HEADER CHAPERONE 12-MAY-19 6OWZ
TITLE SPY H96L:IM7 L19PI-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 6OWZ 1 LINK
REVDAT 5 11-DEC-19 6OWZ 1 JRNL
REVDAT 4 20-NOV-19 6OWZ 1 REMARK
REVDAT 3 09-OCT-19 6OWZ 1 REMARK LINK SITE CRYST1
REVDAT 3 2 1 ATOM
REVDAT 2 05-JUN-19 6OWZ 1 AUTHOR JRNL
REVDAT 1 29-MAY-19 6OWZ 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. 2.05 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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.02
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.910
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 28898
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1746
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 42.4300 - 4.6900 1.00 2257 148 0.2077 0.2691
REMARK 3 2 4.6900 - 3.7200 1.00 2288 147 0.1718 0.1658
REMARK 3 3 3.7200 - 3.2500 1.00 2265 145 0.2134 0.2593
REMARK 3 4 3.2500 - 2.9600 1.00 2272 148 0.2424 0.2748
REMARK 3 5 2.9600 - 2.7400 1.00 2244 142 0.2357 0.3516
REMARK 3 6 2.7400 - 2.5800 1.00 2270 148 0.2547 0.3218
REMARK 3 7 2.5800 - 2.4500 1.00 2282 145 0.2358 0.2927
REMARK 3 8 2.4500 - 2.3500 1.00 2227 138 0.2246 0.3298
REMARK 3 9 2.3500 - 2.2600 1.00 2263 148 0.2332 0.2513
REMARK 3 10 2.2600 - 2.1800 1.00 2272 147 0.2351 0.2592
REMARK 3 11 2.1800 - 2.1100 1.00 2277 144 0.2567 0.2963
REMARK 3 12 2.1100 - 2.0500 1.00 2235 146 0.2851 0.2981
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) : 0.294
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.046
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 46.91
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.61
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 : 0.015 1411
REMARK 3 ANGLE : 1.203 1886
REMARK 3 CHIRALITY : 0.050 209
REMARK 3 PLANARITY : 0.007 253
REMARK 3 DIHEDRAL : 17.983 554
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 6OWZ 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_1000241498.
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, 4.5085, 4.3200
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 : 17581
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 43.020
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
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 128.57500
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 64.28750
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 192.86250
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 128.57500
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 192.86250
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 64.28750
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: 2970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 HOH A 328 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 SER A 28
REMARK 465 GLY A 48
REMARK 465 GLN A 49
REMARK 465 ARG A 50
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 PRO A 56
REMARK 465 LEU A 123
REMARK 465 THR A 124
REMARK 465 SER B 28
REMARK 465 PHE B 29
REMARK 465 ASP B 51
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 58
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 PHE A 29 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 30 CG CD CE NZ
REMARK 470 LYS A 121 CG CD CE NZ
REMARK 470 ARG A 122 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 30 CG CD CE NZ
REMARK 470 GLN B 40 CG CD OE1 NE2
