HEADER HYDROLASE 09-JUN-17 5O7N
TITLE BETA-LACTAMASE VIM-2 IN COMPLEX WITH (2R)-1-(2-BENZYL-3-
TITLE 2 MERCAPTOPROPANOYL)PIPERIDINE-2-CARBOXYLIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-LACTAMASE VIM-2;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KLEBSIELLA PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 573;
SOURCE 4 GENE: BLAVIM-2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PDEST14
KEYWDS INHIBITOR, COMPLEX, MBL, BETA-LACTAMASE VIM-2, (2R)-1-(2-BENZYL-3-
KEYWDS 2 MERCAPTOPROPANOYL)PIPERIDINE-2-CARBOXYLIC ACID, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.BUETTNER,J.S.KRAMER,D.POGORYELOV,E.PROSCHAK
REVDAT 3 08-MAY-24 5O7N 1 LINK
REVDAT 2 03-JUL-19 5O7N 1 JRNL
REVDAT 1 20-JUN-18 5O7N 0
JRNL AUTH D.BUTTNER,J.S.KRAMER,F.M.KLINGLER,S.K.WITTMANN,M.R.HARTMANN,
JRNL AUTH 2 C.G.KURZ,D.KOHNHAUSER,L.WEIZEL,A.BRUGGERHOFF,D.FRANK,
JRNL AUTH 3 D.STEINHILBER,T.A.WICHELHAUS,D.POGORYELOV,E.PROSCHAK
JRNL TITL CHALLENGES IN THE DEVELOPMENT OF A THIOL-BASED
JRNL TITL 2 BROAD-SPECTRUM INHIBITOR FOR METALLO-BETA-LACTAMASES.
JRNL REF ACS INFECT DIS. V. 4 360 2018
JRNL REFN ESSN 2373-8227
JRNL PMID 29172434
JRNL DOI 10.1021/ACSINFECDIS.7B00129
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.51
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 128064
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.790
REMARK 3 FREE R VALUE TEST SET COUNT : 3573
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 51.4800 - 4.4430 0.99 4822 137 0.1752 0.1787
REMARK 3 2 4.4430 - 3.5267 1.00 4819 140 0.1513 0.1873
REMARK 3 3 3.5267 - 3.0810 1.00 4801 152 0.1659 0.1811
REMARK 3 4 3.0810 - 2.7993 1.00 4832 146 0.0000 0.2400
REMARK 3 5 2.7993 - 2.5987 1.00 4795 142 0.0000 0.1874
REMARK 3 6 2.5987 - 2.4454 0.94 4618 125 0.0000 0.1753
REMARK 3 7 2.4454 - 2.3230 0.94 4492 122 0.0000 0.2314
REMARK 3 8 2.3230 - 2.2219 0.98 4771 135 0.1862 0.2350
REMARK 3 9 2.2219 - 2.1363 0.99 4780 128 0.1788 0.2213
REMARK 3 10 2.1363 - 2.0626 0.99 4805 131 0.1716 0.2016
REMARK 3 11 2.0626 - 1.9981 0.99 4762 148 0.1711 0.1835
REMARK 3 12 1.9981 - 1.9410 1.00 4820 120 0.1705 0.1807
REMARK 3 13 1.9410 - 1.8899 1.00 4803 141 0.1803 0.2025
REMARK 3 14 1.8899 - 1.8438 1.00 4810 147 0.1807 0.2209
REMARK 3 15 1.8438 - 1.8019 1.00 4797 143 0.1988 0.2217
REMARK 3 16 1.8019 - 1.7635 1.00 4800 126 0.2145 0.2771
REMARK 3 17 1.7635 - 1.7282 1.00 4842 146 0.2237 0.2483
REMARK 3 18 1.7282 - 1.6956 1.00 4850 142 0.2303 0.2280
REMARK 3 19 1.6956 - 1.6653 1.00 4826 138 0.2304 0.2927
REMARK 3 20 1.6653 - 1.6371 1.00 4807 134 0.2436 0.2714
REMARK 3 21 1.6371 - 1.6107 1.00 4819 128 0.2432 0.2711
REMARK 3 22 1.6107 - 1.5859 1.00 4816 152 0.2463 0.2772
REMARK 3 23 1.5859 - 1.5626 1.00 4789 126 0.2538 0.2502
