HEADER LYASE 03-FEB-15 4XZ5
TITLE STRUCTURE OF THE THERMOSTABLE ALPHA-CARBONIC ANYDRASE FROM
TITLE 2 THIOMICROSPIRA CRUNOGENA XCL-2 GAMMAPROTEOBACTERIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE, ALPHA FAMILY;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 4.2.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THIOMICROSPIRA CRUNOGENA (STRAIN XCL-2);
SOURCE 3 ORGANISM_TAXID: 317025;
SOURCE 4 STRAIN: XCL-2;
SOURCE 5 GENE: TCR_1545;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CARBONIC ANHYDRASE, THIOMICROSPIRA CRUNOGENA XCL-2, THERMOSTABILITY,
KEYWDS 2 CO2 SEQUESTRATION, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.P.MAHON,N.A.DIAZ-TORRES,M.A.PINARD,R.MCKENNA
REVDAT 7 27-SEP-23 4XZ5 1 LINK
REVDAT 6 25-DEC-19 4XZ5 1 REMARK
REVDAT 5 27-SEP-17 4XZ5 1 REMARK
REVDAT 4 09-AUG-17 4XZ5 1 REMARK
REVDAT 3 26-AUG-15 4XZ5 1 JRNL
REVDAT 2 12-AUG-15 4XZ5 1 JRNL
REVDAT 1 29-JUL-15 4XZ5 0
JRNL AUTH N.A.DIAZ-TORRES,B.P.MAHON,C.D.BOONE,M.A.PINARD,C.TU,R.NG,
JRNL AUTH 2 M.AGBANDJE-MCKENNA,D.SILVERMAN,K.SCOTT,R.MCKENNA
JRNL TITL STRUCTURAL AND BIOPHYSICAL CHARACTERIZATION OF THE
JRNL TITL 2 ALPHA-CARBONIC ANHYDRASE FROM THE GAMMAPROTEOBACTERIUM
JRNL TITL 3 THIOMICROSPIRA CRUNOGENA XCL-2: INSIGHTS INTO ENGINEERING
JRNL TITL 4 THERMOSTABLE ENZYMES FOR CO2 SEQUESTRATION.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 71 1745 2015
JRNL REFN ESSN 1399-0047
JRNL PMID 26249355
JRNL DOI 10.1107/S1399004715012183
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1839)
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.91
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 32782
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1643
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 19.9128 - 5.8966 1.00 2676 140 0.1650 0.2066
REMARK 3 2 5.8966 - 4.7006 1.00 2617 142 0.1396 0.1880
REMARK 3 3 4.7006 - 4.1124 1.00 2622 138 0.1354 0.1930
REMARK 3 4 4.1124 - 3.7391 1.00 2606 137 0.1545 0.2258
REMARK 3 5 3.7391 - 3.4726 1.00 2637 138 0.1670 0.2111
REMARK 3 6 3.4726 - 3.2688 1.00 2563 135 0.1800 0.2816
REMARK 3 7 3.2688 - 3.1057 1.00 2630 135 0.1947 0.2805
REMARK 3 8 3.1057 - 2.9710 1.00 2605 140 0.2042 0.2743
REMARK 3 9 2.9710 - 2.8570 1.00 2616 139 0.2028 0.2820
REMARK 3 10 2.8570 - 2.7586 1.00 2580 137 0.2055 0.3162
REMARK 3 11 2.7586 - 2.6726 0.99 2578 135 0.2272 0.3379
