| content |
HEADER HYDROLASE 25-APR-18 5ZRQ
TITLE CRYSTAL STRUCTURE OF PET-DEGRADING CUTINASE CUT190 S176A/S226P/R228S
TITLE 2 MUTANT IN ZN(2+)-BOUND STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FAMILY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CUTINASE;
COMPND 5 ENGINEERED: YES;
COMPND 6 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;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PQE80L
KEYWDS POLYESTERASE, ALPHA/BETA-HYDROLASE FOLD, PROTEIN ENGINEERING,
KEYWDS 2 THERMOSTABILITY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.NUMOTO,N.KAMIYA,G.J.BEKKER,Y.YAMAGAMI,S.INABA,K.ISHII,S.UCHIYAMA,
AUTHOR 2 F.KAWAI,N.ITO,M.ODA
REVDAT 1 12-SEP-18 5ZRQ 0
JRNL AUTH N.NUMOTO,N.KAMIYA,G.J.BEKKER,Y.YAMAGAMI,S.INABA,K.ISHII,
JRNL AUTH 2 S.UCHIYAMA,F.KAWAI,N.ITO,M.ODA
JRNL TITL STRUCTURAL DYNAMICS OF THE PET-DEGRADING CUTINASE-LIKE
JRNL TITL 2 ENZYME FROM SACCHAROMONOSPORA VIRIDIS AHK190 IN
JRNL TITL 3 SUBSTRATE-BOUND STATES ELUCIDATES THE CA2+-DRIVEN CATALYTIC
JRNL TITL 4 CYCLE.
JRNL REF BIOCHEMISTRY 2018
JRNL REFN ISSN 1520-4995
JRNL PMID 30110540
JRNL DOI 10.1021/ACS.BIOCHEM.8B00624
REMARK 2
REMARK 2 RESOLUTION. 1.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 1.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.32
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 93488
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.122
REMARK 3 R VALUE (WORKING SET) : 0.121
REMARK 3 FREE R VALUE : 0.142
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.015
REMARK 3 FREE R VALUE TEST SET COUNT : 4688
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 42.3472 - 3.4644 0.99 3318 173 0.1379 0.1500
REMARK 3 2 3.4644 - 2.7499 1.00 3195 171 0.1397 0.1771
REMARK 3 3 2.7499 - 2.4024 1.00 3175 162 0.1375 0.1507
REMARK 3 4 2.4024 - 2.1827 1.00 3133 168 0.1268 0.1434
REMARK 3 5 2.1827 - 2.0263 1.00 3149 165 0.1190 0.1347
REMARK 3 6 2.0263 - 1.9068 1.00 3125 166 0.1143 0.1138
REMARK 3 7 1.9068 - 1.8113 1.00 3131 161 0.1127 0.1211
REMARK 3 8 1.8113 - 1.7325 1.00 3088 171 0.1090 0.1272
REMARK 3 9 1.7325 - 1.6658 1.00 3115 159 0.1048 0.1378
REMARK 3 10 1.6658 - 1.6083 1.00 3125 162 0.0985 0.1339
REMARK 3 11 1.6083 - 1.5580 1.00 3087 167 0.0984 0.1193
REMARK 3 12 1.5580 - 1.5135 1.00 3083 160 0.0954 0.1072
REMARK 3 13 1.5135 - 1.4736 1.00 3105 160 0.0946 0.1146
REMARK 3 14 1.4736 - 1.4377 1.00 3068 163 0.0972 0.1192
REMARK 3 15 1.4377 - 1.4050 1.00 3097 166 0.1013 0.1338
REMARK 3 16 1.4050 - 1.3751 1.00 3079 162 0.1011 0.1365
REMARK 3 17 1.3751 - 1.3476 1.00 3096 160 0.1057 0.1422
REMARK 3 18 1.3476 - 1.3221 1.00 3088 161 0.1056 0.1321
REMARK 3 19 1.3221 - 1.2985 1.00 3086 167 0.1082 0.1459
REMARK 3 20 1.2985 - 1.2765 1.00 3071 161 0.1071 0.1363
REMARK 3 21 1.2765 - 1.2559 1.00 3086 161 0.1143 0.1303
REMARK 3 22 1.2559 - 1.2366 1.00 3067 162 0.1160 0.1606
REMARK 3 23 1.2366 - 1.2184 0.98 3001 155 0.1268 0.1540
