HEADER HYDROLASE 19-APR-18 6D5P
TITLE HEXAGONAL THERMOLYSIN CRYOCOOLED TO 100 K WITH 20% XYLOSE AS
TITLE 2 CRYOPROTECTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOLYSIN;
COMPND 3 CHAIN: A;
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 ZINC PROTEASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.H.JUERS
REVDAT 5 13-MAR-24 6D5P 1 HETSYN
REVDAT 4 29-JUL-20 6D5P 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 01-JAN-20 6D5P 1 REMARK
REVDAT 2 31-OCT-18 6D5P 1 JRNL
REVDAT 1 19-SEP-18 6D5P 0
JRNL AUTH D.H.JUERS,C.A.FARLEY,C.P.SAXBY,R.A.COTTER,J.K.B.CAHN,
JRNL AUTH 2 R.C.HOLTON-BURKE,K.HARRISON,Z.WU
JRNL TITL THE IMPACT OF CRYOSOLUTION THERMAL CONTRACTION ON PROTEINS
JRNL TITL 2 AND PROTEIN CRYSTALS: VOLUMES, CONFORMATION AND ORDER.
JRNL REF ACTA CRYSTALLOGR D STRUCT V. 74 922 2018
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 30198901
JRNL DOI 10.1107/S2059798318008793
REMARK 2
REMARK 2 RESOLUTION. 3.00 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 13.75
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.327
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 6859
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.237
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.308
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.724
REMARK 3 FREE R VALUE TEST SET COUNT : 324
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 13.7526 - 3.7669 0.97 3326 171 0.1860 0.2440
REMARK 3 2 3.7669 - 3.0001 0.99 3209 153 0.3051 0.4197
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) : 0.460
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.317
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.83
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.14
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 : 0.002 2551
REMARK 3 ANGLE : 0.459 3476
REMARK 3 CHIRALITY : 0.039 377
REMARK 3 PLANARITY : 0.002 453
REMARK 3 DIHEDRAL : 12.233 873
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 6D5P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-APR-18.
REMARK 100 THE DEPOSITION ID IS D_1000233989.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUL-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : AGILENT SUPERNOVA
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : OXFORD ONYX CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6950
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 13.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.16
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 100 MG/ML IN 45% DMSO, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 43.04167
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 86.08333
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 64.56250
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 107.60417
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 21.52083
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 43.04167
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 86.08333
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 107.60417
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 64.56250
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 21.52083