REMARK 3 12 2.6726 - 2.5964 0.92 2409 127 0.2146 0.3058
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.440
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.87
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.009 7692
REMARK 3 ANGLE : 1.303 10436
REMARK 3 CHIRALITY : 0.056 1072
REMARK 3 PLANARITY : 0.008 1352
REMARK 3 DIHEDRAL : 14.936 2852
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -21.3263 -21.5212 189.9641
REMARK 3 T TENSOR
REMARK 3 T11: 0.0439 T22: 0.0468
REMARK 3 T33: 0.0396 T12: -0.0241
REMARK 3 T13: 0.0006 T23: -0.0247
REMARK 3 L TENSOR
REMARK 3 L11: 0.0584 L22: 0.0343
REMARK 3 L33: 0.0372 L12: 0.0030
REMARK 3 L13: -0.0115 L23: 0.0022
REMARK 3 S TENSOR
REMARK 3 S11: 0.0510 S12: 0.0325 S13: -0.0399
REMARK 3 S21: 0.0020 S22: -0.0235 S23: -0.0500
REMARK 3 S31: -0.0126 S32: -0.0542 S33: 0.0341
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
REMARK 3 SELECTION : CHAIN B
REMARK 3 ATOM PAIRS NUMBER : 4533
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN C
REMARK 3 ATOM PAIRS NUMBER : 4533
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 4533
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4XZ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000206564.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9177
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32793
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.40500
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: PHASER, PHENIX
REMARK 200 STARTING MODEL: 3KS3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE TRIHYDRATE PH
REMARK 280 4.6, 16% W/V PEG 3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 63.52950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.11400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 63.52950
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 51.11400
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 ARG A 305
REMARK 465 ASN A 306
REMARK 465 ALA A 307
REMARK 465 ARG B 305
REMARK 465 ASN B 306
REMARK 465 ALA B 307
REMARK 465 ARG C 305
REMARK 465 ASN C 306
REMARK 465 ALA C 307
REMARK 465 ARG D 305
REMARK 465 ASN D 306
REMARK 465 ALA D 307
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NH2 ARG A 129 O GLU C 203 2.13
REMARK 500 OG SER C 120 OD1 ASP D 304 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG B 129 O GLU D 203 3545 2.03
