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HEADER HYDROLASE 23-JUN-20 7CEF
TITLE CRYSTAL STRUCTURE OF PET-DEGRADING CUTINASE CUT190 /S226P/R228S/
TITLE 2 MUTANT WITH THE C-TERMINAL THREE RESIDUES DELETION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FAMILY PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CUTINASE;
COMPND 5 EC: 3.1.1.74;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMONOSPORA VIRIDIS;
SOURCE 3 ORGANISM_TAXID: 1852;
SOURCE 4 GENE: CUT190, SAMN02982918_2340;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN ENGINEERING, THERMOSTABILITY, POLYESTERASE, MULTIPLE
KEYWDS 2 CONFORMATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SENGA,N.NUMOTO,N.ITO,F.KAWAI,M.ODA
REVDAT 1 26-AUG-20 7CEF 0
JRNL AUTH A.SENGA,N.NUMOTO,M.YAMASHITA,A.IIDA,N.ITO,F.KAWAI,M.ODA
JRNL TITL MULTIPLE STRUCTURAL STATES OF CA2+ REGULATED PET HYDROLASE,
JRNL TITL 2 CUT190, AND ITS CORRELATION WITH ACTIVITY AND STABILITY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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 : GEOSTD + MONOMER LIBRARY
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 60336
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3017
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 41.7200 - 4.4800 0.97 2701 139 0.1719 0.1913
REMARK 3 2 4.4800 - 3.5600 0.98 2648 146 0.1381 0.1686
REMARK 3 3 3.5600 - 3.1100 0.99 2656 138 0.1559 0.1839
REMARK 3 4 3.1100 - 2.8200 0.98 2640 144 0.1707 0.2350
REMARK 3 5 2.8200 - 2.6200 0.99 2611 135 0.1735 0.1958
REMARK 3 6 2.6200 - 2.4700 0.98 2643 131 0.1654 0.1958
REMARK 3 7 2.4700 - 2.3400 0.99 2594 145 0.1642 0.2533
REMARK 3 8 2.3400 - 2.2400 0.99 2636 132 0.1684 0.2304
REMARK 3 9 2.2400 - 2.1500 0.99 2646 136 0.1688 0.2070
REMARK 3 10 2.1500 - 2.0800 0.99 2611 151 0.1763 0.2291
REMARK 3 11 2.0800 - 2.0100 0.98 2626 124 0.1761 0.2404
REMARK 3 12 2.0100 - 1.9600 0.98 2591 131 0.1823 0.2312
REMARK 3 13 1.9600 - 1.9100 0.98 2601 144 0.1910 0.2299
REMARK 3 14 1.9100 - 1.8600 0.97 2539 129 0.1945 0.2932
REMARK 3 15 1.8600 - 1.8200 0.97 2580 138 0.2148 0.2750
REMARK 3 16 1.8200 - 1.7800 0.97 2575 146 0.2243 0.2778
REMARK 3 17 1.7800 - 1.7400 0.97 2582 133 0.2304 0.3139
REMARK 3 18 1.7400 - 1.7100 0.97 2609 128 0.2446 0.2967
REMARK 3 19 1.7100 - 1.6800 0.97 2543 137 0.2521 0.2700
REMARK 3 20 1.6800 - 1.6500 0.97 2596 120 0.2622 0.3323
REMARK 3 21 1.6500 - 1.6200 0.97 2557 140 0.2601 0.2893
REMARK 3 22 1.6200 - 1.6000 0.97 2534 150 0.2723 0.2901
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) : 0.196
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.457
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.55
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.99
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 : 0.008 4180
REMARK 3 ANGLE : 0.928 5698
REMARK 3 CHIRALITY : 0.058 610
REMARK 3 PLANARITY : 0.007 758
REMARK 3 DIHEDRAL : 10.431 2502
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 7CEF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUL-20.