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 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 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 A 555 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 597 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 638 LIES ON A SPECIAL POSITION.
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 C VAL A 401 N LYS A 402 1.33
REMARK 500 O ALA A 141 HG1 THR A 145 1.56
REMARK 500 HH TYR A 274 OD2 ASP A 294 1.58
REMARK 500 O SER A 300 O HOH A 501 1.99
REMARK 500 O HOH A 521 O HOH A 553 2.18
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 A 25 86.18 -164.32
REMARK 500 THR A 26 -68.93 71.54
REMARK 500 SER A 92 -172.49 62.86
REMARK 500 SER A 107 -163.36 52.53
REMARK 500 ASN A 111 54.94 -95.58
REMARK 500 ASN A 116 31.75 -93.86
REMARK 500 GLN A 128 -62.16 -105.73
REMARK 500 THR A 152 -98.42 -118.00
REMARK 500 ASN A 159 -148.19 64.51
REMARK 500 THR A 194 87.80 38.92
REMARK 500 ILE A 232 -65.45 -104.48
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 613 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH A 614 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH A 615 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH A 616 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH A 617 DISTANCE = 6.87 ANGSTROMS
REMARK 525 HOH A 618 DISTANCE = 7.07 ANGSTROMS
REMARK 525 HOH A 619 DISTANCE = 7.20 ANGSTROMS
REMARK 525 HOH A 620 DISTANCE = 7.29 ANGSTROMS
REMARK 525 HOH A 621 DISTANCE = 7.36 ANGSTROMS
REMARK 525 HOH A 622 DISTANCE = 7.47 ANGSTROMS
REMARK 525 HOH A 623 DISTANCE = 7.65 ANGSTROMS
REMARK 525 HOH A 624 DISTANCE = 7.74 ANGSTROMS
REMARK 525 HOH A 625 DISTANCE = 7.80 ANGSTROMS
REMARK 525 HOH A 626 DISTANCE = 7.97 ANGSTROMS
REMARK 525 HOH A 627 DISTANCE = 8.19 ANGSTROMS
REMARK 525 HOH A 628 DISTANCE = 8.20 ANGSTROMS
REMARK 525 HOH A 629 DISTANCE = 8.27 ANGSTROMS
REMARK 525 HOH A 630 DISTANCE = 8.27 ANGSTROMS
REMARK 525 HOH A 631 DISTANCE = 8.43 ANGSTROMS
REMARK 525 HOH A 632 DISTANCE = 8.73 ANGSTROMS
REMARK 525 HOH A 633 DISTANCE = 8.73 ANGSTROMS
REMARK 525 HOH A 634 DISTANCE = 8.89 ANGSTROMS
REMARK 525 HOH A 635 DISTANCE = 9.57 ANGSTROMS
REMARK 525 HOH A 636 DISTANCE = 9.86 ANGSTROMS
REMARK 525 HOH A 637 DISTANCE = 10.22 ANGSTROMS
REMARK 525 HOH A 638 DISTANCE = 10.72 ANGSTROMS
REMARK 525 HOH A 639 DISTANCE = 11.12 ANGSTROMS
REMARK 525 HOH A 640 DISTANCE = 11.29 ANGSTROMS
REMARK 525 HOH A 641 DISTANCE = 11.75 ANGSTROMS
REMARK 525 HOH A 642 DISTANCE = 11.94 ANGSTROMS
REMARK 525 HOH A 643 DISTANCE = 12.52 ANGSTROMS
REMARK 525 HOH A 644 DISTANCE = 15.25 ANGSTROMS
REMARK 525 HOH A 645 DISTANCE = 15.33 ANGSTROMS
REMARK 525 HOH A 646 DISTANCE = 16.14 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 VAL A 401
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 405 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 57 OD1
REMARK 620 2 ASP A 57 OD2 50.0
REMARK 620 3 ASP A 59 OD1 116.6 66.6
REMARK 620 4 GLN A 61 O 88.7 87.5 89.1
REMARK 620 5 HOH A 511 O 78.2 127.7 163.6 84.2
REMARK 620 6 HOH A 569 O 91.8 91.1 88.7 177.7 98.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 404 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 138 OD2