REMARK 500 NE2 GLN A 202 OE1 GLU B 208 47410 2.06
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 SER A 120 38.45 -151.01
REMARK 500 GLU A 225 81.45 49.71
REMARK 500 ASN A 294 -125.97 54.07
REMARK 500 SER B 120 37.81 -153.75
REMARK 500 GLU B 225 76.15 50.83
REMARK 500 ASN B 294 -123.59 54.67
REMARK 500 SER C 120 40.85 -152.67
REMARK 500 GLU C 225 75.67 50.25
REMARK 500 ASN C 294 -126.87 54.81
REMARK 500 ALA D 93 147.73 -173.36
REMARK 500 SER D 120 41.85 -153.41
REMARK 500 GLU D 225 78.02 50.80
REMARK 500 ASN D 294 -124.80 55.56
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 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 165 NE2
REMARK 620 2 HIS A 167 NE2 99.7
REMARK 620 3 HIS A 184 ND1 123.0 97.2
REMARK 620 4 BCT A 402 O3 98.5 123.9 115.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 165 NE2
REMARK 620 2 HIS B 167 NE2 102.1
REMARK 620 3 HIS B 184 ND1 107.3 100.4
REMARK 620 4 BCT B 402 O2 102.6 120.8 121.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 165 NE2
REMARK 620 2 HIS C 167 NE2 102.8
REMARK 620 3 HIS C 184 ND1 112.0 97.0
REMARK 620 4 BCT C 402 O1 97.8 126.5 119.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 165 NE2
REMARK 620 2 HIS D 167 NE2 100.4
REMARK 620 3 HIS D 184 ND1 115.3 102.5
REMARK 620 4 BCT D 402 O2 102.8 116.9 118.0
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT D 402
DBREF 4XZ5 A 75 306 UNP Q31FD6 Q31FD6_THICR 75 306
DBREF 4XZ5 B 75 306 UNP Q31FD6 Q31FD6_THICR 75 306
DBREF 4XZ5 C 75 306 UNP Q31FD6 Q31FD6_THICR 75 306
DBREF 4XZ5 D 75 306 UNP Q31FD6 Q31FD6_THICR 75 306
SEQADV 4XZ5 ALA A 307 UNP Q31FD6 EXPRESSION TAG
SEQADV 4XZ5 ALA B 307 UNP Q31FD6 EXPRESSION TAG
SEQADV 4XZ5 ALA C 307 UNP Q31FD6 EXPRESSION TAG
SEQADV 4XZ5 ALA D 307 UNP Q31FD6 EXPRESSION TAG
SEQRES 1 A 233 PRO PRO HIS TRP GLY TYR PHE GLY GLU GLU GLY PRO GLN
SEQRES 2 A 233 TYR TRP GLY GLU LEU ALA PRO GLU PHE SER THR CYS LYS
SEQRES 3 A 233 THR GLY LYS ASN GLN SER PRO ILE ASN LEU LYS PRO GLN
SEQRES 4 A 233 THR ALA VAL GLY THR THR SER LEU PRO GLY PHE ASP VAL
SEQRES 5 A 233 TYR TYR ARG GLU THR ALA LEU LYS LEU ILE ASN ASN GLY
SEQRES 6 A 233 HIS THR LEU GLN VAL ASN ILE PRO LEU GLY SER TYR ILE
SEQRES 7 A 233 LYS ILE ASN GLY HIS ARG TYR GLU LEU LEU GLN TYR HIS
SEQRES 8 A 233 PHE HIS THR PRO SER GLU HIS GLN ARG ASP GLY PHE ASN
SEQRES 9 A 233 TYR PRO MET GLU MET HIS LEU VAL HIS LYS ASP GLY ASP