REMARK 100 THE DEPOSITION ID IS D_1300017429.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUN-19
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1000
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 : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60359
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08300
REMARK 200 FOR THE DATA SET : 9.3000
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) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.68400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4WFI, 4WFJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M ZINC ACETATE, 0.1M SODIUM
REMARK 280 CACODYLATE, 18% PEG 8000, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 24.55000
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 TOTAL BURIED SURFACE AREA: 770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -198.0 KCAL/MOL
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 TOTAL BURIED SURFACE AREA: 610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -180.0 KCAL/MOL
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: 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 OD2 ASP B 204 O HOH B 501 1.76
REMARK 500 O HOH B 501 O HOH B 549 2.11
REMARK 500 O THR A 206 O HOH A 501 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 611 O HOH B 698 2656 2.16
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 ASN A 47 113.18 -164.74
REMARK 500 THR A 107 -8.88 68.10
REMARK 500 SER A 176 -118.59 60.10
REMARK 500 THR A 199 61.75 28.13
REMARK 500 HIS A 230 -82.68 -117.27
REMARK 500 ASN B 47 110.00 -161.35
REMARK 500 ALA B 78 149.80 -170.72
REMARK 500 ASP B 158 153.25 -48.06
REMARK 500 SER B 176 -122.84 64.52
REMARK 500 THR B 199 61.74 28.27
REMARK 500 HIS B 230 -82.95 -120.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 802 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH B 904 DISTANCE = 6.47 ANGSTROMS
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 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 43 N
REMARK 620 2 GLY A 43 O 78.4
REMARK 620 3 ASP A 46 OD1 138.1 88.4
REMARK 620 4 ASP A 46 OD2 74.1 75.1 64.0
REMARK 620 5 GLU A 50 OE1 88.6 76.0 126.7 148.7
REMARK 620 6 GLU A 50 OE2 143.8 106.1 78.1 142.1 59.1
REMARK 620 7 HOH A 637 O 93.2 162.7 88.0 88.2 119.2 89.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 76 O
REMARK 620 2 ALA A 78 O 100.4
REMARK 620 3 PHE A 81 O 91.9 78.0
REMARK 620 4 HOH A 517 O 91.7 149.3 73.5
REMARK 620 5 HOH A 672 O 158.6 100.8 89.4 68.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 406 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD2
REMARK 620 2 HOH A 551 O 80.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 408 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 118 OE1
REMARK 620 2 GLU A 118 OE2 64.3
REMARK 620 3 HOH A 523 O 74.6 138.5