REMARK 620 2 GLU A 177 OE1 65.5
REMARK 620 3 GLU A 177 OE2 115.7 52.7
REMARK 620 4 ASP A 185 OD1 151.4 135.1 82.5
REMARK 620 5 GLU A 187 O 93.4 144.3 148.2 76.4
REMARK 620 6 GLU A 190 OE1 75.5 120.7 120.7 76.3 77.0
REMARK 620 7 GLU A 190 OE2 89.0 82.6 68.6 77.1 127.6 53.0
REMARK 620 8 HOH A 525 O 107.3 84.3 84.2 95.8 74.7 151.7 152.4
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 403 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 142 NE2
REMARK 620 2 HIS A 146 NE2 93.4
REMARK 620 3 GLU A 166 OE2 119.8 88.6
REMARK 620 4 HOH A 526 O 125.5 133.5 91.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 407 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 177 OE2
REMARK 620 2 ASN A 183 O 95.6
REMARK 620 3 ASP A 185 OD2 89.9 94.5
REMARK 620 4 GLU A 190 OE2 70.9 166.2 82.8
REMARK 620 N 1 2 3
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 TYR A 193 O
REMARK 620 2 THR A 194 O 65.1
REMARK 620 3 THR A 194 OG1 63.5 60.7
REMARK 620 4 ILE A 197 O 150.8 89.3 92.5
REMARK 620 5 ASP A 200 OD1 110.4 119.0 64.1 68.8
REMARK 620 6 HOH A 507 O 82.5 143.3 120.3 125.8 87.3
REMARK 620 7 HOH A 541 O 73.9 77.8 129.5 115.8 163.1 76.9
REMARK 620 N 1 2 3 4 5 6
DBREF 6D5P A 1 316 UNP P00800 THER_BACTH 233 548
SEQRES 1 A 316 ILE THR GLY THR SER THR VAL GLY VAL GLY ARG GLY VAL
SEQRES 2 A 316 LEU GLY ASP GLN LYS ASN ILE ASN THR THR TYR SER THR
SEQRES 3 A 316 TYR TYR TYR LEU GLN ASP ASN THR ARG GLY ASN GLY ILE
SEQRES 4 A 316 PHE THR TYR ASP ALA LYS TYR ARG THR THR LEU PRO GLY
SEQRES 5 A 316 SER LEU TRP ALA ASP ALA ASP ASN GLN PHE PHE ALA SER
SEQRES 6 A 316 TYR ASP ALA PRO ALA VAL ASP ALA HIS TYR TYR ALA GLY
SEQRES 7 A 316 VAL THR TYR ASP TYR TYR LYS ASN VAL HIS ASN ARG LEU
SEQRES 8 A 316 SER TYR ASP GLY ASN ASN ALA ALA ILE ARG SER SER VAL
SEQRES 9 A 316 HIS TYR SER GLN GLY TYR ASN ASN ALA PHE TRP ASN GLY
SEQRES 10 A 316 SER GLN MET VAL TYR GLY ASP GLY ASP GLY GLN THR PHE
SEQRES 11 A 316 ILE PRO LEU SER GLY GLY ILE ASP VAL VAL ALA HIS GLU
SEQRES 12 A 316 LEU THR HIS ALA VAL THR ASP TYR THR ALA GLY LEU ILE
SEQRES 13 A 316 TYR GLN ASN GLU SER GLY ALA ILE ASN GLU ALA ILE SER
SEQRES 14 A 316 ASP ILE PHE GLY THR LEU VAL GLU PHE TYR ALA ASN LYS
SEQRES 15 A 316 ASN PRO ASP TRP GLU ILE GLY GLU ASP VAL TYR THR PRO
SEQRES 16 A 316 GLY ILE SER GLY ASP SER LEU ARG SER MET SER ASP PRO
SEQRES 17 A 316 ALA LYS TYR GLY ASP PRO ASP HIS TYR SER LYS ARG TYR
SEQRES 18 A 316 THR GLY THR GLN ASP ASN GLY GLY VAL HIS ILE ASN SER
SEQRES 19 A 316 GLY ILE ILE ASN LYS ALA ALA TYR LEU ILE SER GLN GLY
SEQRES 20 A 316 GLY THR HIS TYR GLY VAL SER VAL VAL GLY ILE GLY ARG
SEQRES 21 A 316 ASP LYS LEU GLY LYS ILE PHE TYR ARG ALA LEU THR GLN
SEQRES 22 A 316 TYR LEU THR PRO THR SER ASN PHE SER GLN LEU ARG ALA
SEQRES 23 A 316 ALA ALA VAL GLN SER ALA THR ASP LEU TYR GLY SER THR
SEQRES 24 A 316 SER GLN GLU VAL ALA SER VAL LYS GLN ALA PHE ASP ALA
SEQRES 25 A 316 VAL GLY VAL LYS
HET VAL A 401 15
HET LYS A 402 23
HET ZN A 403 1
HET CA A 404 1
HET CA A 405 1
HET CA A 406 1
HET CA A 407 1
HET XYP A 408 20
HET XYP A 409 20
HET XYP A 410 20
HETNAM VAL VALINE
HETNAM LYS LYSINE
