HEADER HYDROLASE 04-MAY-10 3MVI
TITLE CRYSTAL STRUCTURE OF HOLO MADA AT 1.6 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSINE DEAMINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 4-352;
COMPND 5 SYNONYM: ADENOSINE AMINOHYDROLASE;
COMPND 6 EC: 3.5.4.4;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: ADA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRC4
KEYWDS HYDROLASE, ADENOSINE DEAMINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.NIU,Q.SHU,Z.CHEN,S.MATHEWS,E.DI CERA,C.FRIEDEN
REVDAT 3 06-SEP-23 3MVI 1 REMARK LINK
REVDAT 2 23-FEB-11 3MVI 1 JRNL
REVDAT 1 03-NOV-10 3MVI 0
JRNL AUTH W.NIU,Q.SHU,Z.CHEN,S.MATHEWS,E.DI CERA,C.FRIEDEN
JRNL TITL THE ROLE OF ZN2+ ON THE STRUCTURE AND STABILITY OF MURINE
JRNL TITL 2 ADENOSINE DEAMINASE.
JRNL REF J.PHYS.CHEM.B V. 114 16156 2010
JRNL REFN ISSN 1089-5647
JRNL PMID 20815357
JRNL DOI 10.1021/JP106041V
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Z.WANG,F.A.QUIOCHO
REMARK 1 TITL COMPLEXES OF ADENOSINE DEAMINASE WITH TWO POTENT INHIBITORS:
REMARK 1 TITL 2 X-RAY STRUCTURES IN FOUR INDEPENDENT MOLECULES AT PH OF
REMARK 1 TITL 3 MAXIMUM ACTIVITY.
REMARK 1 REF BIOCHEMISTRY V. 37 8314 1998
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 9622483
REMARK 1 DOI 10.1021/BI980324O
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0066
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.66
REMARK 3 DATA CUTOFF (SIGMA(F)) : -1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 92137
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 + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4624
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5227
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.83
REMARK 3 BIN R VALUE (WORKING SET) : 0.2850
REMARK 3 BIN FREE R VALUE SET COUNT : 259
REMARK 3 BIN FREE R VALUE : 0.3450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5584
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 648
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.090
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.067
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.961
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5722 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7742 ; 1.295 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 696 ; 5.481 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 270 ;37.108 ;24.593
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1016 ;12.873 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;15.640 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 842 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4336 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3482 ; 0.706 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5638 ; 1.308 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2240 ; 2.280 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2104 ; 3.857 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3MVI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAY-10.
REMARK 100 THE DEPOSITION ID IS D_1000059045.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : BENT GE(111) MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92164
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.37400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP FROM CCP4
REMARK 200 STARTING MODEL: PDB ENTRY 1A4M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS_HCL, PH 8.5 AND 25% PEG
REMARK 280 6000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 46.90200
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 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 ASN A 8 55.60 -90.99
REMARK 500 ALA A 21 52.49 -142.12
REMARK 500 LEU A 56 -112.09 -125.99
REMARK 500 HIS A 238 -87.46 76.18
REMARK 500 ASP A 295 -79.55 76.65
REMARK 500 ALA B 21 43.65 -141.09
REMARK 500 LEU B 56 -123.85 -127.23
REMARK 500 HIS B 238 -89.00 78.11
REMARK 500 ASP B 295 -76.61 72.65
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 901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 15 NE2
REMARK 620 2 HIS A 17 NE2 108.6
REMARK 620 3 HIS A 214 NE2 92.0 103.1
REMARK 620 4 ASP A 295 OD1 86.1 87.9 168.8
REMARK 620 5 HOH A 616 O 115.9 133.1 89.8 81.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 15 NE2
REMARK 620 2 HIS B 17 NE2 114.2
REMARK 620 3 HIS B 214 NE2 92.1 100.1
REMARK 620 4 ASP B 295 OD1 86.6 90.6 168.7
REMARK 620 5 HOH B 619 O 114.7 128.5 93.4 77.1
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 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 902
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A4M RELATED DB: PDB
REMARK 900 COMPLEXES OF ADENOSINE DEAMINASE WITH TWO POTENT INHIBITORS: X-RAY
REMARK 900 STRUCTURES IN FOUR INDEPENDENT MOLECULES AT PH OF MAXIMUM ACTIVITY.