REMARK 470 ARG B 43 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 47 CG CD CE NZ
REMARK 470 GLN B 49 CG CD OE1 NE2
REMARK 470 ARG B 50 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 59 CG CD OE1 OE2
REMARK 470 GLU B 60 CG CD OE1 OE2
REMARK 470 LYS B 121 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 ZN ZN A 207 HN3 IMD B 203 1.44
REMARK 500 ZN ZN A 206 HN1 IMD A 213 1.49
REMARK 500 ZN ZN A 205 H4 IMD A 212 1.55
REMARK 500 OE2 GLU A 120 ZN ZN A 206 1.61
REMARK 500 OE2 GLU A 44 O HOH A 301 1.97
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 HZ1 LYS B 90 ZN ZN B 201 8555 1.02
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 ASP A 31 170.66 -56.12
REMARK 500 MET A 46 14.97 -65.46
REMARK 500 ALA A 69 49.45 -90.32
REMARK 500 ASP B 31 49.19 -98.03
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 ASP A 31 LEU A 32 -148.44
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 OD2
REMARK 620 2 GLU A 44 OE1 55.3
REMARK 620 3 HOH A 301 O 53.3 10.2
REMARK 620 4 HOH A 329 O 44.3 11.5 15.4
REMARK 620 5 GLU B 110 OE1 118.6 81.8 90.8 87.3
REMARK 620 6 GLU B 110 OE2 118.9 81.0 89.9 86.8 1.5
REMARK 620 N 1 2 3 4 5
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 GLU A 59 OE2
REMARK 620 2 ASP B 71 OD2 103.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 207 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 65 ND1
REMARK 620 2 GLU B 120 OE2 90.8
REMARK 620 3 IMD B 203 N3 100.8 128.7
REMARK 620 N 1 2
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 66 OD1
REMARK 620 2 ASP A 66 OD2 55.7
REMARK 620 3 HOH A 324 O 97.9 83.4
REMARK 620 4 HOH A 327 O 90.1 87.6 161.6
REMARK 620 5 ASP B 66 OD1 56.9 63.8 41.1 144.4
REMARK 620 6 ASP B 66 OD2 55.2 60.9 42.7 141.8 2.9
REMARK 620 N 1 2 3 4 5
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 ASP A 71 OD2
REMARK 620 2 ASP A 74 OD2 99.3
REMARK 620 3 HOH A 333 O 115.6 16.8
REMARK 620 N 1 2
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 86 OE1
REMARK 620 2 HOH A 326 O 105.9
REMARK 620 3 GLU B 79 OE2 71.9 78.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 209 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 87 OE1
REMARK 620 2 GLU A 87 OE2 50.0
REMARK 620 3 GLU A 87 OE1 0.0 50.0
REMARK 620 4 GLU A 87 OE2 50.0 0.0 50.0
REMARK 620 5 HOH A 328 O 96.9 144.6 96.9 144.6
REMARK 620 6 HOH A 328 O 96.9 144.6 96.9 144.6 0.0
REMARK 620 N 1 2 3 4 5
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 IMD A 213 N1
REMARK 620 2 HIS B 65 ND1 97.6
REMARK 620 N 1
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 85.9
REMARK 620 3 LYS B 90 NZ 87.0 6.5
REMARK 620 4 HOH B 312 O 95.3 141.1 147.4
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 IOD A 215
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 205
DBREF 6OWZ A 29 124 UNP P77754 SPY_ECOLI 52 147
DBREF 6OWZ B 29 124 UNP P77754 SPY_ECOLI 52 147
SEQADV 6OWZ SER A 28 UNP P77754 EXPRESSION TAG
SEQADV 6OWZ LEU A 96 UNP P77754 HIS 119 ENGINEERED MUTATION
SEQADV 6OWZ SER B 28 UNP P77754 EXPRESSION TAG
SEQADV 6OWZ 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 IOD A 215 1
HET ZN B 201 1
HET ZN B 202 1
HET IMD B 203 10
HET IOD B 204 1
HET IOD B 205 1
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 4(I 1-)
FORMUL 23 HOH *62(H2 O)
HELIX 1 AA1 THR A 35 MET A 46 1 12
HELIX 2 AA2 LEU A 58 ALA A 69 1 12