REMARK 3 24 1.2184 - 1.2012 0.95 2896 155 0.1300 0.1569
REMARK 3 25 1.2012 - 1.1850 0.91 2782 154 0.1267 0.1365
REMARK 3 26 1.1850 - 1.1696 0.87 2643 139 0.1299 0.1392
REMARK 3 27 1.1696 - 1.1550 0.81 2494 134 0.1348 0.1912
REMARK 3 28 1.1550 - 1.1411 0.76 2308 129 0.1454 0.1517
REMARK 3 29 1.1411 - 1.1278 0.71 2183 114 0.1512 0.1710
REMARK 3 30 1.1278 - 1.1151 0.63 1926 100 0.1635 0.2211
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) : 0.066
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 11.130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 7.56
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.16
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 2154
REMARK 3 ANGLE : 1.280 2939
REMARK 3 CHIRALITY : 0.085 313
REMARK 3 PLANARITY : 0.008 389
REMARK 3 DIHEDRAL : 12.057 805
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 5ZRQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1300007538.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-OCT-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8000
REMARK 200 MONOCHROMATOR : FIXED EXIT SI (111) DOUBLE
REMARK 200 CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93489
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.120
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 (%) : 95.3
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05700
REMARK 200 FOR THE DATA SET : 18.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.28200
REMARK 200 FOR SHELL : 4.100
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: 4WFJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01 M ZNSO4, 0.1 M MES PH 6.5, 25%
REMARK 280 V/V PEG MME 550, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 25.09800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.33750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.62150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.33750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.09800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.62150
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 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 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 LEU A 306
REMARK 465 ASN A 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 O HOH A 705 O HOH A 793 2.08
REMARK 500 O HOH A 716 O HOH A 850 2.15
REMARK 500 O HOH A 525 O HOH A 842 2.15
REMARK 500 O HOH A 743 O HOH A 790 2.15
REMARK 500 O HOH A 777 O HOH A 859 2.18
REMARK 500 O HOH A 610 O HOH A 766 2.19
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 503 O HOH A 819 2455 2.14
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 47 109.32 -163.80
REMARK 500 THR A 107 -2.17 71.72
REMARK 500 ALA A 176 -122.16 67.43
REMARK 500 THR A 199 57.79 33.11
REMARK 500 HIS A 230 -88.50 -116.06