REMARK 900 RELATED ID: 3MVT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APO MADA AT 2.2 A RESOLUTION
DBREF 3MVI A 4 352 UNP P03958 ADA_MOUSE 4 352
DBREF 3MVI B 4 352 UNP P03958 ADA_MOUSE 4 352
SEQRES 1 A 349 THR PRO ALA PHE ASN LYS PRO LYS VAL GLU LEU HIS VAL
SEQRES 2 A 349 HIS LEU ASP GLY ALA ILE LYS PRO GLU THR ILE LEU TYR
SEQRES 3 A 349 PHE GLY LYS LYS ARG GLY ILE ALA LEU PRO ALA ASP THR
SEQRES 4 A 349 VAL GLU GLU LEU ARG ASN ILE ILE GLY MET ASP LYS PRO
SEQRES 5 A 349 LEU SER LEU PRO GLY PHE LEU ALA LYS PHE ASP TYR TYR
SEQRES 6 A 349 MET PRO VAL ILE ALA GLY CYS ARG GLU ALA ILE LYS ARG
SEQRES 7 A 349 ILE ALA TYR GLU PHE VAL GLU MET LYS ALA LYS GLU GLY
SEQRES 8 A 349 VAL VAL TYR VAL GLU VAL ARG TYR SER PRO HIS LEU LEU
SEQRES 9 A 349 ALA ASN SER LYS VAL ASP PRO MET PRO TRP ASN GLN THR
SEQRES 10 A 349 GLU GLY ASP VAL THR PRO ASP ASP VAL VAL ASP LEU VAL
SEQRES 11 A 349 ASN GLN GLY LEU GLN GLU GLY GLU GLN ALA PHE GLY ILE
SEQRES 12 A 349 LYS VAL ARG SER ILE LEU CYS CYS MET ARG HIS GLN PRO
SEQRES 13 A 349 SER TRP SER LEU GLU VAL LEU GLU LEU CYS LYS LYS TYR
SEQRES 14 A 349 ASN GLN LYS THR VAL VAL ALA MET ASP LEU ALA GLY ASP
SEQRES 15 A 349 GLU THR ILE GLU GLY SER SER LEU PHE PRO GLY HIS VAL
SEQRES 16 A 349 GLU ALA TYR GLU GLY ALA VAL LYS ASN GLY ILE HIS ARG
SEQRES 17 A 349 THR VAL HIS ALA GLY GLU VAL GLY SER PRO GLU VAL VAL
SEQRES 18 A 349 ARG GLU ALA VAL ASP ILE LEU LYS THR GLU ARG VAL GLY
SEQRES 19 A 349 HIS GLY TYR HIS THR ILE GLU ASP GLU ALA LEU TYR ASN
SEQRES 20 A 349 ARG LEU LEU LYS GLU ASN MET HIS PHE GLU VAL CYS PRO
SEQRES 21 A 349 TRP SER SER TYR LEU THR GLY ALA TRP ASP PRO LYS THR
SEQRES 22 A 349 THR HIS ALA VAL VAL ARG PHE LYS ASN ASP LYS ALA ASN
SEQRES 23 A 349 TYR SER LEU ASN THR ASP ASP PRO LEU ILE PHE LYS SER
SEQRES 24 A 349 THR LEU ASP THR ASP TYR GLN MET THR LYS LYS ASP MET
SEQRES 25 A 349 GLY PHE THR GLU GLU GLU PHE LYS ARG LEU ASN ILE ASN
SEQRES 26 A 349 ALA ALA LYS SER SER PHE LEU PRO GLU GLU GLU LYS LYS
SEQRES 27 A 349 GLU LEU LEU GLU ARG LEU TYR ARG GLU TYR GLN
SEQRES 1 B 349 THR PRO ALA PHE ASN LYS PRO LYS VAL GLU LEU HIS VAL
SEQRES 2 B 349 HIS LEU ASP GLY ALA ILE LYS PRO GLU THR ILE LEU TYR
SEQRES 3 B 349 PHE GLY LYS LYS ARG GLY ILE ALA LEU PRO ALA ASP THR
SEQRES 4 B 349 VAL GLU GLU LEU ARG ASN ILE ILE GLY MET ASP LYS PRO
SEQRES 5 B 349 LEU SER LEU PRO GLY PHE LEU ALA LYS PHE ASP TYR TYR
SEQRES 6 B 349 MET PRO VAL ILE ALA GLY CYS ARG GLU ALA ILE LYS ARG
SEQRES 7 B 349 ILE ALA TYR GLU PHE VAL GLU MET LYS ALA LYS GLU GLY
SEQRES 8 B 349 VAL VAL TYR VAL GLU VAL ARG TYR SER PRO HIS LEU LEU