REMARK 3 24 1.5626 - 1.5406 1.00 4796 145 0.2601 0.2837
REMARK 3 25 1.5406 - 1.5197 1.00 4798 133 0.2749 0.2742
REMARK 3 26 1.5197 - 1.5000 1.00 4821 146 0.2836 0.2915
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.97
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.20
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 : 0.007 3730
REMARK 3 ANGLE : 0.936 5094
REMARK 3 CHIRALITY : 0.065 574
REMARK 3 PLANARITY : 0.006 674
REMARK 3 DIHEDRAL : 19.994 1304
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 5O7N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1200002178.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-SEP-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : MASSIF-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9677
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 128072
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 55.507
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.07561
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.54090
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.170
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: AUTOSOL, PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 32.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE VIM-2 IN CRYSTALLIZATION BUFFER
REMARK 280 (50 MM TRIS/HCL PH 7.2, 100 UM ZNCL2 AND 150 MM NACL) WAS
REMARK 280 CONCENTRATED TO 11,4 MG/ML, BEFORE 5 % GLYCEROL WAS ADDED AND
REMARK 280 THE PROTEIN WAS FLASH FROZEN IN LIQUID NITROGEN. FOR
REMARK 280 CRYSTALLISATION THE THRAWED PROTEIN SOLUTIONS WAS MIXED WITH
REMARK 280 PRECIPITATION SOLUTION (34% PEG3350, 0,25 M MG FORMATE, 5 MM BME
REMARK 280 + 2.5% OF A 1M DMSO INHIBITOR STOCK IN THE DROP) IN DIFFERANT
REMARK 280 RATIOS. AS RESERVOIR PRECIPITATION SOLUTION WITHOUT INHIBITOR
REMARK 280 WAS USED., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290.15K
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 50.99450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.65400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 50.99450
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 39.65400
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 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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 435 LIES ON A SPECIAL POSITION.
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 13
REMARK 465 HIS A 14
REMARK 465 HIS A 15
REMARK 465 HIS A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 HIS A 19
REMARK 465 GLU A 20
REMARK 465 ASN A 21
REMARK 465 LEU A 22
REMARK 465 TYR A 23
REMARK 465 PHE A 24
REMARK 465 GLN A 25
REMARK 465 GLY A 26
REMARK 465 VAL A 27
REMARK 465 ASP A 28
REMARK 465 SER A 29