SEQRES 10 A 233 GLY ASN LEU ALA VAL ILE ALA ILE LEU PHE GLN GLU GLY
SEQRES 11 A 233 GLU GLU ASN GLU THR LEU ALA LYS LEU MET SER PHE LEU
SEQRES 12 A 233 PRO GLN THR LEU LYS LYS GLN GLU ILE HIS GLU SER VAL
SEQRES 13 A 233 LYS ILE HIS PRO ALA LYS PHE PHE PRO ALA ASP LYS LYS
SEQRES 14 A 233 PHE TYR LYS TYR SER GLY SER LEU THR THR PRO PRO CYS
SEQRES 15 A 233 SER GLU GLY VAL TYR TRP MET VAL PHE LYS GLN PRO ILE
SEQRES 16 A 233 GLN ALA SER VAL THR GLN LEU GLU LYS MET HIS GLU TYR
SEQRES 17 A 233 LEU GLY SER ASN ALA ARG PRO VAL GLN ARG GLN ASN ALA
SEQRES 18 A 233 ARG THR LEU LEU LYS SER TRP PRO ASP ARG ASN ALA
SEQRES 1 B 233 PRO PRO HIS TRP GLY TYR PHE GLY GLU GLU GLY PRO GLN
SEQRES 2 B 233 TYR TRP GLY GLU LEU ALA PRO GLU PHE SER THR CYS LYS
SEQRES 3 B 233 THR GLY LYS ASN GLN SER PRO ILE ASN LEU LYS PRO GLN
SEQRES 4 B 233 THR ALA VAL GLY THR THR SER LEU PRO GLY PHE ASP VAL
SEQRES 5 B 233 TYR TYR ARG GLU THR ALA LEU LYS LEU ILE ASN ASN GLY
SEQRES 6 B 233 HIS THR LEU GLN VAL ASN ILE PRO LEU GLY SER TYR ILE
SEQRES 7 B 233 LYS ILE ASN GLY HIS ARG TYR GLU LEU LEU GLN TYR HIS
SEQRES 8 B 233 PHE HIS THR PRO SER GLU HIS GLN ARG ASP GLY PHE ASN
SEQRES 9 B 233 TYR PRO MET GLU MET HIS LEU VAL HIS LYS ASP GLY ASP
SEQRES 10 B 233 GLY ASN LEU ALA VAL ILE ALA ILE LEU PHE GLN GLU GLY
SEQRES 11 B 233 GLU GLU ASN GLU THR LEU ALA LYS LEU MET SER PHE LEU
SEQRES 12 B 233 PRO GLN THR LEU LYS LYS GLN GLU ILE HIS GLU SER VAL
SEQRES 13 B 233 LYS ILE HIS PRO ALA LYS PHE PHE PRO ALA ASP LYS LYS
SEQRES 14 B 233 PHE TYR LYS TYR SER GLY SER LEU THR THR PRO PRO CYS
SEQRES 15 B 233 SER GLU GLY VAL TYR TRP MET VAL PHE LYS GLN PRO ILE
SEQRES 16 B 233 GLN ALA SER VAL THR GLN LEU GLU LYS MET HIS GLU TYR
SEQRES 17 B 233 LEU GLY SER ASN ALA ARG PRO VAL GLN ARG GLN ASN ALA
SEQRES 18 B 233 ARG THR LEU LEU LYS SER TRP PRO ASP ARG ASN ALA
SEQRES 1 C 233 PRO PRO HIS TRP GLY TYR PHE GLY GLU GLU GLY PRO GLN
SEQRES 2 C 233 TYR TRP GLY GLU LEU ALA PRO GLU PHE SER THR CYS LYS
SEQRES 3 C 233 THR GLY LYS ASN GLN SER PRO ILE ASN LEU LYS PRO GLN
SEQRES 4 C 233 THR ALA VAL GLY THR THR SER LEU PRO GLY PHE ASP VAL
SEQRES 5 C 233 TYR TYR ARG GLU THR ALA LEU LYS LEU ILE ASN ASN GLY
SEQRES 6 C 233 HIS THR LEU GLN VAL ASN ILE PRO LEU GLY SER TYR ILE
SEQRES 7 C 233 LYS ILE ASN GLY HIS ARG TYR GLU LEU LEU GLN TYR HIS
SEQRES 8 C 233 PHE HIS THR PRO SER GLU HIS GLN ARG ASP GLY PHE ASN