REMARK 620 4 GLU B 278 OE1 135.4 91.4 123.5
REMARK 620 5 GLU B 278 OE2 81.4 93.4 85.6 62.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 407 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 184 OE2
REMARK 620 2 HOH A 519 O 107.8
REMARK 620 3 HOH A 577 O 86.5 72.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 404 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 204 OD2
REMARK 620 2 GLU A 278 OE1 115.0
REMARK 620 3 GLU A 278 OE2 115.8 4.3
REMARK 620 4 HOH A 501 O 104.3 50.1 54.3
REMARK 620 5 HOH A 507 O 77.8 160.6 156.8 144.1
REMARK 620 6 HOH A 661 O 104.5 57.4 53.2 107.5 106.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 403 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 220 OE1
REMARK 620 2 ASP A 250 OD1 100.1
REMARK 620 3 GLU A 296 OE1 82.7 88.0
REMARK 620 4 GLU B 220 OE2 118.3 21.1 100.6
REMARK 620 5 HOH B 504 O 159.1 100.3 93.4 82.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 405 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 248 OE2
REMARK 620 2 HOH A 535 O 109.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 404 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 250 OD2
REMARK 620 2 HOH A 615 O 64.6
REMARK 620 3 GLU B 296 OE1 64.5 3.0
REMARK 620 4 GLU B 296 OE2 64.8 0.5 2.6
REMARK 620 5 HOH B 504 O 66.9 3.7 2.4 3.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 403 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 296 OE2
REMARK 620 2 HOH A 558 O 94.4
REMARK 620 3 HOH A 611 O 92.3 2.2
REMARK 620 4 ASP B 250 OD1 91.7 3.0 0.9
REMARK 620 5 HOH B 504 O 92.1 2.9 2.3 3.1
REMARK 620 6 HOH B 698 O 90.6 3.9 2.1 2.3 1.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 410 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 297 OE2
REMARK 620 2 GLU B 91 OE2 58.7
REMARK 620 3 HOH B 694 O 60.8 2.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 405 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 611 O
REMARK 620 2 ASP B 250 OD2 97.9
REMARK 620 3 HOH B 634 O 87.6 174.0
REMARK 620 4 HOH B 697 O 162.9 89.3 84.7
REMARK 620 5 HOH B 698 O 63.6 88.0 92.5 101.4
REMARK 620 6 HOH B 707 O 101.9 91.5 89.5 93.3 165.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 407 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 611 O
REMARK 620 2 HOH A 718 O 102.9
REMARK 620 3 HOH B 796 O 109.9 110.7
REMARK 620 4 HOH B 817 O 105.2 124.7 103.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 406 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 615 O
REMARK 620 2 HOH B 698 O 110.0
REMARK 620 3 HOH B 777 O 111.7 107.7
REMARK 620 4 HOH B 783 O 107.2 111.2 109.1
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 GLY B 43 N
REMARK 620 2 GLY B 43 O 80.7
REMARK 620 3 ASP B 46 OD1 153.7 86.5
REMARK 620 4 ASP B 46 OD2 88.3 75.5 66.2
REMARK 620 5 GLU B 50 OE1 68.5 75.1 130.0 144.9
REMARK 620 6 GLU B 50 OE2 121.2 108.4 84.7 150.5 59.4