REMARK 465 SER A 30
REMARK 465 VAL A 36
REMARK 465 SER A 37
REMARK 465 VAL A 264
REMARK 465 VAL A 265
REMARK 465 GLU A 266
REMARK 465 MET B 13
REMARK 465 HIS B 14
REMARK 465 HIS B 15
REMARK 465 HIS B 16
REMARK 465 HIS B 17
REMARK 465 HIS B 18
REMARK 465 HIS B 19
REMARK 465 GLU B 20
REMARK 465 ASN B 21
REMARK 465 LEU B 22
REMARK 465 TYR B 23
REMARK 465 PHE B 24
REMARK 465 GLN B 25
REMARK 465 GLY B 26
REMARK 465 VAL B 27
REMARK 465 ASP B 28
REMARK 465 SER B 29
REMARK 465 SER B 30
REMARK 465 GLY B 31
REMARK 465 VAL B 264
REMARK 465 VAL B 265
REMARK 465 GLU B 266
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 O HOH A 539 O HOH A 557 1.84
REMARK 500 O HOH A 414 O HOH A 532 1.95
REMARK 500 O HOH A 519 O HOH A 523 1.97
REMARK 500 O HOH A 533 O HOH A 534 1.99
REMARK 500 O HOH A 506 O HOH A 550 2.04
REMARK 500 OE1 GLU A 43 NH2 ARG A 45 2.07
REMARK 500 O HOH B 497 O HOH B 556 2.14
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 O HOH A 477 O HOH B 534 3454 2.15
REMARK 500 O HOH A 444 O HOH A 504 4747 2.18
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 ASP A 84 145.46 72.09
REMARK 500 TRP A 87 68.80 70.71
REMARK 500 ALA A 178 -105.33 -150.38
REMARK 500 ASP B 84 148.17 75.02
REMARK 500 TRP B 87 72.06 69.51
REMARK 500 ALA B 178 -106.63 -151.43
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 A 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 114 NE2
REMARK 620 2 HIS A 116 ND1 96.1
REMARK 620 3 HIS A 179 NE2 102.1 106.3
REMARK 620 4 9NK A 305 S01 132.0 104.1 112.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 118 OD2
REMARK 620 2 CYS A 198 SG 116.6
REMARK 620 3 HIS A 240 NE2 95.1 109.3
REMARK 620 4 9NK A 305 S01 97.9 116.6 119.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 303 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 153 NE2
REMARK 620 2 HIS A 251 ND1 47.8
REMARK 620 3 FMT A 306 O2 45.5 3.3
REMARK 620 4 FMT A 306 O1 47.9 3.9 2.9
REMARK 620 5 FMT A 307 O1 45.0 2.8 2.9 5.3
REMARK 620 6 FMT A 307 O2 47.2 2.6 5.1 6.5 2.9
REMARK 620 7 FMT A 308 O2 45.5 3.0 0.3 3.0 2.7 4.8
REMARK 620 8 FMT A 308 O1 47.6 4.1 2.6 0.4 5.3 6.6 2.8
REMARK 620 9 FMT A 309 O1 45.1 2.8 3.3 5.6 0.4 2.6 3.0 5.5
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 304 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 153 NE2
REMARK 620 2 HIS A 251 ND1 49.6
REMARK 620 3 FMT A 306 O1 80.3 70.4
REMARK 620 4 FMT A 306 O2 122.3 78.2 57.7
REMARK 620 5 FMT A 307 O2 100.8 100.2 166.9 112.3
REMARK 620 6 FMT A 307 O1 134.5 93.3 114.9 57.3 55.3
REMARK 620 7 FMT A 308 O1 86.7 73.8 6.5 52.3 164.0 109.6
REMARK 620 8 FMT A 308 O2 124.0 78.0 62.5 5.1 107.3 52.4 57.2
REMARK 620 9 FMT A 309 O1 133.4 96.7 122.3 64.7 48.2 7.5 116.9 59.8
REMARK 620 N 1 2 3 4 5 6 7 8