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 928 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A 929 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH A 930 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH A 931 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH A 932 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH A 933 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH A 934 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH A 935 DISTANCE = 6.49 ANGSTROMS
REMARK 525 HOH A 936 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH A 937 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH A 938 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH A 939 DISTANCE = 6.90 ANGSTROMS
REMARK 525 HOH A 940 DISTANCE = 7.54 ANGSTROMS
REMARK 525 HOH A 941 DISTANCE = 8.02 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 403 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 43 N
REMARK 620 2 GLY A 43 O 79.7
REMARK 620 3 ASP A 46 OD1 134.2 86.9
REMARK 620 4 GLU A 50 OE2 128.1 97.3 96.8
REMARK 620 5 HOH A 725 O 90.6 169.1 96.7 92.5
REMARK 620 N 1 2 3 4
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 GLU A 57 OE1
REMARK 620 2 HOH A 700 O 98.6
REMARK 620 3 HOH A 551 O 87.7 89.5
REMARK 620 4 HOH A 634 O 90.9 87.7 176.6
REMARK 620 5 GLU A 155 OE1 44.2 54.5 90.2 86.6
REMARK 620 6 GLU A 155 OE2 46.1 52.6 90.3 86.5 1.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 406 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 76 O
REMARK 620 2 ALA A 78 O 99.3
REMARK 620 3 PHE A 81 O 103.3 83.8
REMARK 620 4 HOH A 641 O 91.1 165.7 84.2
REMARK 620 5 HOH A 650 O 168.3 91.5 82.5 79.2
REMARK 620 6 HOH A 781 O 94.4 87.3 161.3 101.9 81.3
REMARK 620 N 1 2 3 4 5
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 ASP A 204 OD1
REMARK 620 2 ASP A 204 OD2 51.4
REMARK 620 3 THR A 206 O 84.3 114.1
REMARK 620 4 THR A 206 OG1 77.6 124.5 75.3
REMARK 620 5 HOH A 702 O 83.1 80.4 147.2 72.5
REMARK 620 6 HOH A 783 O 130.3 81.4 135.7 131.6 73.3
REMARK 620 7 HOH A 708 O 151.2 156.8 75.1 77.9 103.5 77.9
REMARK 620 8 HOH A 624 O 104.8 75.7 72.0 146.7 140.7 72.5 87.9
REMARK 620 N 1 2 3 4 5 6 7
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 GLU A 220 OE1
REMARK 620 2 GLU A 220 OE2 54.4
REMARK 620 3 ASP A 250 OD1 100.0 154.4
REMARK 620 4 GLU A 296 OE1 105.4 86.4 101.3
REMARK 620 5 GLU A 118 OE2 62.9 108.7 50.1 80.0
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 HOH A 503 O
REMARK 620 2 HOH A 582 O 77.4
REMARK 620 3 HOH A 754 O 79.1 80.8
REMARK 620 4 HOH A 908 O 166.7 94.1 89.4
REMARK 620 5 HOH A 809 O 102.9 177.9 101.3 85.9
REMARK 620 6 HOH A 819 O 66.1 101.2 143.5 126.3 77.2
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 ZN 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 CA A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 410
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5ZNO RELATED DB: PDB
REMARK 900 5ZNO CONTAINS THE SAME PROTEIN COMPLEXED WITH CA(2+)
REMARK 900 RELATED ID: 5ZRR RELATED DB: PDB
