHE SER GLY
SEQRES 39 A 678 THR ASN VAL GLU ARG ASP PHE VAL GLU VAL PRO SER GLN
SEQRES 40 A 678 MET LEU GLU ASN TRP VAL TRP ASP VAL ASP SER LEU ARG
SEQRES 41 A 678 LYS LEU SER LYS HIS TYR LYS ASP GLY HIS PRO ILE THR
SEQRES 42 A 678 ASP GLU LEU LEU GLU LYS LEU VAL ALA SER ARG LEU VAL
SEQRES 43 A 678 ASN THR GLY LEU LEU THR LEU ARG GLN ILE VAL LEU SER
SEQRES 44 A 678 LYS VAL ASP GLN SER LEU HIS THR ASN ALA THR LEU ASP
SEQRES 45 A 678 ALA ALA SER GLU TYR ALA LYS TYR CYS THR GLU ILE LEU
SEQRES 46 A 678 GLY VAL ALA ALA THR PRO GLY THR ASN MET PRO ALA THR
SEQRES 47 A 678 PHE GLY HIS LEU ALA GLY GLY TYR ASP GLY GLN TYR TYR
SEQRES 48 A 678 GLY TYR LEU TRP SER GLU VAL PHE SER MET ASP MET PHE
SEQRES 49 A 678 HIS SER CYS PHE LYS LYS GLU GLY ILE MET ASN PRO GLU
SEQRES 50 A 678 VAL GLY MET LYS TYR ARG ASN LEU ILE LEU LYS PRO GLY
SEQRES 51 A 678 GLY SER LEU ASP GLY MET ASP MET LEU GLN ASN PHE LEU
SEQRES 52 A 678 GLN ARG GLU PRO ASN GLN LYS ALA PHE LEU MET SER ARG
SEQRES 53 A 678 GLY LEU
HET ZN A 679 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
FORMUL 3 HOH *209(H2 O)
HELIX 1 1 SER A 30 GLY A 53 1 24
HELIX 2 2 THR A 54 ILE A 55 5 2
HELIX 3 3 ALA A 56 VAL A 60 5 5
HELIX 4 4 CYS A 65 PHE A 85 1 21
HELIX 5 5 PHE A 85 SER A 90 1 6
HELIX 6 6 ASP A 92 MET A 115 1 24
HELIX 7 7 ARG A 116 CYS A 130 1 15
HELIX 8 8 LYS A 136 ASN A 153 1 18
HELIX 9 9 SER A 158 ILE A 165 1 8
HELIX 10 10 ILE A 165 ASP A 186 1 22
HELIX 11 11 PRO A 201 SER A 207 1 7
HELIX 12 12 LYS A 221 CYS A 232 1 12
HELIX 13 13 VAL A 234 HIS A 246 1 13
HELIX 14 14 CYS A 249 LEU A 271 1 23
HELIX 15 15 THR A 275 GLU A 282 1 8
HELIX 16 16 SER A 288 ARG A 325 1 38
HELIX 17 17 ASN A 334 TRP A 336 5 3
HELIX 18 18 ASP A 337 TYR A 350 1 14
HELIX 19 19 ASP A 353 LYS A 358 1 6
HELIX 20 20 GLU A 359 PHE A 361 5 3
HELIX 21 21 PRO A 362 GLY A 379 1 18
HELIX 22 22 ARG A 465 ALA A 485 1 21
HELIX 23 23 PHE A 489 SER A 493 5 5
HELIX 24 24 GLU A 503 ASN A 511 1 9
HELIX 25 25 TRP A 512 TRP A 514 5 3
HELIX 26 26 ASP A 515 SER A 523 1 9
HELIX 27 27 THR A 533 SER A 543 1 11
HELIX 28 28 ASN A 547 HIS A 566 1 20
HELIX 29 29 ASP A 572 ILE A 584 1 13
HELIX 30 30 ASN A 594 PHE A 599 5 6
HELIX 31 31 TYR A 611 CYS A 627 1 17
HELIX 32 32 CYS A 627 GLY A 632 1 6
HELIX 33 33 ASN A 635 LEU A 647 1 13
HELIX 34 34 PRO A 649 LEU A 653 5 5
HELIX 35 35 ASP A 654 GLN A 664 1 11
HELIX 36 36 GLN A 669 GLY A 677 1 9
SHEET 1 A 2 SER A 189 SER A 193 0
SHEET 2 A 2 LYS A 215 THR A 219 -1 O TYR A 216 N PHE A 192
SHEET 1 B 5 LEU A 380 GLN A 384 0
SHEET 2 B 5 SER A 396 ASP A 402 -1 O THR A 399 N GLU A 383
SHEET 3 B 5 VAL A 408 ASP A 415 -1 O GLY A 410 N VAL A 400
SHEET 4 B 5 SER A 445 VAL A 450 1 O LEU A 449 N TYR A 413
SHEET 5 B 5 ALA A 427 GLN A 432 -1 N LEU A 431 O VAL A 446
LINK NE2 HIS A 474 ZN ZN A 679 1555 1555 2.21
LINK NE2 HIS A 478 ZN ZN A 679 1555 1555 2.15
LINK OE1 GLU A 503 ZN ZN A 679 1555 1555 2.16
LINK OE2 GLU A 503 ZN ZN A 679 1555 1555 2.68
LINK ZN ZN A 679 O HOH A 888 1555 1555 2.34
SITE 1 AC1 4 HIS A 474 HIS A 478 GLU A 503 HOH A 888
CRYST1 159.550 87.700 58.400 90.00 90.00 90.00 P 21 21 2 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 0.006268 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011403 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017123 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
