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HEADER HYDROLASE 10-APR-18 5ZNO
TITLE CRYSTAL STRUCTURE OF PET-DEGRADING CUTINASE CUT190 S176A/S226P/R228S/
TITLE 2 MUTANT IN CA(2+)-BOUND STATE
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 STRAIN: AHK190;
SOURCE 5 GENE: CUT190, SAMN02982918_2340;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA-GAMI B (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE80L
KEYWDS POLYESTERASE, ALPHA/BETA-HYDROLASE FOLD, PROTEIN ENGINEERING,
KEYWDS 2 THERMOSTABILITY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.NUMOTO,S.INABA,Y.YAMAGAMI,N.KAMIYA,G.J.BEKKER,K.ISHII,S.UCHIYAMA,
AUTHOR 2 F.KAWAI,N.ITO,M.ODA
REVDAT 1 12-SEP-18 5ZNO 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. 1.60 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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.347
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 75047
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.994
REMARK 3 FREE R VALUE TEST SET COUNT : 3748
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 47.7390 - 4.8064 0.98 2737 144 0.1486 0.1753
REMARK 3 2 4.8064 - 3.8155 0.98 2673 141 0.1260 0.1649
REMARK 3 3 3.8155 - 3.3333 0.99 2644 138 0.1364 0.1721
REMARK 3 4 3.3333 - 3.0286 0.99 2656 139 0.1534 0.1987
REMARK 3 5 3.0286 - 2.8115 0.99 2661 141 0.1569 0.1870
REMARK 3 6 2.8115 - 2.6458 0.99 2663 139 0.1599 0.2133
REMARK 3 7 2.6458 - 2.5133 1.00 2657 140 0.1593 0.1843
REMARK 3 8 2.5133 - 2.4039 0.99 2640 139 0.1648 0.1987
REMARK 3 9 2.4039 - 2.3114 0.99 2633 139 0.1613 0.2275
REMARK 3 10 2.3114 - 2.2316 0.99 2622 136 0.1749 0.2301
REMARK 3 11 2.2316 - 2.1618 0.99 2651 138 0.1812 0.1992
REMARK 3 12 2.1618 - 2.1000 0.99 2660 140 0.1856 0.2528
REMARK 3 13 2.1000 - 2.0447 0.99 2645 137 0.1884 0.2363
REMARK 3 14 2.0447 - 1.9948 1.00 2594 138 0.2007 0.2508
REMARK 3 15 1.9948 - 1.9495 0.99 2653 140 0.2112 0.2686
REMARK 3 16 1.9495 - 1.9080 0.99 2613 137 0.2148 0.2614
REMARK 3 17 1.9080 - 1.8698 1.00 2648 139 0.2091 0.2795
REMARK 3 18 1.8698 - 1.8346 1.00 2618 138 0.2221 0.2723
REMARK 3 19 1.8346 - 1.8018 0.99 2642 140 0.2252 0.2866
REMARK 3 20 1.8018 - 1.7712 0.99 2605 138 0.2381 0.2815
REMARK 3 21 1.7712 - 1.7427 0.99 2631 139 0.2551 0.2849
REMARK 3 22 1.7427 - 1.7159 1.00 2623 137 0.2715 0.3175
REMARK 3 23 1.7159 - 1.6906 0.99 2655 139 0.2800 0.3571
REMARK 3 24 1.6906 - 1.6668 1.00 2601 137 0.3213 0.3482
REMARK 3 25 1.6668 - 1.6443 0.99 2637 140 0.3303 0.3305
REMARK 3 26 1.6443 - 1.6229 1.00 2637 139 0.3177 0.3790
REMARK 3 27 1.6229 - 1.6026 0.98 2600 136 0.3187 0.3257
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) : 0.236
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.943
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.92
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 4199
REMARK 3 ANGLE : 1.062 5710
REMARK 3 CHIRALITY : 0.045 612
REMARK 3 PLANARITY : 0.006 753
REMARK 3 DIHEDRAL : 12.180 1551
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 5ZNO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-APR-18.