REMARK 900 RELATED ID: 5ZRS RELATED DB: PDB
DBREF 5ZRQ A 45 304 UNP W0TJ64 W0TJ64_9PSEU 45 304
SEQADV 5ZRQ GLY A 43 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZRQ PRO A 44 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZRQ ALA A 176 UNP W0TJ64 SER 176 ENGINEERED MUTATION
SEQADV 5ZRQ PRO A 226 UNP W0TJ64 SER 226 ENGINEERED MUTATION
SEQADV 5ZRQ SER A 228 UNP W0TJ64 ARG 228 ENGINEERED MUTATION
SEQADV 5ZRQ LYS A 305 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZRQ LEU A 306 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZRQ ASN A 307 UNP W0TJ64 EXPRESSION TAG
SEQRES 1 A 265 GLY PRO GLN ASP ASN PRO TYR GLU ARG GLY PRO ASP PRO
SEQRES 2 A 265 THR GLU ASP SER ILE GLU ALA ILE ARG GLY PRO PHE SER
SEQRES 3 A 265 VAL ALA THR GLU ARG VAL SER SER PHE ALA SER GLY PHE
SEQRES 4 A 265 GLY GLY GLY THR ILE TYR TYR PRO ARG GLU THR ASP GLU
SEQRES 5 A 265 GLY THR PHE GLY ALA VAL ALA VAL ALA PRO GLY PHE THR
SEQRES 6 A 265 ALA SER GLN GLY SER MET SER TRP TYR GLY GLU ARG VAL
SEQRES 7 A 265 ALA SER GLN GLY PHE ILE VAL PHE THR ILE ASP THR ASN
SEQRES 8 A 265 THR ARG LEU ASP GLN PRO GLY GLN ARG GLY ARG GLN LEU
SEQRES 9 A 265 LEU ALA ALA LEU ASP TYR LEU VAL GLU ARG SER ASP ARG
SEQRES 10 A 265 LYS VAL ARG GLU ARG LEU ASP PRO ASN ARG LEU ALA VAL
SEQRES 11 A 265 MET GLY HIS ALA MET GLY GLY GLY GLY SER LEU GLU ALA
SEQRES 12 A 265 THR VAL MHO ARG PRO SER LEU LYS ALA SER ILE PRO LEU
SEQRES 13 A 265 THR PRO TRP ASN LEU ASP LYS THR TRP GLY GLN VAL GLN
SEQRES 14 A 265 VAL PRO THR PHE ILE ILE GLY ALA GLU LEU ASP THR ILE
SEQRES 15 A 265 ALA PRO VAL SER THR HIS ALA LYS PRO PHE TYR GLU SER
SEQRES 16 A 265 LEU PRO SER SER LEU PRO LYS ALA TYR MET GLU LEU ASP
SEQRES 17 A 265 GLY ALA THR HIS PHE ALA PRO ASN ILE PRO ASN THR THR
SEQRES 18 A 265 ILE ALA LYS TYR VAL ILE SER TRP LEU LYS ARG PHE VAL
SEQRES 19 A 265 ASP GLU ASP THR ARG TYR SER GLN PHE LEU CYS PRO ASN
SEQRES 20 A 265 PRO THR ASP ARG ALA ILE GLU GLU TYR ARG SER THR CYS
SEQRES 21 A 265 PRO TYR LYS LEU ASN
MODRES 5ZRQ MHO A 188 MET MODIFIED RESIDUE
HET MHO A 188 9
HET ZN A 401 1
HET ZN A 402 1
HET ZN A 403 1
HET ZN A 404 1
HET ZN A 405 1
HET CA A 406 1
HET SO4 A 407 5
HET GOL A 408 6
HET GOL A 409 6
HET GOL A 410 6
HETNAM MHO S-OXYMETHIONINE
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MHO C5 H11 N O3 S
FORMUL 2 ZN 5(ZN 2+)
FORMUL 7 CA CA 2+
FORMUL 8 SO4 O4 S 2-
FORMUL 9 GOL 3(C3 H8 O3)
FORMUL 12 HOH *441(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 112 5 4
HELIX 4 AA4 MET A 113 SER A 122 1 10
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 ALA 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
SHEET 1 AA1 6 VAL A 69 VAL A 74 0
SHEET 2 AA1 6 GLY A 84 PRO A 89 -1 O GLY A 84 N VAL A 74
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 VAL A 102 O PHE A 128
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
SSBOND 1 CYS A 287 CYS A 302 1555 1555 2.04
