HEADER HYDROLASE 08-FEB-17 5N2T
TITLE THERMOLYSIN IN COMPLEX WITH INHIBITOR JC287
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOLYSIN;
COMPND 3 CHAIN: E;
COMPND 4 SYNONYM: THERMOSTABLE NEUTRAL PROTEINASE;
COMPND 5 EC: 3.4.24.27
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS THERMOPROTEOLYTICUS;
SOURCE 3 ORGANISM_TAXID: 1427
KEYWDS INHIBITOR, PHOSPHONAMIDATE, PROTEASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.CRAMER,S.G.KRIMMER,A.HEINE,G.KLEBE
REVDAT 3 17-JAN-24 5N2T 1 LINK
REVDAT 2 26-JUL-17 5N2T 1
REVDAT 1 21-JUN-17 5N2T 0
JRNL AUTH J.CRAMER,S.G.KRIMMER,A.HEINE,G.KLEBE
JRNL TITL PAYING THE PRICE OF DESOLVATION IN SOLVENT-EXPOSED PROTEIN
JRNL TITL 2 POCKETS: IMPACT OF DISTAL SOLUBILIZING GROUPS ON AFFINITY
JRNL TITL 3 AND BINDING THERMODYNAMICS IN A SERIES OF THERMOLYSIN
JRNL TITL 4 INHIBITORS.
JRNL REF J. MED. CHEM. V. 60 5791 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 28590130
JRNL DOI 10.1021/ACS.JMEDCHEM.7B00490
REMARK 2
REMARK 2 RESOLUTION. 1.38 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.38
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.52
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 69136
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.114
REMARK 3 R VALUE (WORKING SET) : 0.112
REMARK 3 FREE R VALUE : 0.138
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3457
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 46.5500 - 4.0321 1.00 2895 153 0.1383 0.1554
REMARK 3 2 4.0321 - 3.2006 1.00 2729 144 0.1312 0.1406
REMARK 3 3 3.2006 - 2.7961 1.00 2705 142 0.1206 0.1393
REMARK 3 4 2.7961 - 2.5405 1.00 2674 141 0.1113 0.1447
REMARK 3 5 2.5405 - 2.3584 1.00 2653 139 0.1071 0.1427
REMARK 3 6 2.3584 - 2.2193 1.00 2636 139 0.1052 0.1158
REMARK 3 7 2.2193 - 2.1082 1.00 2633 139 0.1044 0.1243
REMARK 3 8 2.1082 - 2.0164 1.00 2623 138 0.1076 0.1486
REMARK 3 9 2.0164 - 1.9388 1.00 2616 138 0.1071 0.1372
REMARK 3 10 1.9388 - 1.8719 1.00 2640 138 0.1026 0.1363
REMARK 3 11 1.8719 - 1.8134 1.00 2605 138 0.1007 0.1266
REMARK 3 12 1.8134 - 1.7615 1.00 2604 137 0.0905 0.1099
REMARK 3 13 1.7615 - 1.7151 1.00 2607 137 0.0913 0.1107
REMARK 3 14 1.7151 - 1.6733 1.00 2605 137 0.0918 0.1285
REMARK 3 15 1.6733 - 1.6353 1.00 2594 136 0.0896 0.1377
REMARK 3 16 1.6353 - 1.6005 1.00 2597 137 0.0868 0.1240
REMARK 3 17 1.6005 - 1.5684 1.00 2595 137 0.0925 0.1205
REMARK 3 18 1.5684 - 1.5388 1.00 2589 136 0.0939 0.1327
REMARK 3 19 1.5388 - 1.5114 1.00 2599 137 0.0988 0.1412
REMARK 3 20 1.5114 - 1.4857 1.00 2579 136 0.1011 0.1616
REMARK 3 21 1.4857 - 1.4618 1.00 2580 135 0.1020 0.1524
REMARK 3 22 1.4618 - 1.4393 1.00 2588 136 0.1103 0.1427
REMARK 3 23 1.4393 - 1.4181 1.00 2600 137 0.1178 0.1515
REMARK 3 24 1.4181 - 1.3981 1.00 2577 136 0.1224 0.1651