SEQRES 9 C 233 TYR PRO MET GLU MET HIS LEU VAL HIS LYS ASP GLY ASP
SEQRES 10 C 233 GLY ASN LEU ALA VAL ILE ALA ILE LEU PHE GLN GLU GLY
SEQRES 11 C 233 GLU GLU ASN GLU THR LEU ALA LYS LEU MET SER PHE LEU
SEQRES 12 C 233 PRO GLN THR LEU LYS LYS GLN GLU ILE HIS GLU SER VAL
SEQRES 13 C 233 LYS ILE HIS PRO ALA LYS PHE PHE PRO ALA ASP LYS LYS
SEQRES 14 C 233 PHE TYR LYS TYR SER GLY SER LEU THR THR PRO PRO CYS
SEQRES 15 C 233 SER GLU GLY VAL TYR TRP MET VAL PHE LYS GLN PRO ILE
SEQRES 16 C 233 GLN ALA SER VAL THR GLN LEU GLU LYS MET HIS GLU TYR
SEQRES 17 C 233 LEU GLY SER ASN ALA ARG PRO VAL GLN ARG GLN ASN ALA
SEQRES 18 C 233 ARG THR LEU LEU LYS SER TRP PRO ASP ARG ASN ALA
SEQRES 1 D 233 PRO PRO HIS TRP GLY TYR PHE GLY GLU GLU GLY PRO GLN
SEQRES 2 D 233 TYR TRP GLY GLU LEU ALA PRO GLU PHE SER THR CYS LYS
SEQRES 3 D 233 THR GLY LYS ASN GLN SER PRO ILE ASN LEU LYS PRO GLN
SEQRES 4 D 233 THR ALA VAL GLY THR THR SER LEU PRO GLY PHE ASP VAL
SEQRES 5 D 233 TYR TYR ARG GLU THR ALA LEU LYS LEU ILE ASN ASN GLY
SEQRES 6 D 233 HIS THR LEU GLN VAL ASN ILE PRO LEU GLY SER TYR ILE
SEQRES 7 D 233 LYS ILE ASN GLY HIS ARG TYR GLU LEU LEU GLN TYR HIS
SEQRES 8 D 233 PHE HIS THR PRO SER GLU HIS GLN ARG ASP GLY PHE ASN
SEQRES 9 D 233 TYR PRO MET GLU MET HIS LEU VAL HIS LYS ASP GLY ASP
SEQRES 10 D 233 GLY ASN LEU ALA VAL ILE ALA ILE LEU PHE GLN GLU GLY
SEQRES 11 D 233 GLU GLU ASN GLU THR LEU ALA LYS LEU MET SER PHE LEU
SEQRES 12 D 233 PRO GLN THR LEU LYS LYS GLN GLU ILE HIS GLU SER VAL
SEQRES 13 D 233 LYS ILE HIS PRO ALA LYS PHE PHE PRO ALA ASP LYS LYS
SEQRES 14 D 233 PHE TYR LYS TYR SER GLY SER LEU THR THR PRO PRO CYS
SEQRES 15 D 233 SER GLU GLY VAL TYR TRP MET VAL PHE LYS GLN PRO ILE
SEQRES 16 D 233 GLN ALA SER VAL THR GLN LEU GLU LYS MET HIS GLU TYR
SEQRES 17 D 233 LEU GLY SER ASN ALA ARG PRO VAL GLN ARG GLN ASN ALA
SEQRES 18 D 233 ARG THR LEU LEU LYS SER TRP PRO ASP ARG ASN ALA
HET ZN A 401 1
HET BCT A 402 4
HET ZN B 401 1
HET BCT B 402 4
HET ZN C 401 1
HET BCT C 402 4
HET ZN D 401 1
HET BCT D 402 4
HETNAM ZN ZINC ION
HETNAM BCT BICARBONATE ION
FORMUL 5 ZN 4(ZN 2+)
FORMUL 6 BCT 4(C H O3 1-)
FORMUL 13 HOH *37(H2 O)
HELIX 1 AA1 PHE A 81 LEU A 92 5 12
HELIX 2 AA2 ALA A 93 PHE A 96 5 4
HELIX 3 AA3 SER A 97 GLY A 102 1 6
HELIX 4 AA4 ASN A 207 SER A 215 1 9
HELIX 5 AA5 HIS A 233 PHE A 238 5 6
HELIX 6 AA6 SER A 272 GLY A 284 1 13
