HEADER LYASE 13-DEC-11 3V3I
TITLE KINETIC AND STRUCTURAL STUDIES OF THERMOSTABILIZED MUTANTS OF HCA II.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND 3 CHAIN: B;
COMPND 4 SYNONYM: CARBONATE DEHYDRATASE II, CARBONIC ANHYDRASE C, CAC,
COMPND 5 CARBONIC ANHYDRASE II, CA-II;
COMPND 6 EC: 4.2.1.1;
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: CA2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS THERMOSTABILE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.BOONE,S.Z.FISHER,R.MCKENNA
REVDAT 4 28-FEB-24 3V3I 1 REMARK SEQADV LINK
REVDAT 3 08-NOV-17 3V3I 1 REMARK
REVDAT 2 01-AUG-12 3V3I 1 JRNL
REVDAT 1 20-JUN-12 3V3I 0
JRNL AUTH Z.FISHER,C.D.BOONE,S.M.BISWAS,B.VENKATAKRISHNAN,M.AGGARWAL,
JRNL AUTH 2 C.TU,M.AGBANDJE-MCKENNA,D.SILVERMAN,R.MCKENNA
JRNL TITL KINETIC AND STRUCTURAL CHARACTERIZATION OF THERMOSTABILIZED
JRNL TITL 2 MUTANTS OF HUMAN CARBONIC ANHYDRASE II.
JRNL REF PROTEIN ENG.DES.SEL. V. 25 347 2012
JRNL REFN ISSN 1741-0126
JRNL PMID 22691706
JRNL DOI 10.1093/PROTEIN/GZS027
REMARK 2
REMARK 2 RESOLUTION. 1.73 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.2_869
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.73
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.46
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.3
REMARK 3 NUMBER OF REFLECTIONS : 20121
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.830
REMARK 3 FREE R VALUE TEST SET COUNT : 1978
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 19.4591 - 4.1552 0.97 1624 178 0.1600 0.1816
REMARK 3 2 4.1552 - 3.3034 0.33 527 57 0.1793 0.2483
REMARK 3 3 3.3034 - 2.8873 0.97 1533 165 0.2103 0.2646
REMARK 3 4 2.8873 - 2.6240 0.99 1539 167 0.2019 0.2550
REMARK 3 5 2.6240 - 2.4363 0.98 1531 168 0.1996 0.2954
REMARK 3 6 2.4363 - 2.2929 0.98 1513 174 0.1938 0.2538
REMARK 3 7 2.2929 - 2.1783 0.40 625 62 0.2068 0.2745
REMARK 3 8 2.1783 - 2.0836 0.99 1514 161 0.1950 0.2804
REMARK 3 9 2.0836 - 2.0034 0.98 1503 173 0.1919 0.2706
REMARK 3 10 2.0034 - 1.9344 0.94 1425 155 0.2073 0.2938
REMARK 3 11 1.9344 - 1.8739 0.32 499 52 0.2013 0.2797
REMARK 3 12 1.8739 - 1.8204 0.96 1460 159 0.2180 0.2773
REMARK 3 13 1.8204 - 1.7725 0.97 1493 173 0.2613 0.3116
REMARK 3 14 1.7725 - 1.7300 0.89 1357 134 0.3015 0.3631
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 21.46
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.550
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.070
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.28960
REMARK 3 B22 (A**2) : 4.28560
REMARK 3 B33 (A**2) : 0.00400
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 : 0.012 2139
REMARK 3 ANGLE : 1.368 2912
REMARK 3 CHIRALITY : 0.083 302
REMARK 3 PLANARITY : 0.007 381
REMARK 3 DIHEDRAL : 13.813 790
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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3V3I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000069548.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : VARIMAX OPTICS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20425
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.729
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.9
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.73
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.36200
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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% W/V PEG 4000 0.2M MAGNESIUM
REMARK 280 CHLORIDE 0.1M TRIS HYDROCHLORIDE, PH 8.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
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 21.00750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.28550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.76300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.28550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.00750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.76300
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: 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 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 B 1
REMARK 465 SER B 2
REMARK 465 HIS B 3
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 LYS B 111 -2.13 74.80
REMARK 500 ASN B 244 45.29 -97.23
REMARK 500 LYS B 252 -122.96 49.43