REMARK 100 THE DEPOSITION ID IS D_1300007412.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-16
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 7.5
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 : CRYO-COOLED CHANNEL-CUT SI(111)
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 : 75063
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 (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.13600
REMARK 200 FOR THE DATA SET : 6.8000
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 (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.95000
REMARK 200 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
REMARK 200 STARTING MODEL: 4WFJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 10% W/V PEG 8000,
REMARK 280 8% V/V ETHYLENE GLYCOL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 61.85250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.86600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 61.85250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.86600
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: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 43
REMARK 465 PRO A 44
REMARK 465 GLN A 45
REMARK 465 LEU A 306
REMARK 465 ASN A 307
REMARK 465 GLY B 43
REMARK 465 PRO B 44
REMARK 465 GLN B 45
REMARK 465 ASN B 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 901 O HOH A 902 2.13
REMARK 500 O HOH A 505 O HOH A 781 2.13
REMARK 500 O HOH A 530 O HOH A 849 2.17
REMARK 500 O HOH A 548 O HOH A 782 2.18
REMARK 500 O HOH A 726 O HOH A 798 2.18
REMARK 500 O HOH B 553 O HOH B 737 2.18
REMARK 500 O HOH B 802 O HOH B 826 2.18
REMARK 500 O HOH A 758 O HOH A 823 2.18
REMARK 500 O HOH B 738 O HOH B 802 2.19
REMARK 500 O HOH A 911 O HOH A 915 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 810 O HOH B 553 1545 2.14
REMARK 500 O HOH B 784 O HOH B 837 4446 2.19
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 THR A 107 -7.34 76.80
REMARK 500 ALA A 176 -121.80 64.94
REMARK 500 THR A 199 59.58 29.86
REMARK 500 HIS A 230 -79.96 -123.89
REMARK 500 ALA B 176 -117.71 63.58
REMARK 500 THR B 199 62.29 26.11
REMARK 500 ALA B 225 71.88 -119.31
REMARK 500 HIS B 230 -88.83 -109.79
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 918 DISTANCE = 6.99 ANGSTROMS
REMARK 525 HOH B 870 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH B 871 DISTANCE = 6.82 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 CA A 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 76 O
REMARK 620 2 ALA A 78 O 97.6
REMARK 620 3 PHE A 81 O 107.0 84.7
REMARK 620 4 HOH A 657 O 160.8 96.2 87.6
REMARK 620 5 HOH A 627 O 91.0 166.2 82.4 78.3
REMARK 620 6 HOH A 786 O 88.4 97.2 164.1 76.6 93.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 204 OD1
REMARK 620 2 ASP A 204 OD2 51.7
REMARK 620 3 THR A 206 O 83.2 106.9
REMARK 620 4 THR A 206 OG1 74.9 125.8 70.9
REMARK 620 5 HOH A 676 O 113.1 77.9 71.7 140.4
REMARK 620 6 HOH A 728 O 150.6 157.7 81.6 76.3 85.7
REMARK 620 7 HOH A 754 O 79.5 84.7 146.0 76.4 142.2 99.8
REMARK 620 8 HOH A 793 O 128.6 86.4 143.8 128.3 78.7 75.6 66.8
REMARK 620 N 1 2 3 4 5 6 7
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 GLU A 220 OE1