REMARK 620 7 HOH B 625 O 84.1 164.1 105.5 99.4 103.6 83.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 408 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 163 OE1
REMARK 620 2 HOH B 811 O 114.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 409 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 163 OE2
REMARK 620 2 HOH B 811 O 124.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 204 OD1
REMARK 620 2 ASP B 204 OD2 57.6
REMARK 620 3 THR B 206 O 90.6 119.8
REMARK 620 4 THR B 206 OG1 78.5 130.8 77.9
REMARK 620 5 HOH B 501 O 104.0 47.6 134.8 146.5
REMARK 620 6 HOH B 549 O 113.0 73.8 75.6 151.1 59.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 410
DBREF 7CEF A 45 304 UNP W0TJ64 W0TJ64_9PSEU 45 304
DBREF 7CEF B 45 304 UNP W0TJ64 W0TJ64_9PSEU 45 304
SEQADV 7CEF GLY A 43 UNP W0TJ64 EXPRESSION TAG
SEQADV 7CEF PRO A 44 UNP W0TJ64 EXPRESSION TAG
SEQADV 7CEF PRO A 226 UNP W0TJ64 SER 226 ENGINEERED MUTATION
SEQADV 7CEF SER A 228 UNP W0TJ64 ARG 228 ENGINEERED MUTATION
SEQADV 7CEF GLY B 43 UNP W0TJ64 EXPRESSION TAG
SEQADV 7CEF PRO B 44 UNP W0TJ64 EXPRESSION TAG
SEQADV 7CEF PRO B 226 UNP W0TJ64 SER 226 ENGINEERED MUTATION
SEQADV 7CEF SER B 228 UNP W0TJ64 ARG 228 ENGINEERED MUTATION
SEQRES 1 A 262 GLY PRO GLN ASP ASN PRO TYR GLU ARG GLY PRO ASP PRO
SEQRES 2 A 262 THR GLU ASP SER ILE GLU ALA ILE ARG GLY PRO PHE SER
SEQRES 3 A 262 VAL ALA THR GLU ARG VAL SER SER PHE ALA SER GLY PHE
SEQRES 4 A 262 GLY GLY GLY THR ILE TYR TYR PRO ARG GLU THR ASP GLU
SEQRES 5 A 262 GLY THR PHE GLY ALA VAL ALA VAL ALA PRO GLY PHE THR
SEQRES 6 A 262 ALA SER GLN GLY SER MET SER TRP TYR GLY GLU ARG VAL
SEQRES 7 A 262 ALA SER GLN GLY PHE ILE VAL PHE THR ILE ASP THR ASN
SEQRES 8 A 262 THR ARG LEU ASP GLN PRO GLY GLN ARG GLY ARG GLN LEU
SEQRES 9 A 262 LEU ALA ALA LEU ASP TYR LEU VAL GLU ARG SER ASP ARG
SEQRES 10 A 262 LYS VAL ARG GLU ARG LEU ASP PRO ASN ARG LEU ALA VAL
SEQRES 11 A 262 MET GLY HIS SER MET GLY GLY GLY GLY SER LEU GLU ALA
SEQRES 12 A 262 THR VAL MET ARG PRO SER LEU LYS ALA SER ILE PRO LEU
SEQRES 13 A 262 THR PRO TRP ASN LEU ASP LYS THR TRP GLY GLN VAL GLN
SEQRES 14 A 262 VAL PRO THR PHE ILE ILE GLY ALA GLU LEU ASP THR ILE
SEQRES 15 A 262 ALA PRO VAL SER THR HIS ALA LYS PRO PHE TYR GLU SER
SEQRES 16 A 262 LEU PRO SER SER LEU PRO LYS ALA TYR MET GLU LEU ASP
SEQRES 17 A 262 GLY ALA THR HIS PHE ALA PRO ASN ILE PRO ASN THR THR
SEQRES 18 A 262 ILE ALA LYS TYR VAL ILE SER TRP LEU LYS ARG PHE VAL
SEQRES 19 A 262 ASP GLU ASP THR ARG TYR SER GLN PHE LEU CYS PRO ASN
SEQRES 20 A 262 PRO THR ASP ARG ALA ILE GLU GLU TYR ARG SER THR CYS
SEQRES 21 A 262 PRO TYR
SEQRES 1 B 262 GLY PRO GLN ASP ASN PRO TYR GLU ARG GLY PRO ASP PRO
SEQRES 2 B 262 THR GLU ASP SER ILE GLU ALA ILE ARG GLY PRO PHE SER
SEQRES 3 B 262 VAL ALA THR GLU ARG VAL SER SER PHE ALA SER GLY PHE
SEQRES 4 B 262 GLY GLY GLY THR ILE TYR TYR PRO ARG GLU THR ASP GLU