LINK N GLY A 43 ZN ZN A 403 1555 1555 2.04
LINK O GLY A 43 ZN ZN A 403 1555 1555 2.22
LINK OD1 ASP A 46 ZN ZN A 403 1555 1555 1.92
LINK OE2 GLU A 50 ZN ZN A 403 1555 1555 1.96
LINK OE1AGLU A 57 ZN ZN A 404 1555 1555 1.94
LINK O SER A 76 CA CA A 406 1555 1555 2.31
LINK O ALA A 78 CA CA A 406 1555 1555 2.31
LINK O PHE A 81 CA CA A 406 1555 1555 2.33
LINK C VAL A 187 N MHO A 188 1555 1555 1.32
LINK C MHO A 188 N ARG A 189 1555 1555 1.33
LINK OD1 ASP A 204 ZN ZN A 402 1555 1555 2.39
LINK OD2 ASP A 204 ZN ZN A 402 1555 1555 2.62
LINK O THR A 206 ZN ZN A 402 1555 1555 2.35
LINK OG1 THR A 206 ZN ZN A 402 1555 1555 2.44
LINK OE1 GLU A 220 ZN ZN A 401 1555 1555 1.97
LINK OE2 GLU A 220 ZN ZN A 401 1555 1555 2.64
LINK OD1 ASP A 250 ZN ZN A 401 1555 1555 1.98
LINK OE1 GLU A 296 ZN ZN A 401 1555 1555 1.96
LINK ZN ZN A 402 O HOH A 702 1555 1555 2.47
LINK ZN ZN A 402 O HOH A 783 1555 1555 2.49
LINK ZN ZN A 402 O HOH A 708 1555 1555 2.42
LINK ZN ZN A 402 O HOH A 624 1555 1555 2.38
LINK ZN ZN A 403 O HOH A 725 1555 1555 2.12
LINK ZN ZN A 404 O HOH A 700 1555 1555 1.97
LINK ZN ZN A 404 O HOH A 551 1555 1555 2.13
LINK ZN ZN A 404 O HOH A 634 1555 1555 2.13
LINK ZN ZN A 405 O HOH A 503 1555 1555 1.99
LINK ZN ZN A 405 O HOH A 582 1555 1555 2.19
LINK ZN ZN A 405 O HOH A 754 1555 1555 2.33
LINK ZN ZN A 405 O HOH A 908 1555 1555 2.30
LINK CA CA A 406 O HOH A 641 1555 1555 2.42
LINK CA CA A 406 O HOH A 650 1555 1555 2.58
LINK CA CA A 406 O HOH A 781 1555 1555 2.48
LINK OE2 GLU A 118 ZN ZN A 401 1555 3455 1.90
LINK OE1 GLU A 155 ZN ZN A 404 1555 2454 2.06
LINK OE2 GLU A 155 ZN ZN A 404 1555 2454 2.17
LINK ZN ZN A 405 O HOH A 809 1555 2455 2.12
LINK ZN ZN A 405 O HOH A 819 1555 2455 1.93
CISPEP 1 CYS A 287 PRO A 288 0 -3.35
CISPEP 2 CYS A 302 PRO A 303 0 -1.14
SITE 1 AC1 4 GLU A 118 GLU A 220 ASP A 250 GLU A 296
SITE 1 AC2 6 ASP A 204 THR A 206 HOH A 624 HOH A 702
SITE 2 AC2 6 HOH A 708 HOH A 783
SITE 1 AC3 4 GLY A 43 ASP A 46 GLU A 50 HOH A 725
SITE 1 AC4 5 GLU A 57 GLU A 155 HOH A 551 HOH A 634
SITE 2 AC4 5 HOH A 700
SITE 1 AC5 6 HOH A 503 HOH A 582 HOH A 754 HOH A 809
SITE 2 AC5 6 HOH A 819 HOH A 908
SITE 1 AC6 6 SER A 76 ALA A 78 PHE A 81 HOH A 641
SITE 2 AC6 6 HOH A 650 HOH A 781
SITE 1 AC7 8 GLU A 155 ASP A 292 ARG A 293 HOH A 535
SITE 2 AC7 8 HOH A 551 HOH A 652 HOH A 754 HOH A 809
SITE 1 AC8 7 GLN A 138 GLY A 140 GLN A 141 ARG A 144
SITE 2 AC8 7 SER A 241 HOH A 684 HOH A 843
SITE 1 AC9 6 GLY A 52 PHE A 67 GLU A 91 ASP A 93
SITE 2 AC9 6 GLU A 94 HOH A 538
SITE 1 AD1 9 SER A 59 PRO A 66 HOH A 506 HOH A 510
SITE 2 AD1 9 HOH A 669 HOH A 763 HOH A 799 HOH A 855
SITE 3 AD1 9 HOH A 939
CRYST1 50.196 63.243 78.675 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 0.019922 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015812 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012711 0.00000
TER 2073 LYS A 305
MASTER 425 0 11 12 9 0 19 6 2512 1 76 21
END |