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 114 NE2
REMARK 620 2 HIS B 116 ND1 97.8
REMARK 620 3 HIS B 179 NE2 103.9 107.4
REMARK 620 4 9NK B 305 S01 127.9 119.2 98.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 118 OD2
REMARK 620 2 CYS B 198 SG 111.6
REMARK 620 3 HIS B 240 NE2 96.1 105.7
REMARK 620 4 9NK B 305 S01 110.7 115.3 115.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 303 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 153 NE2
REMARK 620 2 HIS B 251 ND1 45.3
REMARK 620 3 FMT B 306 O1 91.1 99.0
REMARK 620 4 FMT B 306 O2 134.8 100.0 62.9
REMARK 620 5 FMT B 307 O1 84.4 75.0 174.0 118.0
REMARK 620 6 FMT B 307 O2 138.9 101.0 121.5 59.7 61.0
REMARK 620 7 FMT B 308 O1 74.6 62.4 161.3 119.4 12.7 67.5
REMARK 620 8 FMT B 308 O2 125.5 90.6 132.8 69.9 48.9 13.6 54.3
REMARK 620 9 FMT B 309 O1 97.1 91.7 17.3 48.5 159.8 108.3 150.9 117.7
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 304 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 153 NE2
REMARK 620 2 HIS B 251 ND1 44.1
REMARK 620 3 FMT B 306 O2 41.8 2.4
REMARK 620 4 FMT B 306 O1 44.4 2.2 2.9
REMARK 620 5 FMT B 307 O2 41.7 3.3 2.9 5.1
REMARK 620 6 FMT B 307 O1 44.5 3.6 5.0 5.7 3.0
REMARK 620 7 FMT B 308 O2 41.8 3.9 3.8 5.9 0.9 2.7
REMARK 620 8 FMT B 308 O1 44.8 3.4 5.0 5.5 3.2 0.4 3.0
REMARK 620 9 FMT B 309 O2 41.5 2.6 0.6 3.4 2.4 4.7 3.3 4.7
REMARK 620 N 1 2 3 4 5 6 7 8
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 ZN A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9NK A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9NK B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues FMT A 306 and FMT A
REMARK 800 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues FMT A 306 and FMT A
REMARK 800 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues FMT A 307 and FMT A
REMARK 800 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues FMT B 307 and FMT B
REMARK 800 308
DBREF1 5O7N A 27 266 UNP A0A173FE28_KLEPN
DBREF2 5O7N A A0A173FE28 9 248
DBREF1 5O7N B 27 266 UNP A0A173FE28_KLEPN
DBREF2 5O7N B A0A173FE28 9 248
SEQADV 5O7N MET A 13 UNP A0A173FE2 INITIATING METHIONINE
SEQADV 5O7N HIS A 14 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N HIS A 15 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N HIS A 16 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N HIS A 17 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N HIS A 18 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N HIS A 19 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N GLU A 20 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N ASN A 21 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N LEU A 22 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N TYR A 23 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N PHE A 24 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N GLN A 25 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N GLY A 26 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N MET B 13 UNP A0A173FE2 INITIATING METHIONINE
