HEADER CHAPERONE 12-MAY-19 6OWY
TITLE SPY H96L:IM7 K20PI-PHE COMPLEX; MULTIPLE ANOMALOUS DATASETS CONTAINED
TITLE 2 HEREIN FOR ELEMENT IDENTIFICATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PERIPLASMIC CHAPERONE SPY;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: SPHEROPLAST PROTEIN Y;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PERIPLASMIC, CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.ROCCHIO,R.DUMAN,K.EL OMARI,V.MYKHAYLYK,Z.YAN,A.WAGNER,
AUTHOR 2 J.C.A.BARDWELL,S.HOROWITZ
REVDAT 6 11-OCT-23 6OWY 1 LINK
REVDAT 5 11-DEC-19 6OWY 1 JRNL
REVDAT 4 20-NOV-19 6OWY 1 REMARK
REVDAT 3 09-OCT-19 6OWY 1 REMARK CRYST1 ATOM
REVDAT 2 05-JUN-19 6OWY 1 AUTHOR JRNL
REVDAT 1 29-MAY-19 6OWY 0
JRNL AUTH S.ROCCHIO,R.DUMAN,K.EL OMARI,V.MYKHAYLYK,C.ORR,Z.YAN,
JRNL AUTH 2 L.SALMON,A.WAGNER,J.C.A.BARDWELL,S.HOROWITZ
JRNL TITL IDENTIFYING DYNAMIC, PARTIALLY OCCUPIED RESIDUES USING
JRNL TITL 2 ANOMALOUS SCATTERING.
JRNL REF ACTA CRYSTALLOGR D STRUCT V. 75 1084 2019
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 31793902
JRNL DOI 10.1107/S2059798319014475
REMARK 2
REMARK 2 RESOLUTION. 2.07 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3260
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) : 2.07
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.84
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 15674
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.230
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.990
REMARK 3 FREE R VALUE TEST SET COUNT : 939
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 42.2600 - 3.9600 1.00 2318 148 0.2056 0.2525
REMARK 3 2 3.9600 - 3.1400 1.00 2149 137 0.2113 0.2246
REMARK 3 3 3.1400 - 2.7500 1.00 2083 133 0.2318 0.3089
REMARK 3 4 2.7500 - 2.4900 1.00 2088 132 0.2452 0.3274
REMARK 3 5 2.4900 - 2.3200 0.99 2051 132 0.2762 0.3203
REMARK 3 6 2.3200 - 2.1800 1.00 2023 129 0.3137 0.3831
REMARK 3 7 2.1800 - 2.0700 0.99 2023 128 0.3579 0.4118
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) : 0.332
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.912
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 46.91
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.31
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 : 0.013 1432
REMARK 3 ANGLE : 1.227 1917
REMARK 3 CHIRALITY : 0.054 215
REMARK 3 PLANARITY : 0.007 257
REMARK 3 DIHEDRAL : 24.537 551
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 6OWY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1000241499.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-OCT-17
REMARK 200 TEMPERATURE (KELVIN) : 75
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I23
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 2.3843, 2.7552
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15762
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.070
REMARK 200 RESOLUTION RANGE LOW (A) : 42.840
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
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 : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 5WNW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22-34% PEG 3000, 70-270 MM ZINC
REMARK 280 ACETATE, AND 0.1 M IMIDAZOLE, PH 8.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+3/4
REMARK 290 8555 -Y,-X,-Z+1/4
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 128.81500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 64.40750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 193.22250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 128.81500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 193.22250
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 64.40750
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 ZN ZN A 209 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 311 LIES ON A SPECIAL POSITION.
