HEADER HYDROLASE 07-MAY-16 5JS3
TITLE THERMOLYSIN IN COMPLEX WITH JC114.
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 HYDROLASE, METALLOPROTEASE, HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.G.KRIMMER,J.CRAMER,A.HEINE,G.KLEBE
REVDAT 2 10-JAN-24 5JS3 1 LINK
REVDAT 1 21-DEC-16 5JS3 0
JRNL AUTH S.G.KRIMMER,J.CRAMER,M.BETZ,V.FRIDH,R.KARLSSON,A.HEINE,
JRNL AUTH 2 G.KLEBE
JRNL TITL RATIONAL DESIGN OF THERMODYNAMIC AND KINETIC BINDING
JRNL TITL 2 PROFILES BY OPTIMIZING SURFACE WATER NETWORKS COATING
JRNL TITL 3 PROTEIN-BOUND LIGANDS.
JRNL REF J. MED. CHEM. V. 59 10530 2016
JRNL REFN ISSN 1520-4804
JRNL PMID 27933956
JRNL DOI 10.1021/ACS.JMEDCHEM.6B00998
REMARK 2
REMARK 2 RESOLUTION. 1.16 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.16
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.10
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 114611
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.104
REMARK 3 R VALUE (WORKING SET) : 0.103
REMARK 3 FREE R VALUE : 0.124
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5731
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 40.1279 - 3.5991 1.00 4006 211 0.1339 0.1496
REMARK 3 2 3.5991 - 2.8570 1.00 3797 200 0.1158 0.1388
REMARK 3 3 2.8570 - 2.4959 1.00 3722 196 0.1083 0.1249
REMARK 3 4 2.4959 - 2.2677 1.00 3721 196 0.1041 0.1210
REMARK 3 5 2.2677 - 2.1052 1.00 3686 194 0.1001 0.1073
REMARK 3 6 2.1052 - 1.9811 1.00 3684 194 0.1003 0.1072
REMARK 3 7 1.9811 - 1.8819 1.00 3668 193 0.0971 0.1134
REMARK 3 8 1.8819 - 1.7999 1.00 3666 193 0.0951 0.1078
REMARK 3 9 1.7999 - 1.7307 1.00 3637 191 0.0934 0.1181
REMARK 3 10 1.7307 - 1.6709 1.00 3643 192 0.0905 0.1127
REMARK 3 11 1.6709 - 1.6187 1.00 3652 192 0.0871 0.1102
REMARK 3 12 1.6187 - 1.5724 1.00 3612 190 0.0844 0.1220
REMARK 3 13 1.5724 - 1.5310 1.00 3629 191 0.0822 0.1131
REMARK 3 14 1.5310 - 1.4937 1.00 3601 190 0.0840 0.1146
REMARK 3 15 1.4937 - 1.4597 1.00 3626 191 0.0822 0.1144
REMARK 3 16 1.4597 - 1.4286 1.00 3600 189 0.0829 0.1012
REMARK 3 17 1.4286 - 1.4001 1.00 3613 190 0.0852 0.1120
REMARK 3 18 1.4001 - 1.3736 1.00 3605 190 0.0884 0.1143
REMARK 3 19 1.3736 - 1.3491 1.00 3594 189 0.0876 0.1155
REMARK 3 20 1.3491 - 1.3262 1.00 3593 189 0.0908 0.1093
REMARK 3 21 1.3262 - 1.3048 1.00 3568 188 0.0921 0.1149
REMARK 3 22 1.3048 - 1.2848 0.99 3591 189 0.0931 0.1242
REMARK 3 23 1.2848 - 1.2659 0.99 3576 188 0.0969 0.1330
REMARK 3 24 1.2659 - 1.2480 0.99 3567 188 0.0999 0.1207
REMARK 3 25 1.2480 - 1.2312 0.99 3581 189 0.1024 0.1351
REMARK 3 26 1.2312 - 1.2152 0.99 3570 187 0.1038 0.1303
REMARK 3 27 1.2152 - 1.2000 0.99 3542 187 0.1072 0.1300
REMARK 3 28 1.2000 - 1.1855 0.99 3553 187 0.1051 0.1453
REMARK 3 29 1.1855 - 1.1717 0.99 3547 187 0.1101 0.1168
REMARK 3 30 1.1717 - 1.1586 0.96 3430 180 0.1160 0.1493
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) : 0.060
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 8.690
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 : 0.010 2618
REMARK 3 ANGLE : 1.190 3579
REMARK 3 CHIRALITY : 0.238 378
REMARK 3 PLANARITY : 0.009 470
REMARK 3 DIHEDRAL : 17.505 917
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 5JS3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221146.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-AUG-14
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) : 0.918410
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 114612
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.160
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 (%) : 99.5
REMARK 200 DATA REDUNDANCY : 16.08
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.5400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.16
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 15.38
REMARK 200 R MERGE FOR SHELL (I) : 0.44700