SEQADV 5O7N HIS B 14 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N HIS B 15 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N HIS B 16 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N HIS B 17 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N HIS B 18 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N HIS B 19 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N GLU B 20 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N ASN B 21 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N LEU B 22 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N TYR B 23 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N PHE B 24 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N GLN B 25 UNP A0A173FE2 EXPRESSION TAG
SEQADV 5O7N GLY B 26 UNP A0A173FE2 EXPRESSION TAG
SEQRES 1 A 254 MET HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN
SEQRES 2 A 254 GLY VAL ASP SER SER GLY GLU TYR PRO THR VAL SER GLU
SEQRES 3 A 254 ILE PRO VAL GLY GLU VAL ARG LEU TYR GLN ILE ALA ASP
SEQRES 4 A 254 GLY VAL TRP SER HIS ILE ALA THR GLN SER PHE ASP GLY
SEQRES 5 A 254 ALA VAL TYR PRO SER ASN GLY LEU ILE VAL ARG ASP GLY
SEQRES 6 A 254 ASP GLU LEU LEU LEU ILE ASP THR ALA TRP GLY ALA LYS
SEQRES 7 A 254 ASN THR ALA ALA LEU LEU ALA GLU ILE GLU LYS GLN ILE
SEQRES 8 A 254 GLY LEU PRO VAL THR ARG ALA VAL SER THR HIS PHE HIS
SEQRES 9 A 254 ASP ASP ARG VAL GLY GLY VAL ASP VAL LEU ARG ALA ALA
SEQRES 10 A 254 GLY VAL ALA THR TYR ALA SER PRO SER THR ARG ARG LEU
SEQRES 11 A 254 ALA GLU VAL GLU GLY ASN GLU ILE PRO THR HIS SER LEU
SEQRES 12 A 254 GLU GLY LEU SER SER SER GLY ASP ALA VAL ARG PHE GLY
SEQRES 13 A 254 PRO VAL GLU LEU PHE TYR PRO GLY ALA ALA HIS SER THR
SEQRES 14 A 254 ASP ASN LEU VAL VAL TYR VAL PRO SER ALA SER VAL LEU
SEQRES 15 A 254 TYR GLY GLY CYS ALA ILE TYR GLU LEU SER ARG THR SER
SEQRES 16 A 254 ALA GLY ASN VAL ALA ASP ALA ASP LEU ALA GLU TRP PRO
SEQRES 17 A 254 THR SER ILE GLU ARG ILE GLN GLN HIS TYR PRO GLU ALA
SEQRES 18 A 254 GLN PHE VAL ILE PRO GLY HIS GLY LEU PRO GLY GLY LEU
SEQRES 19 A 254 ASP LEU LEU LYS HIS THR THR ASN VAL VAL LYS ALA HIS
SEQRES 20 A 254 THR ASN ARG SER VAL VAL GLU
SEQRES 1 B 254 MET HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN
SEQRES 2 B 254 GLY VAL ASP SER SER GLY GLU TYR PRO THR VAL SER GLU
SEQRES 3 B 254 ILE PRO VAL GLY GLU VAL ARG LEU TYR GLN ILE ALA ASP
SEQRES 4 B 254 GLY VAL TRP SER HIS ILE ALA THR GLN SER PHE ASP GLY