HELIX 7 AA7 PHE B 81 GLN B 87 5 7
HELIX 8 AA8 TYR B 88 ALA B 93 1 6
HELIX 9 AA9 PRO B 94 PHE B 96 5 3
HELIX 10 AB1 SER B 97 GLY B 102 1 6
HELIX 11 AB2 ASN B 207 SER B 215 1 9
HELIX 12 AB3 HIS B 233 PHE B 238 5 6
HELIX 13 AB4 SER B 272 GLY B 284 1 13
HELIX 14 AB5 PHE C 81 LEU C 92 5 12
HELIX 15 AB6 ALA C 93 PHE C 96 5 4
HELIX 16 AB7 SER C 97 GLY C 102 1 6
HELIX 17 AB8 ASN C 207 SER C 215 1 9
HELIX 18 AB9 HIS C 233 PHE C 238 5 6
HELIX 19 AC1 SER C 272 GLY C 284 1 13
HELIX 20 AC2 PHE D 81 GLN D 87 5 7
HELIX 21 AC3 TYR D 88 ALA D 93 1 6
HELIX 22 AC4 PRO D 94 PHE D 96 5 3
HELIX 23 AC5 SER D 97 GLY D 102 1 6
HELIX 24 AC6 ASN D 207 PHE D 216 1 10
HELIX 25 AC7 HIS D 233 PHE D 238 5 6
HELIX 26 AC8 SER D 272 GLY D 284 1 13
SHEET 1 AA1 3 ASN A 109 LEU A 110 0
SHEET 2 AA1 3 GLN A 173 ARG A 174 1 O GLN A 173 N LEU A 110
SHEET 3 AA1 3 PHE A 177 ASN A 178 -1 O PHE A 177 N ARG A 174
SHEET 1 AA2 6 PHE A 124 TYR A 127 0
SHEET 2 AA2 6 TYR A 151 ILE A 154 -1 O TYR A 151 N TYR A 127
SHEET 3 AA2 6 HIS A 157 HIS A 167 -1 O HIS A 157 N ILE A 154
SHEET 4 AA2 6 MET A 181 LYS A 188 -1 O GLU A 182 N HIS A 167
SHEET 5 AA2 6 LEU A 194 GLU A 203 -1 O ILE A 197 N LEU A 185
SHEET 6 AA2 6 ILE A 269 ALA A 271 1 O ILE A 269 N LEU A 200
SHEET 1 AA3 9 ILE A 226 LYS A 231 0
SHEET 2 AA3 9 ALA A 132 ASN A 137 -1 N LEU A 133 O HIS A 227
SHEET 3 AA3 9 LEU A 142 ASN A 145 -1 O GLN A 143 N ILE A 136
SHEET 4 AA3 9 HIS A 157 HIS A 167 -1 O TYR A 164 N VAL A 144
SHEET 5 AA3 9 MET A 181 LYS A 188 -1 O GLU A 182 N HIS A 167
SHEET 6 AA3 9 LEU A 194 GLU A 203 -1 O ILE A 197 N LEU A 185
SHEET 7 AA3 9 GLU A 258 PHE A 265 1 O TYR A 261 N VAL A 196
SHEET 8 AA3 9 PHE A 244 SER A 250 -1 N GLY A 249 O VAL A 260
SHEET 9 AA3 9 LEU A 299 LYS A 300 -1 O LEU A 299 N LYS A 246
SHEET 1 AA4 3 ASN B 109 LEU B 110 0
SHEET 2 AA4 3 GLN B 173 ARG B 174 1 O GLN B 173 N LEU B 110
SHEET 3 AA4 3 PHE B 177 ASN B 178 -1 O PHE B 177 N ARG B 174
SHEET 1 AA5 6 PHE B 124 TYR B 127 0
SHEET 2 AA5 6 TYR B 151 ILE B 154 -1 O TYR B 151 N TYR B 127
SHEET 3 AA5 6 HIS B 157 HIS B 167 -1 O HIS B 157 N ILE B 154
SHEET 4 AA5 6 MET B 181 LYS B 188 -1 O GLU B 182 N HIS B 167
SHEET 5 AA5 6 LEU B 194 GLU B 203 -1 O ILE B 197 N LEU B 185
SHEET 6 AA5 6 ILE B 269 ALA B 271 1 O ILE B 269 N LEU B 200
SHEET 1 AA6 9 ILE B 226 LYS B 231 0
SHEET 2 AA6 9 ALA B 132 ASN B 137 -1 N LEU B 133 O HIS B 227