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM XYP BETA-D-XYLOPYRANOSE
HETSYN XYP BETA-D-XYLOSE; D-XYLOSE; XYLOSE
FORMUL 2 VAL C5 H11 N O2
FORMUL 3 LYS C6 H15 N2 O2 1+
FORMUL 4 ZN ZN 2+
FORMUL 5 CA 4(CA 2+)
FORMUL 9 XYP 3(C5 H10 O5)
FORMUL 12 HOH *146(H2 O)
HELIX 1 AA1 ALA A 64 TYR A 66 5 3
HELIX 2 AA2 ASP A 67 VAL A 87 1 21
HELIX 3 AA3 PRO A 132 GLY A 135 5 4
HELIX 4 AA4 GLY A 136 THR A 152 1 17
HELIX 5 AA5 GLN A 158 ASN A 181 1 24
HELIX 6 AA6 ASP A 207 GLY A 212 5 6
HELIX 7 AA7 HIS A 216 ARG A 220 5 5
HELIX 8 AA8 THR A 224 VAL A 230 1 7
HELIX 9 AA9 ASN A 233 GLY A 247 1 15
HELIX 10 AB1 GLY A 259 TYR A 274 1 16
HELIX 11 AB2 ASN A 280 GLY A 297 1 18
HELIX 12 AB3 SER A 300 VAL A 313 1 14
SHEET 1 AA1 5 ALA A 56 ASP A 57 0
SHEET 2 AA1 5 TYR A 28 TYR A 29 -1 N TYR A 28 O ASP A 57
SHEET 3 AA1 5 GLN A 17 TYR A 24 -1 N THR A 23 O TYR A 29
SHEET 4 AA1 5 THR A 4 ARG A 11 -1 N THR A 6 O THR A 22
SHEET 5 AA1 5 GLN A 61 PHE A 62 1 O PHE A 62 N VAL A 9
SHEET 1 AA2 3 GLN A 31 ASP A 32 0
SHEET 2 AA2 3 ILE A 39 ASP A 43 -1 O ILE A 39 N ASP A 32
SHEET 3 AA2 3 SER A 53 LEU A 54 -1 O SER A 53 N ASP A 43
SHEET 1 AA3 5 GLN A 31 ASP A 32 0
SHEET 2 AA3 5 ILE A 39 ASP A 43 -1 O ILE A 39 N ASP A 32
SHEET 3 AA3 5 ILE A 100 TYR A 106 1 O SER A 102 N TYR A 42
SHEET 4 AA3 5 MET A 120 GLY A 123 1 O TYR A 122 N SER A 103
SHEET 5 AA3 5 ALA A 113 TRP A 115 -1 N PHE A 114 O VAL A 121
SHEET 1 AA4 2 GLU A 187 ILE A 188 0
SHEET 2 AA4 2 ARG A 203 SER A 204 -1 O ARG A 203 N ILE A 188
SHEET 1 AA5 2 GLY A 248 HIS A 250 0
SHEET 2 AA5 2 VAL A 253 VAL A 255 -1 O VAL A 255 N GLY A 248
LINK OD1 ASP A 57 CA CA A 405 1555 1555 2.77
LINK OD2 ASP A 57 CA CA A 405 1555 1555 2.37
LINK OD1 ASP A 59 CA CA A 405 1555 1555 2.26
LINK O GLN A 61 CA CA A 405 1555 1555 2.36
LINK OD2 ASP A 138 CA CA A 404 1555 1555 2.64
LINK NE2 HIS A 142 ZN ZN A 403 1555 1555 2.10
LINK NE2 HIS A 146 ZN ZN A 403 1555 1555 2.26
LINK OE2 GLU A 166 ZN ZN A 403 1555 1555 1.83
LINK OE1 GLU A 177 CA CA A 404 1555 1555 2.40
LINK OE2 GLU A 177 CA CA A 404 1555 1555 2.53
LINK OE2 GLU A 177 CA CA A 407 1555 1555 2.42
LINK O ASN A 183 CA CA A 407 1555 1555 2.18
LINK OD1 ASP A 185 CA CA A 404 1555 1555 2.75
LINK OD2 ASP A 185 CA CA A 407 1555 1555 2.34
LINK O GLU A 187 CA CA A 404 1555 1555 2.28
LINK OE1 GLU A 190 CA CA A 404 1555 1555 2.59
LINK OE2 GLU A 190 CA CA A 404 1555 1555 2.28
LINK OE2 GLU A 190 CA CA A 407 1555 1555 2.26
LINK O TYR A 193 CA CA A 406 1555 1555 2.52
LINK O THR A 194 CA CA A 406 1555 1555 2.33
LINK OG1 THR A 194 CA CA A 406 1555 1555 2.84
LINK O ILE A 197 CA CA A 406 1555 1555 2.29
LINK OD1 ASP A 200 CA CA A 406 1555 1555 2.43
LINK ZN ZN A 403 O HOH A 526 1555 1555 2.26
LINK CA CA A 404 O HOH A 525 1555 1555 2.58
LINK CA CA A 405 O HOH A 511 1555 1555 2.39
LINK CA CA A 405 O HOH A 569 1555 1555 2.78
LINK CA CA A 406 O HOH A 507 1555 1555 2.52
LINK CA CA A 406 O HOH A 541 1555 1555 2.39
CISPEP 1 LEU A 50 PRO A 51 0 -0.68
CRYST1 93.307 93.307 129.125 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 0.010717 0.006188 0.000000 0.00000
SCALE2 0.000000 0.012375 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007744 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