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 ASP A 51
REMARK 465 GLN A 52
REMARK 465 MET A 53
REMARK 465 LYS A 54
REMARK 465 ARG A 55
REMARK 465 LEU A 123
REMARK 465 THR A 124
REMARK 465 SER B 28
REMARK 465 GLN B 52
REMARK 465 MET B 53
REMARK 465 LYS B 54
REMARK 465 ARG B 55
REMARK 465 PRO B 56
REMARK 465 PRO B 57
REMARK 465 LEU B 123
REMARK 465 THR B 124
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 SER A 28 OG
REMARK 470 PHE A 29 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 30 CG CD CE NZ
REMARK 470 ASP A 31 CG OD1 OD2
REMARK 470 LYS A 47 CG CD CE NZ
REMARK 470 GLN A 49 CG CD OE1 NE2
REMARK 470 ARG A 50 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 114 CG CD OE1 NE2
REMARK 470 LYS A 121 CG CD CE NZ
REMARK 470 ARG A 122 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 29 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP B 31 CG OD1 OD2
REMARK 470 ARG B 43 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 47 CG CD CE NZ
REMARK 470 ARG B 50 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 51 CG OD1 OD2
REMARK 470 LEU B 58 CG CD1 CD2
REMARK 470 GLU B 59 CG CD OE1 OE2
REMARK 470 GLU B 60 CG CD OE1 OE2
REMARK 470 ARG B 62 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 75 CG CD CE NZ
REMARK 470 LYS B 77 CG CD CE NZ
REMARK 470 ARG B 122 CG CD NE CZ NH1 NH2
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 HE21 GLN A 40 OE2 GLU A 44 1.56
REMARK 500 O ASP B 31 O HOH B 301 2.02
REMARK 500 OE2 GLU A 44 O HOH A 301 2.10
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 ZN ZN A 208 HN3 IMD B 203 1545 1.37
REMARK 500 ZN ZN A 205 H2 IMD A 212 1565 1.52
REMARK 500 HZ1 LYS B 90 ZN ZN B 201 8555 1.53
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 PHE A 29 -59.81 44.97
REMARK 500 GLN A 49 52.88 -155.29
REMARK 500 ALA A 69 49.50 -95.28
REMARK 500 LYS B 30 79.10 -161.02
REMARK 500 ASP B 31 49.38 -81.37
REMARK 500 MET B 46 44.47 -78.10
REMARK 500 LYS B 47 -34.58 -138.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN B 49 ARG B 50 136.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 36 OD1
REMARK 620 2 ASP A 36 OD2 49.9
REMARK 620 3 GLU A 44 OE1 40.3 55.0
REMARK 620 4 HOH A 301 O 54.1 102.4 77.5
REMARK 620 5 GLU B 110 OE1 71.9 121.7 81.6 23.7
REMARK 620 6 GLU B 110 OE2 72.6 122.4 81.2 25.1 1.5
REMARK 620 7 HOH B 314 O 122.8 73.6 115.2 157.2 162.9 162.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 206 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 59 OE1
REMARK 620 2 GLU A 59 OE2 52.4
REMARK 620 3 ASP B 71 OD2 120.6 78.9
REMARK 620 4 HOH B 320 O 100.7 89.6 41.1
REMARK 620 5 HOH B 321 O 131.8 111.5 93.4 126.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 208 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 65 ND1
REMARK 620 2 GLU B 120 OE2 91.1
REMARK 620 3 IMD B 203 N3 107.0 127.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 202 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 66 OD1
REMARK 620 2 ASP A 66 OD2 55.5
REMARK 620 3 ASP B 66 OD1 49.5 53.5
REMARK 620 4 ASP B 66 OD2 48.3 50.5 3.0
REMARK 620 5 HOH B 302 O 92.6 74.4 43.2 44.4