REMARK 620 2 GLU A 220 OE2 52.8
REMARK 620 3 ASP A 250 OD1 75.4 127.3
REMARK 620 4 GLU A 296 OE1 92.0 81.9 92.5
REMARK 620 5 HOH A 757 O 156.8 150.2 81.4 89.9
REMARK 620 6 HOH A 783 O 87.3 95.1 90.6 176.6 92.0
REMARK 620 7 HOH A 572 O 128.1 76.4 156.3 90.0 75.0 87.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 76 O
REMARK 620 2 ALA B 78 O 96.1
REMARK 620 3 PHE B 81 O 84.0 79.5
REMARK 620 4 HOH B 766 O 153.3 107.7 111.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 204 OD1
REMARK 620 2 ASP B 204 OD2 50.4
REMARK 620 3 THR B 206 O 81.9 110.0
REMARK 620 4 THR B 206 OG1 77.0 124.6 72.8
REMARK 620 5 HOH B 639 O 106.1 76.9 71.2 142.9
REMARK 620 6 HOH B 719 O 150.0 159.6 79.8 75.0 90.2
REMARK 620 7 HOH B 757 O 128.6 81.4 138.8 134.1 73.5 79.8
REMARK 620 8 HOH B 634 O 85.2 87.0 143.2 70.7 145.6 95.4 74.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 220 OE1
REMARK 620 2 GLU B 220 OE2 51.3
REMARK 620 3 ASP B 250 OD1 74.7 126.0
REMARK 620 4 GLU B 296 OE1 95.0 92.6 94.6
REMARK 620 5 HOH B 553 O 67.2 86.0 69.1 158.1
REMARK 620 6 HOH B 737 O 93.8 71.0 115.3 150.1 48.7
REMARK 620 7 HOH B 749 O 150.7 149.1 80.2 102.0 89.9 83.3
REMARK 620 8 HOH B 755 O 134.2 83.0 150.2 90.1 111.3 63.7 70.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 404 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 765 O
REMARK 620 2 HOH B 529 O 82.9
REMARK 620 3 HOH B 571 O 89.7 65.0
REMARK 620 4 HOH B 739 O 154.6 100.7 114.7
REMARK 620 5 HOH B 853 O 94.6 146.0 81.1 95.9
REMARK 620 6 HOH A 531 O 79.5 140.5 148.9 82.1 70.9
REMARK 620 7 HOH A 713 O 81.3 69.7 134.6 76.5 143.6 72.8
REMARK 620 N 1 2 3 4 5 6
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 CA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 406
DBREF 5ZNO A 45 304 UNP W0TJ64 W0TJ64_9PSEU 45 304
DBREF 5ZNO B 45 304 UNP W0TJ64 W0TJ64_9PSEU 45 304
SEQADV 5ZNO GLY A 43 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZNO PRO A 44 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZNO ALA A 176 UNP W0TJ64 SER 176 ENGINEERED MUTATION
SEQADV 5ZNO PRO A 226 UNP W0TJ64 SER 226 ENGINEERED MUTATION
SEQADV 5ZNO SER A 228 UNP W0TJ64 ARG 228 ENGINEERED MUTATION
SEQADV 5ZNO LYS A 305 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZNO LEU A 306 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZNO ASN A 307 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZNO GLY B 43 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZNO PRO B 44 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZNO ALA B 176 UNP W0TJ64 SER 176 ENGINEERED MUTATION
SEQADV 5ZNO PRO B 226 UNP W0TJ64 SER 226 ENGINEERED MUTATION
SEQADV 5ZNO SER B 228 UNP W0TJ64 ARG 228 ENGINEERED MUTATION
SEQADV 5ZNO LYS B 305 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZNO LEU B 306 UNP W0TJ64 EXPRESSION TAG
SEQADV 5ZNO ASN B 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 MET 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
SEQRES 1 B 265 GLY PRO GLN ASP ASN PRO TYR GLU ARG GLY PRO ASP PRO
SEQRES 2 B 265 THR GLU ASP SER ILE GLU ALA ILE ARG GLY PRO PHE SER
SEQRES 3 B 265 VAL ALA THR GLU ARG VAL SER SER PHE ALA SER GLY PHE