SEQRES 9 B 349 ALA ASN SER LYS VAL ASP PRO MET PRO TRP ASN GLN THR
SEQRES 10 B 349 GLU GLY ASP VAL THR PRO ASP ASP VAL VAL ASP LEU VAL
SEQRES 11 B 349 ASN GLN GLY LEU GLN GLU GLY GLU GLN ALA PHE GLY ILE
SEQRES 12 B 349 LYS VAL ARG SER ILE LEU CYS CYS MET ARG HIS GLN PRO
SEQRES 13 B 349 SER TRP SER LEU GLU VAL LEU GLU LEU CYS LYS LYS TYR
SEQRES 14 B 349 ASN GLN LYS THR VAL VAL ALA MET ASP LEU ALA GLY ASP
SEQRES 15 B 349 GLU THR ILE GLU GLY SER SER LEU PHE PRO GLY HIS VAL
SEQRES 16 B 349 GLU ALA TYR GLU GLY ALA VAL LYS ASN GLY ILE HIS ARG
SEQRES 17 B 349 THR VAL HIS ALA GLY GLU VAL GLY SER PRO GLU VAL VAL
SEQRES 18 B 349 ARG GLU ALA VAL ASP ILE LEU LYS THR GLU ARG VAL GLY
SEQRES 19 B 349 HIS GLY TYR HIS THR ILE GLU ASP GLU ALA LEU TYR ASN
SEQRES 20 B 349 ARG LEU LEU LYS GLU ASN MET HIS PHE GLU VAL CYS PRO
SEQRES 21 B 349 TRP SER SER TYR LEU THR GLY ALA TRP ASP PRO LYS THR
SEQRES 22 B 349 THR HIS ALA VAL VAL ARG PHE LYS ASN ASP LYS ALA ASN
SEQRES 23 B 349 TYR SER LEU ASN THR ASP ASP PRO LEU ILE PHE LYS SER
SEQRES 24 B 349 THR LEU ASP THR ASP TYR GLN MET THR LYS LYS ASP MET
SEQRES 25 B 349 GLY PHE THR GLU GLU GLU PHE LYS ARG LEU ASN ILE ASN
SEQRES 26 B 349 ALA ALA LYS SER SER PHE LEU PRO GLU GLU GLU LYS LYS
SEQRES 27 B 349 GLU LEU LEU GLU ARG LEU TYR ARG GLU TYR GLN
HET ZN A 901 1
HET GOL A 902 6
HET ZN B 901 1
HET GOL B 902 6
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 GOL 2(C3 H8 O3)
FORMUL 7 HOH *648(H2 O)
HELIX 1 1 HIS A 17 ALA A 21 5 5
HELIX 2 2 LYS A 23 GLY A 35 1 13
HELIX 3 3 THR A 42 GLY A 51 1 10
HELIX 4 4 SER A 57 ALA A 63 1 7
HELIX 5 5 LYS A 64 ALA A 73 1 10
HELIX 6 6 CYS A 75 GLU A 93 1 19
HELIX 7 7 PRO A 104 ALA A 108 5 5
HELIX 8 8 MET A 115 GLN A 119 5 5
HELIX 9 9 THR A 125 GLY A 145 1 21
HELIX 10 10 GLN A 158 SER A 160 5 3
HELIX 11 11 TRP A 161 TYR A 172 1 12
HELIX 12 12 GLY A 190 LEU A 193 5 4
HELIX 13 13 PHE A 194 GLY A 208 1 15
HELIX 14 14 SER A 220 ILE A 230 1 11
HELIX 15 15 TYR A 240 GLU A 244 5 5
HELIX 16 16 ASP A 245 GLU A 255 1 11
HELIX 17 17 CYS A 262 THR A 269 1 8
HELIX 18 18 HIS A 278 ASP A 286 1 9
HELIX 19 19 ASP A 296 LYS A 301 1 6
HELIX 20 20 THR A 303 GLY A 316 1 14
HELIX 21 21 THR A 318 SER A 333 1 16
HELIX 22 22 PRO A 336 TYR A 351 1 16
HELIX 23 23 ASP B 19 ALA B 21 5 3
HELIX 24 24 LYS B 23 GLY B 35 1 13
HELIX 25 25 THR B 42 GLY B 51 1 10
HELIX 26 26 SER B 57 ALA B 73 1 17
HELIX 27 27 CYS B 75 GLU B 93 1 19
HELIX 28 28 PRO B 104 ALA B 108 5 5
HELIX 29 29 MET B 115 GLN B 119 5 5
HELIX 30 30 THR B 125 GLY B 145 1 21
HELIX 31 31 GLN B 158 SER B 160 5 3