REMARK 200 R SYM FOR SHELL (I) : NULL
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 (%): 47.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM TRIS/HCL, 1.9 M CSCL, 50% DMSO,
REMARK 280 PH 7.5, VAPOR DIFFUSION, TEMPERATURE 291.15K
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 43.82100
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 87.64200
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 65.73150
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 109.55250
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 21.91050
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 43.82100
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 87.64200
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 109.55250
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 65.73150
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 21.91050
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: 1450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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 794 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 CG2 CD1
REMARK 470 LYS E 182 CG 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: 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 HE ARG E 11 O HOH E 501 1.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP E 16 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
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 SER E 25 94.43 -160.02
REMARK 500 THR E 26 -61.43 71.11
REMARK 500 SER E 92 -173.67 60.47
REMARK 500 SER E 107 -161.24 59.94
REMARK 500 ASN E 111 56.32 -91.35
REMARK 500 THR E 152 -100.56 -118.96
REMARK 500 ASN E 159 -144.50 54.81
REMARK 500 THR E 194 74.10 43.03
REMARK 500 ILE E 232 -60.24 -106.62
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 919 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH E 920 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH E 921 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH E 922 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH E 923 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH E 924 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH E 925 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH E 926 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH E 927 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH E 928 DISTANCE = 6.98 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 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 57 OD1
REMARK 620 2 ASP E 57 OD2 51.9
REMARK 620 3 ASP E 59 OD1 121.9 70.3
REMARK 620 4 GLN E 61 O 94.5 89.3 89.5
REMARK 620 5 HOH E 592 O 158.3 147.1 77.2 95.9
REMARK 620 6 HOH E 604 O 82.6 133.2 155.0 83.2 79.7
REMARK 620 7 HOH E 793 O 85.0 87.7 88.0 176.6 85.7 100.1
REMARK 620 N 1 2 3 4 5 6
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 138 OD2
REMARK 620 2 GLU E 177 OE1 77.6
REMARK 620 3 GLU E 177 OE2 127.1 49.5
REMARK 620 4 ASP E 185 OD1 160.1 122.3 72.9
REMARK 620 5 GLU E 187 O 84.0 146.7 141.3 78.4
REMARK 620 6 GLU E 190 OE1 83.9 127.7 123.6 83.0 76.7
REMARK 620 7 GLU E 190 OE2 99.5 83.3 75.0 84.1 127.4 52.0
REMARK 620 8 HOH E 589 O 96.5 79.3 78.2 88.1 75.4 151.9 153.2
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 103.1
REMARK 620 3 GLU E 166 OE2 125.3 96.7
REMARK 620 4 6MG E 411 O45 111.5 126.2 95.4
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 92.1
REMARK 620 3 ASP E 185 OD2 87.9 91.8
REMARK 620 4 GLU E 190 OE2 83.6 172.0 81.3
REMARK 620 5 HOH E 552 O 87.5 94.0 172.7 92.5
REMARK 620 6 HOH E 579 O 172.3 93.1 97.6 91.9 86.5
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 77.0
REMARK 620 3 THR E 194 OG1 76.4 71.4
REMARK 620 4 ILE E 197 O 154.4 79.3 105.0
REMARK 620 5 ASP E 200 OD1 123.6 132.7 73.6 80.1
REMARK 620 6 HOH E 609 O 81.4 152.1 120.2 117.4 74.5