REMARK 620 6 HOH B 316 O 89.4 90.2 134.8 132.4 159.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 203 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 71 OD2
REMARK 620 2 ASP A 74 OD2 100.0
REMARK 620 3 HOH A 330 O 122.6 59.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 204 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 86 OE1
REMARK 620 2 IMD A 213 N1 94.3
REMARK 620 3 GLU B 79 OE2 72.2 157.9
REMARK 620 4 HOH B 319 O 118.3 121.4 80.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 205 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 120 OE2
REMARK 620 2 IMD A 212 N1 131.3
REMARK 620 3 HIS B 65 ND1 94.7 98.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 74 OD2
REMARK 620 2 GLU B 87 OE2 82.7
REMARK 620 3 LYS B 90 NZ 85.7 7.2
REMARK 620 4 HOH B 322 O 95.1 136.4 142.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 208
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 209
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 213
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 214
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD B 203
DBREF 6OWY A 29 124 UNP P77754 SPY_ECOLI 52 147
DBREF 6OWY B 29 124 UNP P77754 SPY_ECOLI 52 147
SEQADV 6OWY SER A 28 UNP P77754 EXPRESSION TAG
SEQADV 6OWY LEU A 96 UNP P77754 HIS 119 ENGINEERED MUTATION
SEQADV 6OWY SER B 28 UNP P77754 EXPRESSION TAG
SEQADV 6OWY LEU B 96 UNP P77754 HIS 119 ENGINEERED MUTATION
SEQRES 1 A 97 SER PHE LYS ASP LEU ASN LEU THR ASP ALA GLN LYS GLN
SEQRES 2 A 97 GLN ILE ARG GLU ILE MET LYS GLY GLN ARG ASP GLN MET
SEQRES 3 A 97 LYS ARG PRO PRO LEU GLU GLU ARG ARG ALA MET HIS ASP
SEQRES 4 A 97 ILE ILE ALA SER ASP THR PHE ASP LYS VAL LYS ALA GLU
SEQRES 5 A 97 ALA GLN ILE ALA LYS MET GLU GLU GLN ARG LYS ALA ASN
SEQRES 6 A 97 MET LEU ALA LEU MET GLU THR GLN ASN LYS ILE TYR ASN
SEQRES 7 A 97 ILE LEU THR PRO GLU GLN LYS LYS GLN PHE ASN ALA ASN
SEQRES 8 A 97 PHE GLU LYS ARG LEU THR
SEQRES 1 B 97 SER PHE LYS ASP LEU ASN LEU THR ASP ALA GLN LYS GLN
SEQRES 2 B 97 GLN ILE ARG GLU ILE MET LYS GLY GLN ARG ASP GLN MET
SEQRES 3 B 97 LYS ARG PRO PRO LEU GLU GLU ARG ARG ALA MET HIS ASP
SEQRES 4 B 97 ILE ILE ALA SER ASP THR PHE ASP LYS VAL LYS ALA GLU
SEQRES 5 B 97 ALA GLN ILE ALA LYS MET GLU GLU GLN ARG LYS ALA ASN
SEQRES 6 B 97 MET LEU ALA LEU MET GLU THR GLN ASN LYS ILE TYR ASN
SEQRES 7 B 97 ILE LEU THR PRO GLU GLN LYS LYS GLN PHE ASN ALA ASN
SEQRES 8 B 97 PHE GLU LYS ARG LEU THR
HET ZN A 201 1
HET ZN A 202 1
HET ZN A 203 1
HET ZN A 204 1
HET ZN A 205 1
HET ZN A 206 1
HET ZN A 207 1
HET ZN A 208 1
HET ZN A 209 1
HET CL A 210 1
HET CL A 211 1
HET IMD A 212 10
HET IMD A 213 10
HET IOD A 214 1
HET ZN B 201 1
HET ZN B 202 1
HET IMD B 203 10
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM IMD IMIDAZOLE
HETNAM IOD IODIDE ION
FORMUL 3 ZN 11(ZN 2+)
FORMUL 12 CL 2(CL 1-)
FORMUL 14 IMD 3(C3 H5 N2 1+)
FORMUL 16 IOD I 1-
FORMUL 20 HOH *58(H2 O)
HELIX 1 AA1 THR A 35 GLY A 48 1 14
HELIX 2 AA2 PRO A 57 ALA A 69 1 13
HELIX 3 AA3 ASP A 74 MET A 85 1 12
HELIX 4 AA4 MET A 85 ASN A 105 1 21
HELIX 5 AA5 THR A 108 ARG A 122 1 15