SEQRES 5 B 254 ALA VAL TYR PRO SER ASN GLY LEU ILE VAL ARG ASP GLY
SEQRES 6 B 254 ASP GLU LEU LEU LEU ILE ASP THR ALA TRP GLY ALA LYS
SEQRES 7 B 254 ASN THR ALA ALA LEU LEU ALA GLU ILE GLU LYS GLN ILE
SEQRES 8 B 254 GLY LEU PRO VAL THR ARG ALA VAL SER THR HIS PHE HIS
SEQRES 9 B 254 ASP ASP ARG VAL GLY GLY VAL ASP VAL LEU ARG ALA ALA
SEQRES 10 B 254 GLY VAL ALA THR TYR ALA SER PRO SER THR ARG ARG LEU
SEQRES 11 B 254 ALA GLU VAL GLU GLY ASN GLU ILE PRO THR HIS SER LEU
SEQRES 12 B 254 GLU GLY LEU SER SER SER GLY ASP ALA VAL ARG PHE GLY
SEQRES 13 B 254 PRO VAL GLU LEU PHE TYR PRO GLY ALA ALA HIS SER THR
SEQRES 14 B 254 ASP ASN LEU VAL VAL TYR VAL PRO SER ALA SER VAL LEU
SEQRES 15 B 254 TYR GLY GLY CYS ALA ILE TYR GLU LEU SER ARG THR SER
SEQRES 16 B 254 ALA GLY ASN VAL ALA ASP ALA ASP LEU ALA GLU TRP PRO
SEQRES 17 B 254 THR SER ILE GLU ARG ILE GLN GLN HIS TYR PRO GLU ALA
SEQRES 18 B 254 GLN PHE VAL ILE PRO GLY HIS GLY LEU PRO GLY GLY LEU
SEQRES 19 B 254 ASP LEU LEU LYS HIS THR THR ASN VAL VAL LYS ALA HIS
SEQRES 20 B 254 THR ASN ARG SER VAL VAL GLU
HET ZN A 301 1
HET ZN A 302 1
HET ZN A 303 1
HET ZN A 304 1
HET 9NK A 305 21
HET FMT A 306 3
HET FMT A 307 3
HET FMT A 308 3
HET FMT A 309 3
HET EDO A 310 4
HET ZN B 301 1
HET ZN B 302 1
HET ZN B 303 1
HET ZN B 304 1
HET 9NK B 305 21
HET FMT B 306 3
HET FMT B 307 3
HET FMT B 308 3
HET FMT B 309 3
HET EDO B 310 4
HETNAM ZN ZINC ION
HETNAM 9NK (2~{R})-1-[(2~{S})-2-(PHENYLMETHYL)-3-SULFANYL-
HETNAM 2 9NK PROPANOYL]PIPERIDINE-2-CARBOXYLIC ACID
HETNAM FMT FORMIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 ZN 8(ZN 2+)
FORMUL 7 9NK 2(C16 H21 N O3 S)
FORMUL 8 FMT 8(C H2 O2)
FORMUL 12 EDO 2(C2 H6 O2)
FORMUL 23 HOH *338(H2 O)
HELIX 1 AA1 GLY A 88 ILE A 103 1 16
HELIX 2 AA2 HIS A 116 GLY A 121 1 6
HELIX 3 AA3 GLY A 122 ALA A 129 1 8
HELIX 4 AA4 SER A 136 GLY A 147 1 12
HELIX 5 AA5 CYS A 198 ILE A 200 5 3
HELIX 6 AA6 GLU A 218 TYR A 230 1 13
HELIX 7 AA7 LEU A 246 ASN A 261 1 16
HELIX 8 AA8 GLY B 88 ILE B 103 1 16
HELIX 9 AA9 HIS B 116 GLY B 121 1 6
HELIX 10 AB1 GLY B 122 ALA B 129 1 8
HELIX 11 AB2 SER B 136 GLY B 147 1 12
HELIX 12 AB3 CYS B 198 ILE B 200 5 3
HELIX 13 AB4 GLU B 218 TYR B 230 1 13
HELIX 14 AB5 LEU B 246 ASN B 261 1 16
SHEET 1 AA1 7 VAL A 44 ALA A 50 0
SHEET 2 AA1 7 VAL A 53 PHE A 62 -1 O ILE A 57 N ARG A 45
SHEET 3 AA1 7 ALA A 65 ASP A 76 -1 O TYR A 67 N GLN A 60
SHEET 4 AA1 7 GLU A 79 ILE A 83 -1 O ILE A 83 N LEU A 72
SHEET 5 AA1 7 VAL A 107 VAL A 111 1 O ARG A 109 N LEU A 82
SHEET 6 AA1 7 ALA A 132 ALA A 135 1 O ALA A 132 N ALA A 110
SHEET 7 AA1 7 HIS A 153 SER A 154 1 O HIS A 153 N THR A 133
SHEET 1 AA2 5 ALA A 164 PHE A 167 0
SHEET 2 AA2 5 VAL A 170 PHE A 173 -1 O LEU A 172 N VAL A 165
