HEADER METAL TRANSPORT 07-JUL-08 3DP8
TITLE STRUCTURAL CHARACTERIZATION OF A PUTATIVE ENDOGENOUS METAL CHELATOR IN
TITLE 2 THE PERIPLASMIC NICKEL TRANSPORTER NIKA (NICKEL BUTANE-1,2,4-
TITLE 3 TRICARBOXYLATE FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NICKEL-BINDING PERIPLASMIC PROTEIN;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: NIKA;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: NIKA, B3476, JW3441;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS NICKEL, NICKELLOPHORE, BUTANE-1, 2, 4-TRICARBOXYLATE, TRANSPORT,
KEYWDS 2 METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR M.V.CHERRIER,C.CAVAZZA,C.BOCHOT,D.LEMAIRE,J.C.FONTECILLA-CAMPS
REVDAT 5 01-NOV-23 3DP8 1 REMARK LINK
REVDAT 4 13-JUL-11 3DP8 1 VERSN
REVDAT 3 24-FEB-09 3DP8 1 VERSN
REVDAT 2 30-SEP-08 3DP8 1 JRNL
REVDAT 1 16-SEP-08 3DP8 0
JRNL AUTH M.V.CHERRIER,C.CAVAZZA,C.BOCHOT,D.LEMAIRE,
JRNL AUTH 2 J.C.FONTECILLA-CAMPS
JRNL TITL STRUCTURAL CHARACTERIZATION OF A PUTATIVE ENDOGENOUS METAL
JRNL TITL 2 CHELATOR IN THE PERIPLASMIC NICKEL TRANSPORTER NIKA
JRNL REF BIOCHEMISTRY V. 47 9937 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18759453
JRNL DOI 10.1021/BI801051Y
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 64541
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.600
REMARK 3 FREE R VALUE TEST SET COUNT : 1707
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4754
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2980
REMARK 3 BIN FREE R VALUE SET COUNT : 143
REMARK 3 BIN FREE R VALUE : 0.4180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11824
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 146
REMARK 3 SOLVENT ATOMS : 265
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.51000
REMARK 3 B22 (A**2) : 0.51000
REMARK 3 B33 (A**2) : -0.77000
REMARK 3 B12 (A**2) : 0.26000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.466
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.300
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.231
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.210
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12540 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17112 ; 1.963 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1571 ; 7.946 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 596 ;40.225 ;24.832
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2089 ;20.330 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 66 ;22.800 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1865 ; 0.136 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9729 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5984 ; 0.252 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 8292 ; 0.323 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 558 ; 0.167 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 51 ; 0.294 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.157 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 7886 ; 0.955 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12415 ; 1.644 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5370 ; 2.408 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4655 ; 3.714 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3DP8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-JUL-08.
REMARK 100 THE DEPOSITION ID IS D_1000048318.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9330
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64541
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.32600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.400
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: PDB ENTRY 1ZLQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M AMMONIUM SULFATE, 100MM SODIUM
REMARK 280 ACETATE, PH4.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
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 89.96000
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 44.98000
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 0.00000
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 89.96000
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 44.98000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 350
REMARK 350 BIOMOLECULE: 3
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: C
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 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 ALA A 1
REMARK 465 VAL A 500
REMARK 465 LYS A 501
REMARK 465 PRO A 502
REMARK 465 ALA B 1
REMARK 465 ALA B 2
REMARK 465 SER B 308
REMARK 465 LYS B 501
REMARK 465 PRO B 502
REMARK 465 ALA C 1
REMARK 465 ALA C 2
REMARK 465 PRO C 3
REMARK 465 VAL C 500
REMARK 465 LYS C 501
REMARK 465 PRO C 502
