HEADER LYASE/LYASE INHIBITOR 22-AUG-13 4MDG
TITLE CLOSO CARBORANE CARBONIC ANHYDRASE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CARBONATE DEHYDRATASE II, CARBONIC ANHYDRASE C, CAC,
COMPND 5 CARBONIC ANHYDRASE II, CA-II;
COMPND 6 EC: 4.2.1.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS CARBONIC ANHYDRASE INHIBITOR COMPLEX, LYASE-LYASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.BRYNDA,P.MADER,P.REZACOVA
REVDAT 3 28-FEB-24 4MDG 1 REMARK LINK
REVDAT 2 18-MAR-15 4MDG 1 AUTHOR
REVDAT 1 01-JAN-14 4MDG 0
JRNL AUTH J.BRYNDA,P.MADER,V.SICHA,M.FABRY,K.PONCOVA,M.BAKARDIEV,
JRNL AUTH 2 B.GRUNER,P.CIGLER,P.REZACOVA
JRNL TITL CARBORANE-BASED CARBONIC ANHYDRASE INHIBITORS.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 52 13760 2013
JRNL REFN ISSN 1433-7851
JRNL PMID 24307504
JRNL DOI 10.1002/ANIE.201307583
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.0
REMARK 3 NUMBER OF REFLECTIONS : 48010
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) : 0.146
REMARK 3 R VALUE (WORKING SET) : 0.144
REMARK 3 FREE R VALUE : 0.179
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2430
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) : 1.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1853
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 50.63
REMARK 3 BIN R VALUE (WORKING SET) : 0.2060
REMARK 3 BIN FREE R VALUE SET COUNT : 109
REMARK 3 BIN FREE R VALUE : 0.2690
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2035
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 258
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.20000
REMARK 3 B22 (A**2) : 0.27000
REMARK 3 B33 (A**2) : -0.36000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.23000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.062
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.058
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.037
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.809
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2220 ; 0.012 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1499 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3122 ; 1.501 ; 1.992
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3678 ; 1.229 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 283 ; 6.427 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 104 ;36.118 ;24.712
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 360 ;11.980 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;19.094 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 317 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2476 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 444 ; 0.003 ; 0.020
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): 2000 ; 5.440 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1958 ;11.489 ; 5.000
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 : BABINET MODEL WITH 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 4MDG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1000081772.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91840
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48024
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 69.948
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 51.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.34200
REMARK 200 R SYM FOR SHELL (I) : 0.34200
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 20.78500
REMARK 290 SMTRY3 2 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 HIS A 4 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 9 CG CD CE NZ
REMARK 470 LYS A 45 CD CE NZ
REMARK 470 LYS A 133 CE NZ
REMARK 470 LYS A 159 CD CE NZ
REMARK 470 LYS A 172 CE NZ
REMARK 470 LYS A 261 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 ARG A 27 55.78 -142.07
REMARK 500 LEU A 57 -53.91 -122.86
REMARK 500 LYS A 111 -4.04 72.84
REMARK 500 PHE A 176 68.51 -152.85
REMARK 500 ASN A 244 47.81 -94.43
REMARK 500 LYS A 252 -136.62 52.97
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 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 94 NE2