REMARK 3 25 1.3981 - 1.3792 0.99 2556 134 0.1316 0.1719
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) : 0.090
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 10.370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 2585
REMARK 3 ANGLE : 0.968 3531
REMARK 3 CHIRALITY : 0.080 373
REMARK 3 PLANARITY : 0.007 468
REMARK 3 DIHEDRAL : 18.836 886
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 5N2T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1200003460.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918409
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69141
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.379
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 11.80
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : 0.06000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.3600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.38
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 12.00
REMARK 200 R MERGE FOR SHELL (I) : 0.49000
REMARK 200 R SYM FOR SHELL (I) : 0.51000
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 8TLN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4 MM TLN, 1.9 M CSCL, 50% DMSO, 50 MM
REMARK 280 TRIS-HCL, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.59833
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 87.19667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 65.39750
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 108.99583
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 21.79917
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 43.59833
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 87.19667
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 108.99583
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 65.39750
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 21.79917
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 E 767 LIES ON A SPECIAL POSITION.
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ILE E 1 CD1
REMARK 470 GLN E 128 CG CD OE1 NE2
REMARK 470 LYS E 182 CD CE NZ
REMARK 470 LYS E 210 CG CD CE NZ
REMARK 470 GLN E 225 CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER E 25 92.82 -160.77
REMARK 500 THR E 26 -58.52 68.42
REMARK 500 SER E 92 -173.24 60.10
REMARK 500 SER E 107 -163.42 61.57
REMARK 500 ASN E 111 48.43 -91.67
REMARK 500 THR E 152 -101.69 -116.40
REMARK 500 ASN E 159 -142.99 55.12
REMARK 500 ASN E 159 -142.99 56.26
REMARK 500 THR E 194 77.11 41.72
REMARK 500 ILE E 232 -61.00 -105.30
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 E 866 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH E 867 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH E 868 DISTANCE = 6.45 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 E 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 57 OD1