HELIX 3 AA3 ASP A 74 MET A 85 1 12
HELIX 4 AA4 MET A 85 ILE A 106 1 22
HELIX 5 AA5 THR A 108 LYS A 121 1 14
HELIX 6 AA6 THR B 35 GLY B 48 1 14
HELIX 7 AA7 GLU B 60 ALA B 69 1 10
HELIX 8 AA8 ASP B 74 ILE B 106 1 33
HELIX 9 AA9 THR B 108 ARG B 122 1 15
LINK OD2 ASP A 36 ZN ZN A 201 1555 5655 2.39
LINK OE1 GLU A 44 ZN ZN A 201 1555 1555 2.01
LINK OE2 GLU A 59 ZN ZN A 202 1555 1555 1.71
LINK ND1 HIS A 65 ZN ZN A 207 1555 1555 2.03
LINK OD1 ASP A 66 ZN ZN A 203 1555 1555 2.05
LINK OD2 ASP A 66 ZN ZN A 203 1555 1555 2.57
LINK OD2 ASP A 71 ZN ZN A 204 1555 8445 1.94
LINK OD2 ASP A 74 ZN ZN A 204 1555 1555 1.99
LINK OE1 GLU A 86 ZN ZN A 205 1555 1555 1.93
LINK OE1 GLU A 87 ZN ZN A 209 1555 1555 2.66
LINK OE2 GLU A 87 ZN ZN A 209 1555 1555 2.53
LINK OE1 GLU A 87 ZN ZN A 209 1555 8555 2.42
LINK OE2 GLU A 87 ZN ZN A 209 1555 8555 2.55
LINK OE2 GLU A 98 ZN ZN A 208 1555 1555 2.70
LINK ZN ZN A 201 O HOH A 301 1555 1555 2.33
LINK ZN ZN A 201 O HOH A 329 1555 1555 1.96
LINK ZN ZN A 201 OE1 GLU B 110 1445 1555 2.01
LINK ZN ZN A 201 OE2 GLU B 110 1445 1555 2.31
LINK ZN ZN A 202 OD2 ASP B 71 1565 1555 1.94
LINK ZN ZN A 203 O HOH A 324 1555 1555 1.88
LINK ZN ZN A 203 O HOH A 327 1555 1555 2.23
LINK ZN ZN A 203 OD1 ASP B 66 1565 1555 2.38
LINK ZN ZN A 203 OD2 ASP B 66 1565 1555 1.99
LINK ZN ZN A 204 O HOH A 333 1555 1555 2.08
LINK ZN ZN A 205 O HOH A 326 1555 1555 1.82
LINK ZN ZN A 205 OE2 GLU B 79 8555 1555 1.80
LINK ZN ZN A 206 N1 IMD A 213 1555 1555 2.00
LINK ZN ZN A 206 ND1 HIS B 65 1555 1555 2.01
LINK ZN ZN A 207 OE2 GLU B 120 1555 1555 1.91
LINK ZN ZN A 207 N3 IMD B 203 1555 1555 1.94
LINK ZN ZN A 209 O HOH A 328 1555 1555 2.02
LINK ZN ZN A 209 O HOH A 328 1555 8555 2.02
LINK OD2 ASP B 74 ZN ZN B 201 1555 1555 1.95
LINK OE2AGLU B 87 ZN ZN B 201 1555 8555 1.84
LINK NZ LYS B 90 ZN ZN B 201 1555 8555 1.89
LINK ZN ZN B 201 O HOH B 312 1555 1555 2.07
SITE 1 AC1 5 ASP A 36 GLU A 44 HOH A 301 HOH A 329
SITE 2 AC1 5 GLU B 110
SITE 1 AC2 3 GLU A 59 HOH A 340 ASP B 71
SITE 1 AC3 6 ASP A 66 IMD A 213 HOH A 324 HOH A 327
SITE 2 AC3 6 ASP B 66 IMD B 203
SITE 1 AC4 4 ASP A 71 ASP A 74 HOH A 333 HOH A 343
SITE 1 AC5 4 GLU A 86 IMD A 212 HOH A 326 GLU B 79
SITE 1 AC6 4 GLU A 120 CL A 210 IMD A 213 HIS B 65
SITE 1 AC7 4 HIS A 65 CL A 211 GLU B 120 IMD B 203
SITE 1 AC8 1 GLU A 98
SITE 1 AC9 2 GLU A 87 HOH A 328
SITE 1 AD1 6 PHE A 119 GLU A 120 ZN A 206 IMD A 213
SITE 2 AD1 6 ARG B 61 HIS B 65
SITE 1 AD2 6 ARG A 61 HIS A 65 ZN A 207 PHE B 119
SITE 2 AD2 6 GLU B 120 IMD B 203
SITE 1 AD3 7 ALA A 83 GLU A 86 ZN A 205 HOH A 326
SITE 2 AD3 7 LYS B 75 VAL B 76 GLU B 79
SITE 1 AD4 9 HIS A 65 ASP A 66 GLU A 120 ZN A 203
SITE 2 AD4 9 ZN A 206 CL A 210 ARG B 62 HIS B 65
SITE 3 AD4 9 IMD B 203
SITE 1 AD5 2 GLN A 100 PHE A 115
SITE 1 AD6 2 MET A 46 THR A 99
SITE 1 AD7 4 ASP B 74 GLU B 87 LYS B 90 HOH B 312
SITE 1 AD8 1 GLU B 98
SITE 1 AD9 10 ARG A 62 HIS A 65 ZN A 203 ZN A 207
SITE 2 AD9 10 CL A 211 IMD A 213 HOH A 324 HIS B 65
SITE 3 AD9 10 ASP B 66 GLU B 120
SITE 1 AE1 1 PHE B 115
SITE 1 AE2 1 PHE B 115
CRYST1 43.020 43.020 257.150 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 0.023245 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023245 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003889 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