REMARK 620 2 HIS A 96 NE2 106.0
REMARK 620 3 HIS A 119 ND1 112.8 100.2
REMARK 620 4 25X A 302 N2 111.6 108.5 116.4
REMARK 620 N 1 2 3
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 25X A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4MDL RELATED DB: PDB
REMARK 900 RELATED ID: 4MDM RELATED DB: PDB
DBREF 4MDG A 3 261 UNP P00918 CAH2_HUMAN 3 260
SEQRES 1 A 258 HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU HIS
SEQRES 2 A 258 TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG GLN
SEQRES 3 A 258 SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR ASP
SEQRES 4 A 258 PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN ALA
SEQRES 5 A 258 THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE ASN
SEQRES 6 A 258 VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU LYS
SEQRES 7 A 258 GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN PHE
SEQRES 8 A 258 HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER GLU
SEQRES 9 A 258 HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU HIS
SEQRES 10 A 258 LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE GLY LYS
SEQRES 11 A 258 ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY ILE
SEQRES 12 A 258 PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN LYS
SEQRES 13 A 258 VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY LYS
SEQRES 14 A 258 SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU LEU
SEQRES 15 A 258 PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER LEU
SEQRES 16 A 258 THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE VAL
SEQRES 17 A 258 LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL LEU
SEQRES 18 A 258 LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU PRO
SEQRES 19 A 258 GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN PRO
SEQRES 20 A 258 LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET ZN A 301 1
HET 25X A 302 18
HETNAM ZN ZINC ION
HETNAM 25X 1-(SULFAMOYLAMINO)METHYL-1,2-DICARBA-CLOSO-DODECABORANE
FORMUL 2 ZN ZN 2+
FORMUL 3 25X C3 H5 B10 N2 O2 S
FORMUL 4 HOH *258(H2 O)
HELIX 1 1 HIS A 15 ASP A 19 5 5
HELIX 2 2 PHE A 20 GLY A 25 5 6
HELIX 3 3 LYS A 127 GLY A 129 5 3
HELIX 4 4 ASP A 130 VAL A 135 1 6
HELIX 5 5 LYS A 154 GLY A 156 5 3
HELIX 6 6 LEU A 157 LEU A 164 1 8
HELIX 7 7 ASP A 165 LYS A 168 5 4
HELIX 8 8 ASP A 180 LEU A 185 5 6
HELIX 9 9 SER A 219 ARG A 227 1 9
SHEET 1 A 2 ASP A 32 ILE A 33 0
SHEET 2 A 2 THR A 108 VAL A 109 1 O THR A 108 N ILE A 33
SHEET 1 B10 LYS A 39 TYR A 40 0
SHEET 2 B10 LYS A 257 ALA A 258 1 O ALA A 258 N LYS A 39
SHEET 3 B10 TYR A 191 GLY A 196 -1 N THR A 193 O LYS A 257
SHEET 4 B10 VAL A 207 LEU A 212 -1 O VAL A 207 N GLY A 196
SHEET 5 B10 LEU A 141 VAL A 150 1 N GLY A 145 O ILE A 210
SHEET 6 B10 ALA A 116 ASN A 124 -1 N LEU A 118 O ILE A 146
SHEET 7 B10 TYR A 88 TRP A 97 -1 N GLN A 92 O VAL A 121
SHEET 8 B10 PHE A 66 PHE A 70 -1 N VAL A 68 O PHE A 93
SHEET 9 B10 SER A 56 ASN A 61 -1 N LEU A 57 O GLU A 69
SHEET 10 B10 SER A 173 ASP A 175 -1 O ALA A 174 N ILE A 59
SHEET 1 C 6 LEU A 47 SER A 50 0
SHEET 2 C 6 VAL A 78 GLY A 81 -1 O LYS A 80 N SER A 48
SHEET 3 C 6 TYR A 88 TRP A 97 -1 O TYR A 88 N LEU A 79
SHEET 4 C 6 ALA A 116 ASN A 124 -1 O VAL A 121 N GLN A 92
SHEET 5 C 6 LEU A 141 VAL A 150 -1 O ILE A 146 N LEU A 118
SHEET 6 C 6 ILE A 216 VAL A 218 1 O VAL A 218 N LYS A 149
LINK NE2 HIS A 94 ZN ZN A 301 1555 1555 2.05
LINK NE2 HIS A 96 ZN ZN A 301 1555 1555 2.00
LINK ND1 HIS A 119 ZN ZN A 301 1555 1555 2.08
LINK ZN ZN A 301 N2 25X A 302 1555 1555 1.86
CISPEP 1 SER A 29 PRO A 30 0 -4.36
CISPEP 2 PRO A 201 PRO A 202 0 6.47
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 25X A 302
SITE 1 AC2 8 GLN A 92 HIS A 94 HIS A 96 HIS A 119
SITE 2 AC2 8 LEU A 198 THR A 199 THR A 200 ZN A 301
CRYST1 42.100 41.570 72.130 90.00 104.13 90.00 P 1 21 1 2
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 0.023753 0.000000 0.005980 0.00000
SCALE2 0.000000 0.024056 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014296 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