REMARK 620 2 ASP E 57 OD2 52.3
REMARK 620 3 ASP E 59 OD1 70.6 122.6
REMARK 620 4 GLN E 61 O 89.0 94.8 88.6
REMARK 620 5 HOH E 590 O 147.3 157.6 77.2 96.0
REMARK 620 6 HOH E 603 O 133.0 82.0 154.9 83.9 79.7
REMARK 620 7 HOH E 771 O 88.1 85.5 87.9 176.1 85.0 100.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 138 OD2
REMARK 620 2 GLU E 177 OE1 78.8
REMARK 620 3 GLU E 177 OE2 127.4 48.7
REMARK 620 4 ASP E 185 OD1 161.3 119.9 71.3
REMARK 620 5 GLU E 187 O 84.5 147.5 141.3 78.7
REMARK 620 6 GLU E 190 OE1 84.9 127.9 121.6 83.3 77.3
REMARK 620 7 GLU E 190 OE2 99.7 82.2 73.1 84.5 128.3 52.3
REMARK 620 8 HOH E 553 O 98.4 79.7 78.2 85.5 75.4 152.1 151.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 142 NE2
REMARK 620 2 HIS E 146 NE2 102.1
REMARK 620 3 GLU E 166 OE1 124.2 96.3
REMARK 620 4 8KK E 410 O03 112.5 127.6 95.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 404 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 177 OE2
REMARK 620 2 ASN E 183 O 92.0
REMARK 620 3 ASP E 185 OD2 87.5 90.7
REMARK 620 4 GLU E 190 OE2 83.5 171.3 81.7
REMARK 620 5 HOH E 561 O 173.3 93.2 96.5 91.8
REMARK 620 6 HOH E 573 O 88.6 92.4 175.2 95.0 87.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 405 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR E 193 O
REMARK 620 2 THR E 194 O 76.5
REMARK 620 3 THR E 194 OG1 77.9 72.3
REMARK 620 4 ILE E 197 O 154.4 79.9 104.4
REMARK 620 5 ASP E 200 OD1 122.9 135.0 73.4 81.4
REMARK 620 6 HOH E 574 O 81.3 150.5 121.6 116.6 73.8
REMARK 620 7 HOH E 739 O 87.1 83.2 153.6 80.3 132.8 76.4
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 ZN E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS E 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS E 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS E 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS E 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8KK E 410
DBREF 5N2T E 1 316 UNP P00800 THER_BACTH 233 548
SEQRES 1 E 316 ILE THR GLY THR SER THR VAL GLY VAL GLY ARG GLY VAL
SEQRES 2 E 316 LEU GLY ASP GLN LYS ASN ILE ASN THR THR TYR SER THR
SEQRES 3 E 316 TYR TYR TYR LEU GLN ASP ASN THR ARG GLY ASN GLY ILE
SEQRES 4 E 316 PHE THR TYR ASP ALA LYS TYR ARG THR THR LEU PRO GLY
SEQRES 5 E 316 SER LEU TRP ALA ASP ALA ASP ASN GLN PHE PHE ALA SER
SEQRES 6 E 316 TYR ASP ALA PRO ALA VAL ASP ALA HIS TYR TYR ALA GLY
SEQRES 7 E 316 VAL THR TYR ASP TYR TYR LYS ASN VAL HIS ASN ARG LEU
SEQRES 8 E 316 SER TYR ASP GLY ASN ASN ALA ALA ILE ARG SER SER VAL
SEQRES 9 E 316 HIS TYR SER GLN GLY TYR ASN ASN ALA PHE TRP ASN GLY
SEQRES 10 E 316 SER GLN MET VAL TYR GLY ASP GLY ASP GLY GLN THR PHE