HELIX 6 AA6 THR B 35 GLN B 49 1 15
HELIX 7 AA7 GLU B 59 ALA B 69 1 11
HELIX 8 AA8 ASP B 74 ASN B 105 1 32
HELIX 9 AA9 THR B 108 ARG B 122 1 15
LINK OD1 ASP A 36 ZN ZN A 201 1555 1555 2.63
LINK OD2 ASP A 36 ZN ZN A 201 1555 1555 2.51
LINK OE1 GLU A 44 ZN ZN A 201 1555 5655 1.96
LINK OE1 GLU A 59 ZN ZN A 206 1555 1555 2.62
LINK OE2 GLU A 59 ZN ZN A 206 1555 1555 2.32
LINK ND1 HIS A 65 ZN ZN A 208 1555 1555 2.13
LINK OD1 ASP A 66 ZN ZN A 202 1555 1555 2.09
LINK OD2 ASP A 66 ZN ZN A 202 1555 1555 2.55
LINK OD2 ASP A 71 ZN ZN A 203 1555 1555 1.93
LINK OD2 ASP A 74 ZN ZN A 203 1555 8445 2.03
LINK OE1 GLU A 86 ZN ZN A 204 1555 1555 2.03
LINK OE2 GLU A 120 ZN ZN A 205 1555 1555 1.73
LINK ZN ZN A 201 O HOH A 301 1555 5655 2.69
LINK ZN ZN A 201 OE1 GLU B 110 5545 1555 2.43
LINK ZN ZN A 201 OE2 GLU B 110 5545 1555 2.21
LINK ZN ZN A 201 O HOH B 314 1555 5565 2.23
LINK ZN ZN A 202 OD1 ASP B 66 1565 1555 2.38
LINK ZN ZN A 202 OD2 ASP B 66 1565 1555 2.12
LINK ZN ZN A 202 O HOH B 302 1555 1545 1.79
LINK ZN ZN A 202 O HOH B 316 1555 1545 2.20
LINK ZN ZN A 203 O HOH A 330 1555 8445 2.28
LINK ZN ZN A 204 N1 IMD A 213 1555 1555 2.33
LINK ZN ZN A 204 OE2 GLU B 79 8555 1555 1.91
LINK ZN ZN A 204 O HOH B 319 1555 8555 2.47
LINK ZN ZN A 205 N1 IMD A 212 1555 1565 2.30
LINK ZN ZN A 205 ND1 HIS B 65 1555 1555 2.16
LINK ZN ZN A 206 OD2 ASP B 71 1565 1555 2.09
LINK ZN ZN A 206 O HOH B 320 1555 1655 2.66
LINK ZN ZN A 206 O HOH B 321 1555 1545 2.38
LINK ZN ZN A 208 OE2 GLU B 120 1555 1555 1.92
LINK ZN ZN A 208 N3 IMD B 203 1555 1545 1.94
LINK OD2 ASP B 74 ZN ZN B 201 1555 1555 1.87
LINK OE2 GLU B 87 ZN ZN B 201 1555 8555 2.47
LINK NZ LYS B 90 ZN ZN B 201 1555 8555 2.19
LINK ZN ZN B 201 O HOH B 322 1555 1555 2.63
SITE 1 AC1 5 ASP A 36 GLU A 44 HOH A 301 GLU B 110
SITE 2 AC1 5 HOH B 314
SITE 1 AC2 6 ASP A 66 IMD A 212 ASP B 66 IMD B 203
SITE 2 AC2 6 HOH B 302 HOH B 316
SITE 1 AC3 4 ASP A 71 ASP A 74 LYS A 77 HOH A 330
SITE 1 AC4 4 GLU A 86 IMD A 213 GLU B 79 HOH B 319
SITE 1 AC5 4 GLU A 120 CL A 210 IMD A 212 HIS B 65
SITE 1 AC6 4 GLU A 59 ASP B 71 HOH B 320 HOH B 321
SITE 1 AC7 1 GLU A 98
SITE 1 AC8 4 HIS A 65 CL A 211 GLU B 120 IMD B 203
SITE 1 AC9 3 GLU A 87 LYS A 90 HOH A 322
SITE 1 AD1 5 PHE A 119 GLU A 120 ZN A 205 IMD A 212
SITE 2 AD1 5 ARG B 61
SITE 1 AD2 6 ARG A 62 HIS A 65 ZN A 208 PHE B 119
SITE 2 AD2 6 GLU B 120 IMD B 203
SITE 1 AD3 9 HIS A 65 ASP A 66 GLU A 120 ZN A 202
SITE 2 AD3 9 ZN A 205 CL A 210 HIS B 65 ASP B 66
SITE 3 AD3 9 IMD B 203
SITE 1 AD4 5 ALA A 83 GLU A 86 ZN A 204 VAL B 76
SITE 2 AD4 5 GLU B 79
SITE 1 AD5 1 GLN A 100
SITE 1 AD6 4 ASP B 74 GLU B 87 LYS B 90 HOH B 322
SITE 1 AD7 1 GLU B 98
SITE 1 AD8 10 ARG A 62 HIS A 65 ZN A 202 ZN A 208
SITE 2 AD8 10 CL A 211 IMD A 212 HIS B 65 ASP B 66
SITE 3 AD8 10 GLU B 120 HOH B 302
CRYST1 42.840 42.840 257.630 90.00 90.00 90.00 P 41 2 2 16
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 0.023343 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023343 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003882 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