SHEET 3 AA2 5 VAL A 185 VAL A 188 -1 O VAL A 185 N PHE A 173
SHEET 4 AA2 5 VAL A 193 GLY A 197 -1 O TYR A 195 N VAL A 186
SHEET 5 AA2 5 PHE A 235 PRO A 238 1 O PHE A 235 N LEU A 194
SHEET 1 AA3 7 VAL B 44 ALA B 50 0
SHEET 2 AA3 7 VAL B 53 PHE B 62 -1 O ILE B 57 N ARG B 45
SHEET 3 AA3 7 ALA B 65 ASP B 76 -1 O TYR B 67 N GLN B 60
SHEET 4 AA3 7 GLU B 79 ILE B 83 -1 O ILE B 83 N LEU B 72
SHEET 5 AA3 7 VAL B 107 VAL B 111 1 O ARG B 109 N LEU B 82
SHEET 6 AA3 7 ALA B 132 ALA B 135 1 O ALA B 132 N THR B 108
SHEET 7 AA3 7 HIS B 153 SER B 154 1 O HIS B 153 N THR B 133
SHEET 1 AA4 5 ASP B 163 PHE B 167 0
SHEET 2 AA4 5 VAL B 170 TYR B 174 -1 O LEU B 172 N VAL B 165
SHEET 3 AA4 5 VAL B 185 VAL B 188 -1 O TYR B 187 N GLU B 171
SHEET 4 AA4 5 VAL B 193 GLY B 197 -1 O TYR B 195 N VAL B 186
SHEET 5 AA4 5 PHE B 235 PRO B 238 1 O PHE B 235 N LEU B 194
LINK C FMT A 306 O2 FMT A 308 1555 4747 1.45
LINK O1 FMT A 306 C FMT A 308 1555 4747 1.48
LINK C FMT A 307 O2 FMT A 309 1555 4747 1.34
LINK C FMT B 307 O1 FMT B 308 1555 4748 1.43
LINK NE2 HIS A 114 ZN ZN A 301 1555 1555 2.04
LINK ND1 HIS A 116 ZN ZN A 301 1555 1555 1.80
LINK OD2 ASP A 118 ZN ZN A 302 1555 1555 2.03
LINK NE2 HIS A 153 ZN ZN A 303 1555 4757 2.00
LINK NE2 HIS A 153 ZN ZN A 304 1555 1555 1.93
LINK NE2 HIS A 179 ZN ZN A 301 1555 1555 2.00
LINK SG ACYS A 198 ZN ZN A 302 1555 1555 2.06
LINK NE2 HIS A 240 ZN ZN A 302 1555 1555 2.08
LINK ND1 HIS A 251 ZN ZN A 303 1555 1555 2.04
LINK ND1 HIS A 251 ZN ZN A 304 1555 4747 2.10
LINK ZN ZN A 301 S01 9NK A 305 1555 1555 2.38
LINK ZN ZN A 302 S01 9NK A 305 1555 1555 2.78
LINK ZN ZN A 303 O2 FMT A 306 1555 1555 2.18
LINK ZN ZN A 303 O1 FMT A 306 1555 1555 2.49
LINK ZN ZN A 303 O1 FMT A 307 1555 1555 2.29
LINK ZN ZN A 303 O2 FMT A 307 1555 1555 2.25
LINK ZN ZN A 303 O2 FMT A 308 1555 4747 2.07
LINK ZN ZN A 303 O1 FMT A 308 1555 4747 2.57
LINK ZN ZN A 303 O1 FMT A 309 1555 4747 2.28
LINK ZN ZN A 303 O2 FMT A 309 1555 4747 2.66
LINK ZN ZN A 304 O1 FMT A 306 1555 4757 2.37
LINK ZN ZN A 304 O2 FMT A 306 1555 4757 2.13
LINK ZN ZN A 304 O2 FMT A 307 1555 4757 2.36
LINK ZN ZN A 304 O1 FMT A 307 1555 4757 2.34
LINK ZN ZN A 304 O1 FMT A 308 1555 1555 2.46
LINK ZN ZN A 304 O2 FMT A 308 1555 1555 2.02
LINK ZN ZN A 304 O1 FMT A 309 1555 1555 2.35
LINK NE2 HIS B 114 ZN ZN B 301 1555 1555 2.04
LINK ND1 HIS B 116 ZN ZN B 301 1555 1555 1.82
LINK OD2 ASP B 118 ZN ZN B 302 1555 1555 2.01
LINK NE2 HIS B 153 ZN ZN B 303 1555 1555 1.94
LINK NE2 HIS B 153 ZN ZN B 304 1555 4748 2.04
LINK NE2 HIS B 179 ZN ZN B 301 1555 1555 2.03
LINK SG ACYS B 198 ZN ZN B 302 1555 1555 2.28
LINK NE2 HIS B 240 ZN ZN B 302 1555 1555 2.13
LINK ND1 HIS B 251 ZN ZN B 303 1555 4758 2.06
LINK ND1 HIS B 251 ZN ZN B 304 1555 1555 1.99