SEQRES 5 B 262 GLY THR PHE GLY ALA VAL ALA VAL ALA PRO GLY PHE THR
SEQRES 6 B 262 ALA SER GLN GLY SER MET SER TRP TYR GLY GLU ARG VAL
SEQRES 7 B 262 ALA SER GLN GLY PHE ILE VAL PHE THR ILE ASP THR ASN
SEQRES 8 B 262 THR ARG LEU ASP GLN PRO GLY GLN ARG GLY ARG GLN LEU
SEQRES 9 B 262 LEU ALA ALA LEU ASP TYR LEU VAL GLU ARG SER ASP ARG
SEQRES 10 B 262 LYS VAL ARG GLU ARG LEU ASP PRO ASN ARG LEU ALA VAL
SEQRES 11 B 262 MET GLY HIS SER MET GLY GLY GLY GLY SER LEU GLU ALA
SEQRES 12 B 262 THR VAL MET ARG PRO SER LEU LYS ALA SER ILE PRO LEU
SEQRES 13 B 262 THR PRO TRP ASN LEU ASP LYS THR TRP GLY GLN VAL GLN
SEQRES 14 B 262 VAL PRO THR PHE ILE ILE GLY ALA GLU LEU ASP THR ILE
SEQRES 15 B 262 ALA PRO VAL SER THR HIS ALA LYS PRO PHE TYR GLU SER
SEQRES 16 B 262 LEU PRO SER SER LEU PRO LYS ALA TYR MET GLU LEU ASP
SEQRES 17 B 262 GLY ALA THR HIS PHE ALA PRO ASN ILE PRO ASN THR THR
SEQRES 18 B 262 ILE ALA LYS TYR VAL ILE SER TRP LEU LYS ARG PHE VAL
SEQRES 19 B 262 ASP GLU ASP THR ARG TYR SER GLN PHE LEU CYS PRO ASN
SEQRES 20 B 262 PRO THR ASP ARG ALA ILE GLU GLU TYR ARG SER THR CYS
SEQRES 21 B 262 PRO TYR
HET CA A 401 1
HET ZN A 402 1
HET ZN A 403 1
HET ZN A 404 1
HET ZN A 405 1
HET ZN A 406 1
HET ZN A 407 1
HET ZN A 408 1
HET ZN B 401 1
HET ZN B 402 1
HET ZN B 403 1
HET ZN B 404 1
HET ZN B 405 1
HET ZN B 406 1
HET ZN B 407 1
HET ZN B 408 1
HET ZN B 409 1
HET ZN B 410 1
HETNAM CA CALCIUM ION
HETNAM ZN ZINC ION
FORMUL 3 CA CA 2+
FORMUL 4 ZN 17(ZN 2+)
FORMUL 21 HOH *706(H2 O)
HELIX 1 AA1 GLY A 43 ASN A 47 5 5
HELIX 2 AA2 THR A 56 ALA A 62 1 7
HELIX 3 AA3 SER A 109 SER A 114 5 6
HELIX 4 AA4 TRP A 115 SER A 122 1 8
HELIX 5 AA5 GLN A 138 ARG A 156 1 19
HELIX 6 AA6 ASP A 158 GLU A 163 1 6
HELIX 7 AA7 SER A 176 ARG A 189 1 14
HELIX 8 AA8 HIS A 230 LEU A 238 1 9
HELIX 9 AA9 PHE A 255 ILE A 259 5 5
HELIX 10 AB1 ASN A 261 ASP A 277 1 17
HELIX 11 AB2 ASP A 279 ARG A 281 5 3
HELIX 12 AB3 TYR A 282 CYS A 287 1 6
HELIX 13 AB4 THR B 56 ALA B 62 1 7
HELIX 14 AB5 ALA B 108 SER B 112 5 5
HELIX 15 AB6 MET B 113 SER B 114 5 2
HELIX 16 AB7 TRP B 115 SER B 122 1 8
HELIX 17 AB8 GLN B 138 ARG B 156 1 19
HELIX 18 AB9 ASP B 158 GLU B 163 1 6
HELIX 19 AC1 SER B 176 ARG B 189 1 14
HELIX 20 AC2 HIS B 230 LEU B 238 1 9
HELIX 21 AC3 PHE B 255 ILE B 259 5 5
HELIX 22 AC4 ASN B 261 ASP B 277 1 17
HELIX 23 AC5 ASP B 279 ARG B 281 5 3
HELIX 24 AC6 TYR B 282 CYS B 287 1 6
SHEET 1 AA1 6 VAL A 69 VAL A 74 0
SHEET 2 AA1 6 GLY A 84 PRO A 89 -1 O ILE A 86 N GLU A 72
SHEET 3 AA1 6 ILE A 126 ILE A 130 -1 O VAL A 127 N TYR A 87
SHEET 4 AA1 6 PHE A 97 ALA A 103 1 N GLY A 98 O ILE A 126
SHEET 5 AA1 6 LEU A 165 HIS A 175 1 O ASP A 166 N PHE A 97
SHEET 6 AA1 6 ALA A 194 LEU A 198 1 O LEU A 198 N GLY A 174
SHEET 1 AA2 3 THR A 214 ALA A 219 0
SHEET 2 AA2 3 LYS A 244 LEU A 249 1 O LEU A 249 N GLY A 218