SEQRES 4 B 265 GLY GLY GLY THR ILE TYR TYR PRO ARG GLU THR ASP GLU
SEQRES 5 B 265 GLY THR PHE GLY ALA VAL ALA VAL ALA PRO GLY PHE THR
SEQRES 6 B 265 ALA SER GLN GLY SER MET SER TRP TYR GLY GLU ARG VAL
SEQRES 7 B 265 ALA SER GLN GLY PHE ILE VAL PHE THR ILE ASP THR ASN
SEQRES 8 B 265 THR ARG LEU ASP GLN PRO GLY GLN ARG GLY ARG GLN LEU
SEQRES 9 B 265 LEU ALA ALA LEU ASP TYR LEU VAL GLU ARG SER ASP ARG
SEQRES 10 B 265 LYS VAL ARG GLU ARG LEU ASP PRO ASN ARG LEU ALA VAL
SEQRES 11 B 265 MET GLY HIS ALA MET GLY GLY GLY GLY SER LEU GLU ALA
SEQRES 12 B 265 THR VAL MET ARG PRO SER LEU LYS ALA SER ILE PRO LEU
SEQRES 13 B 265 THR PRO TRP ASN LEU ASP LYS THR TRP GLY GLN VAL GLN
SEQRES 14 B 265 VAL PRO THR PHE ILE ILE GLY ALA GLU LEU ASP THR ILE
SEQRES 15 B 265 ALA PRO VAL SER THR HIS ALA LYS PRO PHE TYR GLU SER
SEQRES 16 B 265 LEU PRO SER SER LEU PRO LYS ALA TYR MET GLU LEU ASP
SEQRES 17 B 265 GLY ALA THR HIS PHE ALA PRO ASN ILE PRO ASN THR THR
SEQRES 18 B 265 ILE ALA LYS TYR VAL ILE SER TRP LEU LYS ARG PHE VAL
SEQRES 19 B 265 ASP GLU ASP THR ARG TYR SER GLN PHE LEU CYS PRO ASN
SEQRES 20 B 265 PRO THR ASP ARG ALA ILE GLU GLU TYR ARG SER THR CYS
SEQRES 21 B 265 PRO TYR LYS LEU ASN
HET CA A 401 1
HET CA A 402 1
HET CA A 403 1
HET GOL A 404 6
HET GOL A 405 6
HET GOL A 406 6
HET CA B 401 1
HET CA B 402 1
HET CA B 403 1
HET CA B 404 1
HET GOL B 405 6
HET GOL B 406 6
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 CA 7(CA 2+)
FORMUL 6 GOL 5(C3 H8 O3)
FORMUL 15 HOH *789(H2 O)
HELIX 1 AA1 THR A 56 ALA A 62 1 7
HELIX 2 AA2 SER A 109 SER A 114 5 6
HELIX 3 AA3 TRP A 115 SER A 122 1 8
HELIX 4 AA4 GLN A 138 ARG A 156 1 19
HELIX 5 AA5 ASP A 158 GLU A 163 1 6
HELIX 6 AA6 ALA A 176 ARG A 189 1 14
HELIX 7 AA7 HIS A 230 LEU A 238 1 9
HELIX 8 AA8 PHE A 255 ILE A 259 5 5
HELIX 9 AA9 ASN A 261 ASP A 277 1 17
HELIX 10 AB1 ASP A 279 ARG A 281 5 3
HELIX 11 AB2 TYR A 282 CYS A 287 1 6
HELIX 12 AB3 THR B 56 ALA B 62 1 7
HELIX 13 AB4 SER B 109 SER B 114 5 6
HELIX 14 AB5 TRP B 115 SER B 122 1 8
HELIX 15 AB6 GLN B 138 ARG B 156 1 19
HELIX 16 AB7 ASP B 158 GLU B 163 1 6
HELIX 17 AB8 ALA B 176 ARG B 189 1 14
HELIX 18 AB9 HIS B 230 LEU B 238 1 9
HELIX 19 AC1 PHE B 255 ILE B 259 5 5
HELIX 20 AC2 ASN B 261 ASP B 277 1 17
HELIX 21 AC3 ASP B 279 ARG B 281 5 3
HELIX 22 AC4 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 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
SHEET 1 AA3 6 VAL B 69 VAL B 74 0
SHEET 2 AA3 6 GLY B 84 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 LEU B 249 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 O SER A 76 CA CA A 403 1555 1555 2.41
LINK O ALA A 78 CA CA A 403 1555 1555 2.35
LINK O PHE A 81 CA CA A 403 1555 1555 2.30
LINK OD1 ASP A 204 CA CA A 402 1555 1555 2.53
LINK OD2 ASP A 204 CA CA A 402 1555 1555 2.53
LINK O THR A 206 CA CA A 402 1555 1555 2.43
LINK OG1 THR A 206 CA CA A 402 1555 1555 2.46
LINK OE1 GLU A 220 CA CA A 401 1555 1555 2.41
LINK OE2 GLU A 220 CA CA A 401 1555 1555 2.52
LINK OD1 ASP A 250 CA CA A 401 1555 1555 2.35
LINK OE1 GLU A 296 CA CA A 401 1555 1555 2.46
LINK O SER B 76 CA CA B 403 1555 1555 2.55
LINK O ALA B 78 CA CA B 403 1555 1555 2.36