HELIX 32 32 TRP B 161 TYR B 172 1 12
HELIX 33 33 GLY B 190 LEU B 193 5 4
HELIX 34 34 PHE B 194 GLY B 208 1 15
HELIX 35 35 SER B 220 ILE B 230 1 11
HELIX 36 36 TYR B 240 GLU B 244 5 5
HELIX 37 37 ASP B 245 GLU B 255 1 11
HELIX 38 38 CYS B 262 THR B 269 1 8
HELIX 39 39 HIS B 278 ASP B 286 1 9
HELIX 40 40 ASP B 296 LYS B 301 1 6
HELIX 41 41 THR B 303 GLY B 316 1 14
HELIX 42 42 THR B 318 SER B 333 1 16
HELIX 43 43 PRO B 336 TYR B 351 1 16
SHEET 1 A 8 LYS A 11 GLU A 13 0
SHEET 2 A 8 VAL A 95 TYR A 102 1 O VAL A 96 N LYS A 11
SHEET 3 A 8 LYS A 147 MET A 155 1 O CYS A 153 N TYR A 102
SHEET 4 A 8 VAL A 177 ALA A 183 1 O ASP A 181 N CYS A 154
SHEET 5 A 8 HIS A 210 ALA A 215 1 O THR A 212 N MET A 180
SHEET 6 A 8 ARG A 235 HIS A 238 1 O GLY A 237 N VAL A 213
SHEET 7 A 8 HIS A 258 VAL A 261 1 O GLU A 260 N VAL A 236
SHEET 8 A 8 ASN A 289 LEU A 292 1 O ASN A 289 N PHE A 259
SHEET 1 B 8 LYS B 11 HIS B 17 0
SHEET 2 B 8 VAL B 95 TYR B 102 1 O ARG B 101 N VAL B 16
SHEET 3 B 8 LYS B 147 MET B 155 1 O CYS B 153 N TYR B 102
SHEET 4 B 8 VAL B 177 ALA B 183 1 O ASP B 181 N CYS B 154
SHEET 5 B 8 HIS B 210 ALA B 215 1 O THR B 212 N MET B 180
SHEET 6 B 8 ARG B 235 HIS B 238 1 O GLY B 237 N VAL B 213
SHEET 7 B 8 HIS B 258 VAL B 261 1 O GLU B 260 N VAL B 236
SHEET 8 B 8 ASN B 289 LEU B 292 1 O ASN B 289 N PHE B 259
LINK NE2 HIS A 15 ZN ZN A 901 1555 1555 2.06
LINK NE2 HIS A 17 ZN ZN A 901 1555 1555 2.07
LINK NE2 HIS A 214 ZN ZN A 901 1555 1555 2.15
LINK OD1 ASP A 295 ZN ZN A 901 1555 1555 2.41
LINK O HOH A 616 ZN ZN A 901 1555 1555 2.05
LINK NE2 HIS B 15 ZN ZN B 901 1555 1555 2.09
LINK NE2 HIS B 17 ZN ZN B 901 1555 1555 2.12
LINK NE2 HIS B 214 ZN ZN B 901 1555 1555 2.14
LINK OD1 ASP B 295 ZN ZN B 901 1555 1555 2.46
LINK O HOH B 619 ZN ZN B 901 1555 1555 2.13
CISPEP 1 ASP A 113 PRO A 114 0 -4.42
CISPEP 2 LYS A 175 THR A 176 0 4.84
CISPEP 3 ASP B 113 PRO B 114 0 -3.28
CISPEP 4 LYS B 175 THR B 176 0 7.79
SITE 1 AC1 5 HIS A 15 HIS A 17 HIS A 214 ASP A 295
SITE 2 AC1 5 HOH A 616
SITE 1 AC2 7 HIS A 17 ASP A 19 LEU A 106 HOH A 539
SITE 2 AC2 7 HOH A 570 HOH A 620 HOH A 647
SITE 1 AC3 5 HIS B 15 HIS B 17 HIS B 214 ASP B 295
SITE 2 AC3 5 HOH B 619
SITE 1 AC4 8 HIS B 17 ASP B 19 TYR B 102 SER B 103
SITE 2 AC4 8 LEU B 106 HOH B 361 HOH B 554 HOH B 639
CRYST1 46.670 93.804 88.048 90.00 105.27 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 0.021427 0.000000 0.005849 0.00000
SCALE2 0.000000 0.010661 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011773 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