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 B 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 94 NE2
REMARK 620 2 HIS B 96 NE2 109.2
REMARK 620 3 HIS B 119 ND1 118.6 98.3
REMARK 620 4 HOH B 410 O 103.2 110.6 116.8
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 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3V3F RELATED DB: PDB
REMARK 900 RELATED ID: 3V3G RELATED DB: PDB
REMARK 900 RELATED ID: 3V3H RELATED DB: PDB
REMARK 900 RELATED ID: 3V3J RELATED DB: PDB
DBREF 3V3I B 1 261 UNP P00918 CAH2_HUMAN 1 260
SEQADV 3V3I PHE B 7 UNP P00918 TYR 7 ENGINEERED MUTATION
SEQADV 3V3I GLN B 67 UNP P00918 ASN 67 ENGINEERED MUTATION
SEQADV 3V3I HIS B 100 UNP P00918 LEU 100 ENGINEERED MUTATION
SEQADV 3V3I SER B 224 UNP P00918 LEU 223 ENGINEERED MUTATION
SEQADV 3V3I PRO B 240 UNP P00918 LEU 239 ENGINEERED MUTATION
SEQRES 1 B 260 MET SER HIS HIS TRP GLY PHE GLY LYS HIS ASN GLY PRO
SEQRES 2 B 260 GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES 3 B 260 ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES 4 B 260 TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES 5 B 260 GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA
SEQRES 6 B 260 PHE GLN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES 7 B 260 LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE
SEQRES 8 B 260 GLN PHE HIS PHE HIS TRP GLY SER HIS ASP GLY GLN GLY
SEQRES 9 B 260 SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES 10 B 260 LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE
SEQRES 11 B 260 GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES 12 B 260 GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES 13 B 260 GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS
SEQRES 14 B 260 GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES 15 B 260 LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES 16 B 260 SER LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP
SEQRES 17 B 260 ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES 18 B 260 VAL SER LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES 19 B 260 GLU PRO GLU GLU PRO MET VAL ASP ASN TRP ARG PRO ALA
SEQRES 20 B 260 GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET ZN B 301 1
HET CL B 302 1
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
FORMUL 2 ZN ZN 2+
FORMUL 3 CL CL 1-
FORMUL 4 HOH *89(H2 O)
HELIX 1 1 HIS B 15 ASP B 19 5 5
HELIX 2 2 PHE B 20 GLY B 25 5 6
HELIX 3 3 LYS B 127 GLY B 129 5 3
HELIX 4 4 ASP B 130 VAL B 135 1 6
HELIX 5 5 LYS B 154 GLY B 156 5 3
HELIX 6 6 LEU B 157 LEU B 164 1 8
HELIX 7 7 ASP B 165 LYS B 168 5 4
HELIX 8 8 ASP B 180 LEU B 185 5 6
HELIX 9 9 SER B 219 ARG B 227 1 9
SHEET 1 A 2 ASP B 32 ILE B 33 0
SHEET 2 A 2 THR B 108 VAL B 109 1 O THR B 108 N ILE B 33
SHEET 1 B10 LYS B 39 TYR B 40 0
SHEET 2 B10 LYS B 257 ALA B 258 1 O ALA B 258 N LYS B 39
SHEET 3 B10 TYR B 191 GLY B 196 -1 N THR B 193 O LYS B 257
SHEET 4 B10 VAL B 207 LEU B 212 -1 O VAL B 207 N GLY B 196
SHEET 5 B10 LEU B 141 VAL B 150 1 N GLY B 145 O ILE B 210
SHEET 6 B10 ALA B 116 ASN B 124 -1 N LEU B 118 O ILE B 146
SHEET 7 B10 TYR B 88 TRP B 97 -1 N HIS B 94 O HIS B 119
SHEET 8 B10 PHE B 66 PHE B 70 -1 N VAL B 68 O PHE B 93
SHEET 9 B10 SER B 56 ASN B 61 -1 N LEU B 57 O GLU B 69
SHEET 10 B10 SER B 173 ASP B 175 -1 O ALA B 174 N ILE B 59
SHEET 1 C 6 LEU B 47 SER B 50 0
SHEET 2 C 6 VAL B 78 GLY B 81 -1 O VAL B 78 N SER B 50
SHEET 3 C 6 TYR B 88 TRP B 97 -1 O TYR B 88 N LEU B 79
SHEET 4 C 6 ALA B 116 ASN B 124 -1 O HIS B 119 N HIS B 94
SHEET 5 C 6 LEU B 141 VAL B 150 -1 O ILE B 146 N LEU B 118
SHEET 6 C 6 ILE B 216 VAL B 218 1 O VAL B 218 N LYS B 149
LINK NE2 HIS B 94 ZN ZN B 301 1555 1555 2.06
LINK NE2 HIS B 96 ZN ZN B 301 1555 1555 2.08
LINK ND1 HIS B 119 ZN ZN B 301 1555 1555 2.04
LINK ZN ZN B 301 O HOH B 410 1555 1555 1.98
CISPEP 1 SER B 29 PRO B 30 0 -0.38
CISPEP 2 PRO B 201 PRO B 202 0 16.95
SITE 1 AC1 4 HIS B 94 HIS B 96 HIS B 119 HOH B 410
SITE 1 AC2 2 GLN B 158 GLU B 221
CRYST1 42.015 71.526 74.571 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 0.023801 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013981 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013410 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