SHEET 3 AA6 9 LEU B 142 ASN B 145 -1 O GLN B 143 N ILE B 136
SHEET 4 AA6 9 HIS B 157 HIS B 167 -1 O TYR B 164 N VAL B 144
SHEET 5 AA6 9 MET B 181 LYS B 188 -1 O GLU B 182 N HIS B 167
SHEET 6 AA6 9 LEU B 194 GLU B 203 -1 O ILE B 197 N LEU B 185
SHEET 7 AA6 9 GLU B 258 PHE B 265 1 O MET B 263 N ALA B 198
SHEET 8 AA6 9 PHE B 244 SER B 250 -1 N GLY B 249 O VAL B 260
SHEET 9 AA6 9 LEU B 299 LYS B 300 -1 O LEU B 299 N LYS B 246
SHEET 1 AA7 3 ASN C 109 LEU C 110 0
SHEET 2 AA7 3 GLN C 173 ARG C 174 1 O GLN C 173 N LEU C 110
SHEET 3 AA7 3 PHE C 177 ASN C 178 -1 O PHE C 177 N ARG C 174
SHEET 1 AA8 6 PHE C 124 TYR C 127 0
SHEET 2 AA8 6 TYR C 151 ILE C 154 -1 O LYS C 153 N ASP C 125
SHEET 3 AA8 6 HIS C 157 HIS C 167 -1 O TYR C 159 N ILE C 152
SHEET 4 AA8 6 MET C 181 LYS C 188 -1 O VAL C 186 N LEU C 162
SHEET 5 AA8 6 LEU C 194 GLU C 203 -1 O ILE C 197 N LEU C 185
SHEET 6 AA8 6 ILE C 269 ALA C 271 1 O ILE C 269 N LEU C 200
SHEET 1 AA9 9 ILE C 226 LYS C 231 0
SHEET 2 AA9 9 ALA C 132 ASN C 137 -1 N LEU C 133 O HIS C 227
SHEET 3 AA9 9 LEU C 142 ASN C 145 -1 O GLN C 143 N ILE C 136
SHEET 4 AA9 9 HIS C 157 HIS C 167 -1 O TYR C 164 N VAL C 144
SHEET 5 AA9 9 MET C 181 LYS C 188 -1 O VAL C 186 N LEU C 162
SHEET 6 AA9 9 LEU C 194 GLU C 203 -1 O ILE C 197 N LEU C 185
SHEET 7 AA9 9 GLU C 258 PHE C 265 1 O TYR C 261 N LEU C 194
SHEET 8 AA9 9 PHE C 244 SER C 250 -1 N TYR C 245 O VAL C 264
SHEET 9 AA9 9 LEU C 299 LYS C 300 -1 O LEU C 299 N LYS C 246
SHEET 1 AB1 3 ASN D 109 LEU D 110 0
SHEET 2 AB1 3 GLN D 173 ARG D 174 1 O GLN D 173 N LEU D 110
SHEET 3 AB1 3 PHE D 177 ASN D 178 -1 O PHE D 177 N ARG D 174
SHEET 1 AB2 6 PHE D 124 TYR D 127 0
SHEET 2 AB2 6 TYR D 151 ILE D 154 -1 O TYR D 151 N TYR D 127
SHEET 3 AB2 6 HIS D 157 HIS D 167 -1 O HIS D 157 N ILE D 154
SHEET 4 AB2 6 MET D 181 LYS D 188 -1 O LYS D 188 N GLU D 160
SHEET 5 AB2 6 LEU D 194 GLU D 203 -1 O ILE D 199 N MET D 183
SHEET 6 AB2 6 ILE D 269 ALA D 271 1 O ILE D 269 N LEU D 200
SHEET 1 AB3 9 ILE D 226 LYS D 231 0
SHEET 2 AB3 9 ALA D 132 ASN D 137 -1 N LEU D 133 O HIS D 227
SHEET 3 AB3 9 LEU D 142 ASN D 145 -1 O GLN D 143 N ILE D 136
SHEET 4 AB3 9 HIS D 157 HIS D 167 -1 O TYR D 164 N VAL D 144
SHEET 5 AB3 9 MET D 181 LYS D 188 -1 O LYS D 188 N GLU D 160
SHEET 6 AB3 9 LEU D 194 GLU D 203 -1 O ILE D 199 N MET D 183
SHEET 7 AB3 9 GLU D 258 PHE D 265 1 O MET D 263 N ALA D 198