SEQRES 11 E 316 ILE PRO LEU SER GLY GLY ILE ASP VAL VAL ALA HIS GLU
SEQRES 12 E 316 LEU THR HIS ALA VAL THR ASP TYR THR ALA GLY LEU ILE
SEQRES 13 E 316 TYR GLN ASN GLU SER GLY ALA ILE ASN GLU ALA ILE SER
SEQRES 14 E 316 ASP ILE PHE GLY THR LEU VAL GLU PHE TYR ALA ASN LYS
SEQRES 15 E 316 ASN PRO ASP TRP GLU ILE GLY GLU ASP VAL TYR THR PRO
SEQRES 16 E 316 GLY ILE SER GLY ASP SER LEU ARG SER MET SER ASP PRO
SEQRES 17 E 316 ALA LYS TYR GLY ASP PRO ASP HIS TYR SER LYS ARG TYR
SEQRES 18 E 316 THR GLY THR GLN ASP ASN GLY GLY VAL HIS ILE ASN SER
SEQRES 19 E 316 GLY ILE ILE ASN LYS ALA ALA TYR LEU ILE SER GLN GLY
SEQRES 20 E 316 GLY THR HIS TYR GLY VAL SER VAL VAL GLY ILE GLY ARG
SEQRES 21 E 316 ASP LYS LEU GLY LYS ILE PHE TYR ARG ALA LEU THR GLN
SEQRES 22 E 316 TYR LEU THR PRO THR SER ASN PHE SER GLN LEU ARG ALA
SEQRES 23 E 316 ALA ALA VAL GLN SER ALA THR ASP LEU TYR GLY SER THR
SEQRES 24 E 316 SER GLN GLU VAL ALA SER VAL LYS GLN ALA PHE ASP ALA
SEQRES 25 E 316 VAL GLY VAL LYS
HET ZN E 401 1
HET CA E 402 1
HET CA E 403 1
HET CA E 404 1
HET CA E 405 1
HET DMS E 406 4
HET DMS E 407 4
HET DMS E 408 4
HET DMS E 409 4
HET 8KK E 410 28
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM 8KK ~{N}-[(2~{S})-1-(3-AZANYLPROPYLAMINO)-4-METHYL-1-
HETNAM 2 8KK OXIDANYLIDENE-PENTAN-2-YL]-
HETNAM 3 8KK (PHENYLMETHOXYCARBONYLAMINOMETHYL)PHOSPHONAMIDIC ACID
FORMUL 2 ZN ZN 2+
FORMUL 3 CA 4(CA 2+)
FORMUL 7 DMS 4(C2 H6 O S)
FORMUL 11 8KK C18 H31 N4 O5 P
FORMUL 12 HOH *368(H2 O)
HELIX 1 AA1 ALA E 64 TYR E 66 5 3
HELIX 2 AA2 ASP E 67 ASN E 89 1 23
HELIX 3 AA3 PRO E 132 GLY E 135 5 4
HELIX 4 AA4 GLY E 136 THR E 152 1 17
HELIX 5 AA5 GLN E 158 ASN E 181 1 24
HELIX 6 AA6 ASP E 207 GLY E 212 5 6
HELIX 7 AA7 HIS E 216 ARG E 220 5 5
HELIX 8 AA8 THR E 224 VAL E 230 1 7
HELIX 9 AA9 ASN E 233 GLY E 247 1 15
HELIX 10 AB1 GLY E 259 TYR E 274 1 16
HELIX 11 AB2 ASN E 280 GLY E 297 1 18
HELIX 12 AB3 SER E 300 VAL E 313 1 14
SHEET 1 AA1 5 ALA E 56 ASP E 57 0
SHEET 2 AA1 5 TYR E 28 TYR E 29 -1 N TYR E 28 O ASP E 57
SHEET 3 AA1 5 GLN E 17 TYR E 24 -1 N THR E 23 O TYR E 29
SHEET 4 AA1 5 THR E 4 ARG E 11 -1 N THR E 4 O TYR E 24
SHEET 5 AA1 5 GLN E 61 PHE E 62 1 O PHE E 62 N VAL E 9
SHEET 1 AA2 3 GLN E 31 ASP E 32 0
SHEET 2 AA2 3 ILE E 39 ASP E 43 -1 O ILE E 39 N ASP E 32
SHEET 3 AA2 3 SER E 53 LEU E 54 -1 O SER E 53 N ASP E 43
SHEET 1 AA3 5 GLN E 31 ASP E 32 0
SHEET 2 AA3 5 ILE E 39 ASP E 43 -1 O ILE E 39 N ASP E 32
SHEET 3 AA3 5 ILE E 100 TYR E 106 1 O ILE E 100 N PHE E 40
SHEET 4 AA3 5 MET E 120 GLY E 123 1 O MET E 120 N ARG E 101
SHEET 5 AA3 5 ALA E 113 TRP E 115 -1 N PHE E 114 O VAL E 121
SHEET 1 AA4 2 GLU E 187 ILE E 188 0
SHEET 2 AA4 2 ARG E 203 SER E 204 -1 O ARG E 203 N ILE E 188
SHEET 1 AA5 2 GLY E 248 HIS E 250 0