LINK ZN ZN B 301 S01 9NK B 305 1555 1555 2.32
LINK ZN ZN B 302 S01 9NK B 305 1555 1555 2.33
LINK ZN ZN B 303 O1 FMT B 306 1555 1555 2.04
LINK ZN ZN B 303 O2 FMT B 306 1555 1555 2.14
LINK ZN ZN B 303 O1 FMT B 307 1555 1555 2.10
LINK ZN ZN B 303 O2 FMT B 307 1555 1555 2.20
LINK ZN ZN B 303 O1 FMT B 308 1555 4748 2.04
LINK ZN ZN B 303 O2 FMT B 308 1555 4748 2.61
LINK ZN ZN B 303 O1 FMT B 309 1555 4748 2.16
LINK ZN ZN B 303 O2 FMT B 309 1555 4748 2.22
LINK ZN ZN B 304 O2 FMT B 306 1555 4758 2.03
LINK ZN ZN B 304 O1 FMT B 306 1555 4758 1.91
LINK ZN ZN B 304 O2 FMT B 307 1555 4758 2.20
LINK ZN ZN B 304 O1 FMT B 307 1555 4758 2.23
LINK ZN ZN B 304 O2 FMT B 308 1555 1555 2.65
LINK ZN ZN B 304 O1 FMT B 308 1555 1555 2.18
LINK ZN ZN B 304 O2 FMT B 309 1555 1555 2.13
LINK ZN ZN B 304 O1 FMT B 309 1555 1555 2.03
SITE 1 AC1 4 HIS A 114 HIS A 116 HIS A 179 9NK A 305
SITE 1 AC2 5 ASP A 118 ARG A 119 CYS A 198 HIS A 240
SITE 2 AC2 5 9NK A 305
SITE 1 AC3 6 HIS A 153 HIS A 251 FMT A 306 FMT A 307
SITE 2 AC3 6 FMT A 308 FMT A 309
SITE 1 AC4 6 HIS A 153 HIS A 251 FMT A 306 FMT A 307
SITE 2 AC4 6 FMT A 308 FMT A 309
SITE 1 AC5 12 TRP A 87 HIS A 116 ASP A 118 HIS A 179
SITE 2 AC5 12 CYS A 198 ARG A 205 GLY A 209 ASN A 210
SITE 3 AC5 12 HIS A 240 ZN A 301 ZN A 302 HOH A 436
SITE 1 AC6 5 ASP A 76 LEU A 80 THR A 108 ARG A 109
SITE 2 AC6 5 PRO A 169
SITE 1 AC7 4 HIS B 114 HIS B 116 HIS B 179 9NK B 305
SITE 1 AC8 4 ASP B 118 CYS B 198 HIS B 240 9NK B 305
SITE 1 AC9 3 HIS B 153 FMT B 306 FMT B 307
SITE 1 AD1 3 HIS B 251 FMT B 308 FMT B 309
SITE 1 AD2 13 TYR B 67 HIS B 116 ASP B 118 HIS B 179
SITE 2 AD2 13 CYS B 198 GLY B 209 ASN B 210 HIS B 240
SITE 3 AD2 13 ZN B 301 ZN B 302 HOH B 423 HOH B 428
SITE 4 AD2 13 HOH B 429
SITE 1 AD3 4 ALA B 132 HIS B 153 ZN B 303 FMT B 307
SITE 1 AD4 5 THR B 206 HIS B 251 ASN B 254 ZN B 304
SITE 2 AD4 5 FMT B 308
SITE 1 AD5 6 ASP A 63 GLY A 64 TYR B 67 GLU B 202
SITE 2 AD5 6 ARG B 205 HOH B 455
SITE 1 AD6 9 ALA A 132 THR A 152 HIS A 153 HIS A 251
SITE 2 AD6 9 ASN A 254 ZN A 303 ZN A 304 FMT A 307
SITE 3 AD6 9 FMT A 309
SITE 1 AD7 9 ALA A 132 THR A 152 HIS A 153 HIS A 251
SITE 2 AD7 9 ASN A 254 ZN A 303 ZN A 304 FMT A 307
SITE 3 AD7 9 FMT A 309
SITE 1 AD8 10 ALA A 132 HIS A 153 THR A 206 HIS A 251
SITE 2 AD8 10 ASN A 254 ZN A 303 ZN A 304 FMT A 306
SITE 3 AD8 10 FMT A 308 HOH A 405
SITE 1 AD9 8 THR B 152 HIS B 153 HIS B 251 ASN B 254
SITE 2 AD9 8 ZN B 303 ZN B 304 FMT B 306 FMT B 309
CRYST1 101.989 79.308 67.645 90.00 130.45 90.00 C 1 2 1 8
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 0.009805 0.000000 0.008359 0.00000
SCALE2 0.000000 0.012609 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019427 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