SHEET 8 AB3 9 PHE D 244 SER D 250 -1 N GLY D 249 O VAL D 260
SHEET 9 AB3 9 LEU D 299 LYS D 300 -1 O LEU D 299 N LYS D 246
SSBOND 1 CYS A 99 CYS A 256 1555 1555 2.06
SSBOND 2 CYS B 99 CYS B 256 1555 1555 2.05
SSBOND 3 CYS C 99 CYS C 256 1555 1555 2.05
SSBOND 4 CYS D 99 CYS D 256 1555 1555 2.05
LINK NE2 HIS A 165 ZN ZN A 401 1555 1555 2.05
LINK NE2 HIS A 167 ZN ZN A 401 1555 1555 2.13
LINK ND1 HIS A 184 ZN ZN A 401 1555 1555 2.03
LINK ZN ZN A 401 O3 BBCT A 402 1555 1555 1.98
LINK NE2 HIS B 165 ZN ZN B 401 1555 1555 2.02
LINK NE2 HIS B 167 ZN ZN B 401 1555 1555 2.13
LINK ND1 HIS B 184 ZN ZN B 401 1555 1555 1.99
LINK ZN ZN B 401 O2 BBCT B 402 1555 1555 2.10
LINK NE2 HIS C 165 ZN ZN C 401 1555 1555 2.01
LINK NE2 HIS C 167 ZN ZN C 401 1555 1555 2.05
LINK ND1 HIS C 184 ZN ZN C 401 1555 1555 1.96
LINK ZN ZN C 401 O1 BBCT C 402 1555 1555 2.14
LINK NE2 HIS D 165 ZN ZN D 401 1555 1555 1.99
LINK NE2 HIS D 167 ZN ZN D 401 1555 1555 2.16
LINK ND1 HIS D 184 ZN ZN D 401 1555 1555 2.13
LINK ZN ZN D 401 O2 BBCT D 402 1555 1555 1.91
CISPEP 1 SER A 106 PRO A 107 0 -2.20
CISPEP 2 THR A 168 PRO A 169 0 -8.39
CISPEP 3 PRO A 254 PRO A 255 0 2.34
CISPEP 4 SER B 106 PRO B 107 0 -3.24
CISPEP 5 THR B 168 PRO B 169 0 -8.68
CISPEP 6 PRO B 254 PRO B 255 0 2.51
CISPEP 7 SER C 106 PRO C 107 0 -1.69
CISPEP 8 THR C 168 PRO C 169 0 -6.86
CISPEP 9 PRO C 254 PRO C 255 0 3.53
CISPEP 10 SER D 106 PRO D 107 0 -3.08
CISPEP 11 THR D 168 PRO D 169 0 -9.46
CISPEP 12 PRO D 254 PRO D 255 0 3.04
SITE 1 AC1 4 HIS A 165 HIS A 167 HIS A 184 BCT A 402
SITE 1 AC2 6 HIS A 165 HIS A 167 HIS A 184 LEU A 251
SITE 2 AC2 6 THR A 252 ZN A 401
SITE 1 AC3 5 HIS B 165 HIS B 167 HIS B 184 THR B 252
SITE 2 AC3 5 BCT B 402
SITE 1 AC4 6 HIS B 165 HIS B 167 HIS B 184 LEU B 251
SITE 2 AC4 6 THR B 252 ZN B 401
SITE 1 AC5 4 HIS C 165 HIS C 167 HIS C 184 BCT C 402
SITE 1 AC6 5 HIS C 165 HIS C 184 LEU C 251 THR C 252
SITE 2 AC6 5 ZN C 401
SITE 1 AC7 4 HIS D 165 HIS D 167 HIS D 184 BCT D 402
SITE 1 AC8 6 HIS D 165 HIS D 167 HIS D 184 LEU D 251
SITE 2 AC8 6 THR D 252 ZN D 401
CRYST1 127.059 102.228 105.021 90.00 127.26 90.00 C 1 2 1 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 0.007870 0.000000 0.005986 0.00000
SCALE2 0.000000 0.009782 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011963 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