REMARK 620 7 HOH E 770 O 87.2 83.8 152.7 80.8 133.5 77.6
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 GOL E 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL 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 DMS E 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6MG E 411
DBREF 5JS3 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 GOL E 406 6
HET GOL E 407 6
HET DMS E 408 4
HET DMS E 409 4
HET DMS E 410 4
HET 6MG E 411 35
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM 6MG N~2~-[(R)-({[(BENZYLOXY)CARBONYL]AMINO}METHYL)
HETNAM 2 6MG (HYDROXY)PHOSPHORYL]-N-[(2S)-2,3,3-TRIMETHYLBUTYL]-L-
HETNAM 3 6MG LEUCINAMIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ZN ZN 2+
FORMUL 3 CA 4(CA 2+)
FORMUL 7 GOL 2(C3 H8 O3)
FORMUL 9 DMS 3(C2 H6 O S)
FORMUL 12 6MG C22 H38 N3 O5 P
FORMUL 13 HOH *428(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 GLY E 8 O ILE E 20
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 403 1555 1555 2.39
LINK OD2 ASP E 57 CA CA E 403 1555 1555 2.59
LINK OD1 ASP E 59 CA CA E 403 1555 1555 2.38
LINK O GLN E 61 CA CA E 403 1555 1555 2.28
LINK OD2 ASP E 138 CA CA E 402 1555 1555 2.39
LINK NE2 HIS E 142 ZN ZN E 401 1555 1555 2.02
LINK NE2 HIS E 146 ZN ZN E 401 1555 1555 2.02
LINK OE2 GLU E 166 ZN ZN E 401 1555 1555 1.98
LINK OE1 GLU E 177 CA CA E 402 1555 1555 2.47
LINK OE2 GLU E 177 CA CA E 402 1555 1555 2.71
LINK OE2 GLU E 177 CA CA E 404 1555 1555 2.46
LINK O ASN E 183 CA CA E 404 1555 1555 2.28
LINK OD1 ASP E 185 CA CA E 402 1555 1555 2.47
LINK OD2 ASP E 185 CA CA E 404 1555 1555 2.33
LINK O GLU E 187 CA CA E 402 1555 1555 2.35
LINK OE1 GLU E 190 CA CA E 402 1555 1555 2.49
LINK OE2 GLU E 190 CA CA E 402 1555 1555 2.51
LINK OE2 GLU E 190 CA CA E 404 1555 1555 2.31
LINK O TYR E 193 CA CA E 405 1555 1555 2.37
LINK O THR E 194 CA CA E 405 1555 1555 2.39
LINK OG1 THR E 194 CA CA E 405 1555 1555 2.37
LINK O ILE E 197 CA CA E 405 1555 1555 2.30
LINK OD1 ASP E 200 CA CA E 405 1555 1555 2.38
LINK ZN ZN E 401 O45 6MG E 411 1555 1555 1.97
LINK CA CA E 402 O HOH E 589 1555 1555 2.41
LINK CA CA E 403 O HOH E 592 1555 1555 2.39
LINK CA CA E 403 O HOH E 604 1555 1555 2.41
LINK CA CA E 403 O HOH E 793 1555 1555 2.34
LINK CA CA E 404 O HOH E 552 1555 1555 2.35
LINK CA CA E 404 O HOH E 579 1555 1555 2.29
LINK CA CA E 405 O HOH E 609 1555 1555 2.40
LINK CA CA E 405 O HOH E 770 1555 1555 2.38
CISPEP 1 LEU E 50 PRO E 51 0 3.82
SITE 1 AC1 4 HIS E 142 HIS E 146 GLU E 166 6MG E 411
SITE 1 AC2 6 ASP E 138 GLU E 177 ASP E 185 GLU E 187
SITE 2 AC2 6 GLU E 190 HOH E 589
SITE 1 AC3 6 ASP E 57 ASP E 59 GLN E 61 HOH E 592
SITE 2 AC3 6 HOH E 604 HOH E 793
SITE 1 AC4 6 GLU E 177 ASN E 183 ASP E 185 GLU E 190
SITE 2 AC4 6 HOH E 552 HOH E 579
SITE 1 AC5 6 TYR E 193 THR E 194 ILE E 197 ASP E 200
SITE 2 AC5 6 HOH E 609 HOH E 770
SITE 1 AC6 8 PHE E 114 TRP E 115 HIS E 146 TYR E 157
SITE 2 AC6 8 6MG E 411 HOH E 518 HOH E 562 HOH E 732
SITE 1 AC7 8 GLY E 109 TYR E 110 ASN E 111 ASN E 112
SITE 2 AC7 8 HOH E 517 HOH E 624 HOH E 670 HOH E 757
SITE 1 AC8 6 TYR E 66 HIS E 216 SER E 218 TYR E 251
SITE 2 AC8 6 HOH E 887 HOH E 907
SITE 1 AC9 5 ILE E 1 THR E 2 GLY E 3 GLN E 31
SITE 2 AC9 5 ASN E 33
SITE 1 AD1 5 TYR E 110 ASN E 112 PHE E 114 6MG E 411
SITE 2 AD1 5 HOH E 692
SITE 1 AD2 18 TYR E 106 ASN E 112 ALA E 113 PHE E 114
SITE 2 AD2 18 TRP E 115 HIS E 142 GLU E 143 HIS E 146
SITE 3 AD2 18 TYR E 157 GLU E 166 LEU E 202 ARG E 203
SITE 4 AD2 18 HIS E 231 ZN E 401 GOL E 406 DMS E 410
SITE 5 AD2 18 HOH E 694 HOH E 796
CRYST1 92.616 92.616 131.463 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 0.010797 0.006234 0.000000 0.00000
SCALE2 0.000000 0.012468 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007607 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