SHEET 2 AA5 2 VAL E 253 VAL E 255 -1 O VAL E 255 N GLY E 248
LINK OD1 ASP E 57 CA CA E 402 1555 1555 2.57
LINK OD2 ASP E 57 CA CA E 402 1555 1555 2.38
LINK OD1 ASP E 59 CA CA E 402 1555 1555 2.40
LINK O GLN E 61 CA CA E 402 1555 1555 2.26
LINK OD2 ASP E 138 CA CA E 403 1555 1555 2.38
LINK NE2 HIS E 142 ZN ZN E 401 1555 1555 2.04
LINK NE2 HIS E 146 ZN ZN E 401 1555 1555 2.04
LINK OE1 GLU E 166 ZN ZN E 401 1555 1555 1.99
LINK OE1 GLU E 177 CA CA E 403 1555 1555 2.47
LINK OE2 GLU E 177 CA CA E 403 1555 1555 2.75
LINK OE2 GLU E 177 CA CA E 404 1555 1555 2.41
LINK O ASN E 183 CA CA E 404 1555 1555 2.31
LINK OD1 ASP E 185 CA CA E 403 1555 1555 2.49
LINK OD2 ASP E 185 CA CA E 404 1555 1555 2.31
LINK O GLU E 187 CA CA E 403 1555 1555 2.34
LINK OE1 GLU E 190 CA CA E 403 1555 1555 2.48
LINK OE2 GLU E 190 CA CA E 403 1555 1555 2.51
LINK OE2 GLU E 190 CA CA E 404 1555 1555 2.30
LINK O TYR E 193 CA CA E 405 1555 1555 2.37
LINK O THR E 194 CA CA E 405 1555 1555 2.38
LINK OG1 THR E 194 CA CA E 405 1555 1555 2.35
LINK O ILE E 197 CA CA E 405 1555 1555 2.28
LINK OD1 ASP E 200 CA CA E 405 1555 1555 2.38
LINK ZN ZN E 401 O03 8KK E 410 1555 1555 1.97
LINK CA CA E 402 O HOH E 590 1555 1555 2.40
LINK CA CA E 402 O HOH E 603 1555 1555 2.42
LINK CA CA E 402 O HOH E 771 1555 1555 2.35
LINK CA CA E 403 O HOH E 553 1555 1555 2.46
LINK CA CA E 404 O HOH E 561 1555 1555 2.35
LINK CA CA E 404 O HOH E 573 1555 1555 2.35
LINK CA CA E 405 O HOH E 574 1555 1555 2.42
LINK CA CA E 405 O HOH E 739 1555 1555 2.44
CISPEP 1 LEU E 50 PRO E 51 0 4.13
SITE 1 AC1 4 HIS E 142 HIS E 146 GLU E 166 8KK E 410
SITE 1 AC2 6 ASP E 57 ASP E 59 GLN E 61 HOH E 590
SITE 2 AC2 6 HOH E 603 HOH E 771
SITE 1 AC3 6 ASP E 138 GLU E 177 ASP E 185 GLU E 187
SITE 2 AC3 6 GLU E 190 HOH E 553
SITE 1 AC4 6 GLU E 177 ASN E 183 ASP E 185 GLU E 190
SITE 2 AC4 6 HOH E 561 HOH E 573
SITE 1 AC5 6 TYR E 193 THR E 194 ILE E 197 ASP E 200
SITE 2 AC5 6 HOH E 574 HOH E 739
SITE 1 AC6 6 TYR E 66 HIS E 216 SER E 218 TYR E 251
SITE 2 AC6 6 HOH E 836 HOH E 856
SITE 1 AC7 4 TYR E 110 ASN E 112 PHE E 114 8KK E 410
SITE 1 AC8 4 THR E 2 GLY E 3 GLN E 31 ASN E 33
SITE 1 AC9 5 GLY E 259 ARG E 260 ASP E 261 HOH E 528
SITE 2 AC9 5 HOH E 667
SITE 1 AD1 19 ASN E 111 ASN E 112 ALA E 113 PHE E 114
SITE 2 AD1 19 ASN E 116 HIS E 142 GLU E 143 HIS E 146
SITE 3 AD1 19 TYR E 157 GLU E 166 LEU E 202 ARG E 203
SITE 4 AD1 19 HIS E 231 ZN E 401 DMS E 407 HOH E 534
SITE 5 AD1 19 HOH E 571 HOH E 654 HOH E 657
CRYST1 93.047 93.047 130.795 90.00 90.00 120.00 P 61 2 2 12
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 0.010747 0.006205 0.000000 0.00000
SCALE2 0.000000 0.012410 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007646 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