LINK O PHE B 81 CA CA B 403 1555 1555 2.52
LINK OD1 ASP B 204 CA CA B 401 1555 1555 2.55
LINK OD2 ASP B 204 CA CA B 401 1555 1555 2.59
LINK O THR B 206 CA CA B 401 1555 1555 2.45
LINK OG1 THR B 206 CA CA B 401 1555 1555 2.50
LINK OE1 GLU B 220 CA CA B 402 1555 1555 2.51
LINK OE2 GLU B 220 CA CA B 402 1555 1555 2.53
LINK OD1 ASP B 250 CA CA B 402 1555 1555 2.44
LINK OE1 GLU B 296 CA CA B 402 1555 1555 2.31
LINK CA CA A 401 O HOH A 757 1555 1555 2.42
LINK CA CA A 401 O HOH A 783 1555 1555 2.38
LINK CA CA A 402 O HOH A 676 1555 1555 2.53
LINK CA CA A 402 O HOH A 728 1555 1555 2.41
LINK CA CA A 402 O HOH A 754 1555 1555 2.56
LINK CA CA A 402 O HOH A 793 1555 1555 2.46
LINK CA CA A 403 O HOH A 657 1555 1555 2.60
LINK CA CA A 403 O HOH A 627 1555 1555 2.54
LINK CA CA A 403 O HOH A 786 1555 1555 2.35
LINK CA CA B 401 O HOH B 639 1555 1555 2.45
LINK CA CA B 401 O HOH B 719 1555 1555 2.48
LINK CA CA B 401 O HOH B 757 1555 1555 2.47
LINK CA CA B 401 O HOH B 634 1555 1555 2.41
LINK CA CA B 402 O HOH B 553 1555 1555 2.29
LINK CA CA B 402 O HOH B 737 1555 1555 2.85
LINK CA CA B 402 O HOH B 749 1555 1555 2.57
LINK CA CA B 402 O HOH B 755 1555 1555 2.43
LINK CA CA B 403 O HOH B 766 1555 1555 2.69
LINK CA CA B 404 O HOH A 765 1555 1555 2.43
LINK CA CA B 404 O HOH B 529 1555 1555 2.46
LINK CA CA B 404 O HOH B 571 1555 1555 2.45
LINK CA CA B 404 O HOH B 739 1555 1555 2.46
LINK CA CA B 404 O HOH B 853 1555 1555 2.26
LINK CA CA B 404 O HOH A 531 1555 1555 2.45
LINK CA CA B 404 O HOH A 713 1555 1555 2.58
LINK CA CA A 401 O HOH A 572 1555 4445 2.32
CISPEP 1 CYS A 287 PRO A 288 0 0.44
CISPEP 2 CYS A 302 PRO A 303 0 2.19
CISPEP 3 CYS B 287 PRO B 288 0 0.25
CISPEP 4 CYS B 302 PRO B 303 0 -2.55
SITE 1 AC1 6 GLU A 220 ASP A 250 GLU A 296 HOH A 572
SITE 2 AC1 6 HOH A 757 HOH A 783
SITE 1 AC2 6 ASP A 204 THR A 206 HOH A 676 HOH A 728
SITE 2 AC2 6 HOH A 754 HOH A 793
SITE 1 AC3 6 SER A 76 ALA A 78 PHE A 81 HOH A 627
SITE 2 AC3 6 HOH A 657 HOH A 786
SITE 1 AC4 8 GLU A 236 SER A 240 LYS A 244 PHE A 255
SITE 2 AC4 8 ARG A 299 HOH A 501 HOH A 547 HOH A 600
SITE 1 AC5 7 PHE A 106 MET A 177 TRP A 201 ILE A 224
SITE 2 AC5 7 HOH A 522 HOH A 544 HOH A 622
SITE 1 AC6 6 GLN A 138 PRO A 139 GLY A 140 GLN A 141
SITE 2 AC6 6 HOH A 506 ARG B 64
SITE 1 AC7 6 ASP B 204 THR B 206 HOH B 634 HOH B 639
SITE 2 AC7 6 HOH B 719 HOH B 757
SITE 1 AC8 7 GLU B 220 ASP B 250 GLU B 296 HOH B 553
SITE 2 AC8 7 HOH B 737 HOH B 749 HOH B 755
SITE 1 AC9 4 SER B 76 ALA B 78 PHE B 81 HOH B 766
SITE 1 AD1 7 HOH A 531 HOH A 713 HOH A 765 HOH B 529
SITE 2 AD1 7 HOH B 571 HOH B 739 HOH B 853
SITE 1 AD2 8 PHE B 106 MET B 177 TRP B 201 GLY B 208
SITE 2 AD2 8 HOH B 513 HOH B 606 HOH B 675 HOH B 723
SITE 1 AD3 5 PRO B 53 PRO B 66 PHE B 67 GLU B 94
SITE 2 AD3 5 HOH B 533
CRYST1 123.705 49.732 95.655 90.00 99.59 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 0.008084 0.000000 0.001366 0.00000
SCALE2 0.000000 0.020108 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010602 0.00000
TER 2022 LYS A 305
TER 4064 LEU B 306
MASTER 452 0 12 22 18 0 23 6 4876 2 94 42
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