SHEET 3 AA2 3 ILE A 295 SER A 300 -1 O GLU A 297 N GLU A 248
SHEET 1 AA3 6 VAL B 69 ALA B 78 0
SHEET 2 AA3 6 GLY B 82 PRO B 89 -1 O ILE B 86 N GLU B 72
SHEET 3 AA3 6 ILE B 126 ILE B 130 -1 O VAL B 127 N TYR B 87
SHEET 4 AA3 6 PHE B 97 ALA B 103 1 N VAL B 102 O PHE B 128
SHEET 5 AA3 6 LEU B 165 HIS B 175 1 O ASP B 166 N PHE B 97
SHEET 6 AA3 6 ALA B 194 LEU B 198 1 O LEU B 198 N GLY B 174
SHEET 1 AA4 3 THR B 214 ALA B 219 0
SHEET 2 AA4 3 LYS B 244 LEU B 249 1 O MET B 247 N GLY B 218
SHEET 3 AA4 3 ILE B 295 SER B 300 -1 O GLU B 297 N GLU B 248
SSBOND 1 CYS A 287 CYS A 302 1555 1555 2.04
SSBOND 2 CYS B 287 CYS B 302 1555 1555 2.03
LINK N GLY A 43 ZN ZN A 402 1555 1555 2.17
LINK O GLY A 43 ZN ZN A 402 1555 1555 2.16
LINK OD1 ASP A 46 ZN ZN A 402 1555 1555 2.02
LINK OD2 ASP A 46 ZN ZN A 402 1555 1555 2.09
LINK OE1 GLU A 50 ZN ZN A 402 1555 1555 2.29
LINK OE2 GLU A 50 ZN ZN A 402 1555 1555 2.05
LINK O SER A 76 CA CA A 401 1555 1555 2.45
LINK O ALA A 78 CA CA A 401 1555 1555 2.37
LINK O PHE A 81 CA CA A 401 1555 1555 2.37
LINK OD2 ASP A 93 ZN ZN A 406 1555 1555 2.03
LINK OE1 GLU A 118 ZN ZN A 408 1555 1555 2.08
LINK OE2 GLU A 118 ZN ZN A 408 1555 1555 2.05
LINK OE2 GLU A 184 ZN ZN A 407 1555 1555 2.04
LINK OD2 ASP A 204 ZN ZN A 404 1555 1555 1.98
LINK OE1 GLU A 220 ZN ZN A 403 1555 1555 2.06
LINK OE2 GLU A 248 ZN ZN A 405 1555 1555 2.12
LINK OD1 ASP A 250 ZN ZN A 403 1555 1555 2.02
LINK OD2 ASP A 250 ZN ZN B 404 1555 2656 2.00
LINK OE1 GLU A 278 ZN ZN A 404 1555 2545 2.06
LINK OE2 GLU A 278 ZN ZN A 404 1555 2545 2.25
LINK OE1 GLU A 296 ZN ZN A 403 1555 1555 2.04
LINK OE2 GLU A 296 ZN ZN B 403 1555 2656 2.05
LINK OE2 GLU A 297 ZN ZN B 410 1555 1455 2.04
LINK CA CA A 401 O HOH A 517 1555 1555 2.42
LINK CA CA A 401 O HOH A 672 1555 1555 2.39
LINK ZN ZN A 402 O HOH A 637 1555 1555 2.11
LINK ZN ZN A 403 OE2 GLU B 220 2646 1555 2.00
LINK ZN ZN A 403 O HOH B 504 1555 2656 2.08
LINK ZN ZN A 404 O HOH A 501 1555 1555 1.94
LINK ZN ZN A 404 O HOH A 507 1555 2555 2.00
LINK ZN ZN A 404 O HOH A 661 1555 2555 2.17
LINK ZN ZN A 405 O HOH A 535 1555 1555 2.17
LINK ZN ZN A 406 O HOH A 551 1555 1555 2.07
LINK ZN ZN A 407 O HOH A 519 1555 1555 2.12
LINK ZN ZN A 407 O HOH A 577 1555 1555 2.10
LINK ZN ZN A 408 O HOH A 523 1555 1555 2.10
LINK ZN ZN A 408 OE1 GLU B 278 1555 1555 2.17
LINK ZN ZN A 408 OE2 GLU B 278 1555 1555 2.04
LINK O HOH A 558 ZN ZN B 403 2646 1555 2.02
LINK O HOH A 611 ZN ZN B 403 2646 1555 1.99
LINK O HOH A 611 ZN ZN B 405 2646 1555 1.99
LINK O HOH A 611 ZN ZN B 407 2646 1555 1.89
LINK O HOH A 615 ZN ZN B 404 2646 1555 1.97
LINK O HOH A 615 ZN ZN B 406 2646 1555 1.96
LINK O HOH A 718 ZN ZN B 407 2646 1555 2.09
LINK N GLY B 43 ZN ZN B 401 1555 1555 2.09
LINK O GLY B 43 ZN ZN B 401 1555 1555 2.37
LINK OD1 ASP B 46 ZN ZN B 401 1555 1555 1.97
LINK OD2 ASP B 46 ZN ZN B 401 1555 1555 2.03
LINK OE1 GLU B 50 ZN ZN B 401 1555 1555 2.30
LINK OE2 GLU B 50 ZN ZN B 401 1555 1555 2.00
LINK OE2 GLU B 91 ZN ZN B 410 1555 1555 2.00
LINK OE1 GLU B 163 ZN ZN B 408 1555 1555 2.04
LINK OE2 GLU B 163 ZN ZN B 409 1555 1555 2.02
LINK OD1 ASP B 204 ZN ZN B 402 1555 1555 2.15
LINK OD2 ASP B 204 ZN ZN B 402 1555 1555 2.27
LINK O THR B 206 ZN ZN B 402 1555 1555 2.10
LINK OG1 THR B 206 ZN ZN B 402 1555 1555 2.25
LINK OD1 ASP B 250 ZN ZN B 403 1555 1555 2.12
LINK OD2 ASP B 250 ZN ZN B 405 1555 1555 2.07
LINK OE1 GLU B 296 ZN ZN B 404 1555 1555 2.43
LINK OE2 GLU B 296 ZN ZN B 404 1555 1555 2.00
LINK ZN ZN B 401 O HOH B 625 1555 1555 2.14
LINK ZN ZN B 402 O HOH B 501 1555 1555 2.07
LINK ZN ZN B 402 O HOH B 549 1555 1555 2.19
LINK ZN ZN B 403 O HOH B 504 1555 1555 2.04
LINK ZN ZN B 403 O HOH B 698 1555 1555 1.90
LINK ZN ZN B 404 O HOH B 504 1555 1555 1.99
LINK ZN ZN B 405 O HOH B 634 1555 2746 2.13
LINK ZN ZN B 405 O HOH B 697 1555 1555 2.05
LINK ZN ZN B 405 O HOH B 698 1555 1555 2.10
LINK ZN ZN B 405 O HOH B 707 1555 2746 2.13
LINK ZN ZN B 406 O HOH B 698 1555 1555 1.94
LINK ZN ZN B 406 O HOH B 777 1555 1555 2.07
LINK ZN ZN B 406 O HOH B 783 1555 2746 2.09
LINK ZN ZN B 407 O HOH B 796 1555 2746 2.05
LINK ZN ZN B 407 O HOH B 817 1555 1555 2.08
LINK ZN ZN B 408 O HOH B 811 1555 1555 2.58
LINK ZN ZN B 409 O HOH B 811 1555 1555 2.13
LINK ZN ZN B 410 O HOH B 694 1555 1555 2.19
CISPEP 1 CYS A 287 PRO A 288 0 0.77
CISPEP 2 CYS A 302 PRO A 303 0 5.00
CISPEP 3 CYS B 287 PRO B 288 0 -2.28
CISPEP 4 CYS B 302 PRO B 303 0 5.60
SITE 1 AC1 5 SER A 76 ALA A 78 PHE A 81 HOH A 517
SITE 2 AC1 5 HOH A 672
SITE 1 AC2 4 GLY A 43 ASP A 46 GLU A 50 HOH A 637
SITE 1 AC3 4 GLU A 220 ASP A 250 GLU A 296 HOH A 558
SITE 1 AC4 2 ASP A 204 HOH A 501
SITE 1 AC5 5 LYS A 232 GLU A 248 GLU A 297 HOH A 535
SITE 2 AC5 5 ARG B 90
SITE 1 AC6 2 ASP A 93 HOH A 551
SITE 1 AC7 4 GLY A 140 GLU A 184 HOH A 519 HOH A 577
SITE 1 AC8 3 GLU A 118 HOH A 523 GLU B 278
SITE 1 AC9 4 GLY B 43 ASP B 46 GLU B 50 HOH B 625
SITE 1 AD1 4 ASP B 204 THR B 206 HOH B 501 HOH B 549
SITE 1 AD2 7 ASP B 250 ZN B 404 ZN B 405 ZN B 406
SITE 2 AD2 7 ZN B 407 HOH B 504 HOH B 698
SITE 1 AD3 4 GLU B 296 ZN B 403 ZN B 406 HOH B 504
SITE 1 AD4 6 ASP B 250 ZN B 403 ZN B 406 ZN B 407
SITE 2 AD4 6 HOH B 697 HOH B 698
SITE 1 AD5 5 ZN B 403 ZN B 404 ZN B 405 HOH B 698
SITE 2 AD5 5 HOH B 777
SITE 1 AD6 3 ZN B 403 ZN B 405 HOH B 817
SITE 1 AD7 3 GLU B 163 ZN B 409 HOH B 811
SITE 1 AD8 3 GLU B 163 ZN B 408 HOH B 811
SITE 1 AD9 5 LYS A 232 GLU A 297 SER B 68 GLU B 91
SITE 2 AD9 5 HOH B 694
CRYST1 60.512 49.100 82.948 90.00 107.45 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 0.016526 0.000000 0.005196 0.00000
SCALE2 0.000000 0.020367 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012638 0.00000
TER 2035 TYR A 304
TER 4070 TYR B 304
MASTER 538 0 18 24 18 0 24 6 4792 2 83 42
END |