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 TYR A 382 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 386 CB CG CD NE CZ NH1 NH2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN B 309 CA CB CG 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 NH2 ARG B 95 O ILE B 107 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLN B 309 N GLN B 309 CA -0.361
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 PRO A 3 C - N - CA ANGL. DEV. = -9.2 DEGREES
REMARK 500 PHE A 73 N - CA - C ANGL. DEV. = -20.3 DEGREES
REMARK 500 ARG A 231 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 452 CG - CD - NE ANGL. DEV. = -14.3 DEGREES
REMARK 500 ARG A 452 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ASP B 4 N - CA - C ANGL. DEV. = 19.8 DEGREES
REMARK 500 LEU B 224 CA - CB - CG ANGL. DEV. = 20.8 DEGREES
REMARK 500 GLN B 309 N - CA - CB ANGL. DEV. = -38.0 DEGREES
REMARK 500 GLN B 309 N - CA - C ANGL. DEV. = 33.5 DEGREES
REMARK 500 LEU C 303 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 PRO C 499 C - N - CA ANGL. DEV. = 9.1 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 TYR A 22 -128.74 -114.36
REMARK 500 TRP A 49 -110.21 -127.43
REMARK 500 SER A 74 -72.13 91.13
REMARK 500 ALA A 81 -33.68 -37.70
REMARK 500 LEU A 113 -93.80 -73.36
REMARK 500 PRO A 128 22.12 -77.36
REMARK 500 ARG A 137 136.77 -174.97
REMARK 500 PHE A 139 54.42 -98.63
REMARK 500 SER A 145 -3.83 -53.91
REMARK 500 ASN A 149 -122.45 66.62
REMARK 500 LYS A 157 -72.29 -90.44
REMARK 500 PRO A 159 64.15 -65.14
REMARK 500 GLN A 174 -44.69 -131.72
REMARK 500 ASN A 183 49.33 -103.53
REMARK 500 ASN A 281 -83.55 -81.93
REMARK 500 TYR A 300 -2.65 68.23
REMARK 500 ASP A 311 78.36 -152.46
REMARK 500 ALA A 328 122.98 -36.51
REMARK 500 PHE A 346 148.64 -179.58
REMARK 500 ILE A 347 99.63 -53.52
REMARK 500 ARG A 389 68.62 -110.25
REMARK 500 HIS A 416 -145.41 -149.94
REMARK 500 ASP B 4 -24.72 83.94
REMARK 500 TYR B 22 -147.09 -106.82
REMARK 500 ASP B 43 6.90 -66.34
REMARK 500 TRP B 49 -104.71 -142.62
REMARK 500 SER B 114 -140.05 -115.24
REMARK 500 PRO B 128 3.18 -67.70
REMARK 500 PHE B 139 48.76 -85.75
REMARK 500 LYS B 157 -92.78 -92.18
REMARK 500 PRO B 159 67.68 -62.95
REMARK 500 ASN B 173 9.68 53.69
REMARK 500 GLN B 174 -57.23 -125.08
REMARK 500 LEU B 216 123.46 -173.94
REMARK 500 ALA B 282 -28.64 -153.56
REMARK 500 TYR B 284 -2.44 74.62
REMARK 500 THR B 286 -83.96 83.57
REMARK 500 ASP B 311 86.44 -159.65
REMARK 500 ALA B 322 14.18 -68.67
REMARK 500 ALA B 328 114.57 -39.63
REMARK 500 LEU B 340 90.23 -62.05
REMARK 500 SER B 415 -90.30 -146.37
REMARK 500 HIS B 416 -152.86 -101.41
REMARK 500 LEU C 17 30.67 89.16
REMARK 500 TYR C 22 -133.93 -112.61
REMARK 500 TRP C 49 -116.90 -134.44
REMARK 500 SER C 57 -158.68 -75.36
REMARK 500 ASP C 59 -48.83 179.21
REMARK 500 LEU C 67 -173.66 -44.40
REMARK 500 ARG C 68 -167.42 74.66
REMARK 500
REMARK 500 THIS ENTRY HAS 66 RAMACHANDRAN OUTLIERS.
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 PHE A 73 SER A 74 45.06
REMARK 500 LEU A 172 ASN A 173 -36.71
REMARK 500 SER A 415 HIS A 416 104.30
REMARK 500 PRO B 3 ASP B 4 -47.51
REMARK 500 ASP B 215 LEU B 216 -149.90
REMARK 500 GLU C 58 ASP C 59 -31.36
REMARK 500 ASP C 59 GLY C 60 -39.13
REMARK 500 LEU C 67 ARG C 68 53.26
REMARK 500 ARG C 68 ASP C 69 40.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLN B 309 13.62
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 NI B 503 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 416 NE2
REMARK 620 2 HCT B 511 O6 174.6
REMARK 620 3 HCT B 511 O3 100.0 84.5
REMARK 620 4 HCT B 511 O1 88.5 87.4 167.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI C 503 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 416 NE2
REMARK 620 2 HCT C 509 O6 170.8
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HCT B 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HCT A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HCT C 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 515
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZLQ RELATED DB: PDB
REMARK 900 NIKA - FEEDTA
REMARK 900 RELATED ID: 1UIU RELATED DB: PDB
REMARK 900 NIKA - NICKEL UNLIGANDED FORM
REMARK 900 RELATED ID: 1UIV RELATED DB: PDB
REMARK 900 NIKA - NICKEL LIGANDED FORM
REMARK 900 RELATED ID: 2NOO RELATED DB: PDB
REMARK 900 NIKA MUTANT
DBREF 3DP8 A 1 502 UNP P33590 NIKA_ECOLI 23 524
DBREF 3DP8 B 1 502 UNP P33590 NIKA_ECOLI 23 524
DBREF 3DP8 C 1 502 UNP P33590 NIKA_ECOLI 23 524
SEQRES 1 A 502 ALA ALA PRO ASP GLU ILE THR THR ALA TRP PRO VAL ASN
SEQRES 2 A 502 VAL GLY PRO LEU ASN PRO HIS LEU TYR THR PRO ASN GLN
SEQRES 3 A 502 MET PHE ALA GLN SER MET VAL TYR GLU PRO LEU VAL LYS
SEQRES 4 A 502 TYR GLN ALA ASP GLY SER VAL ILE PRO TRP LEU ALA LYS
SEQRES 5 A 502 SER TRP THR HIS SER GLU ASP GLY LYS THR TRP THR PHE
SEQRES 6 A 502 THR LEU ARG ASP ASP VAL LYS PHE SER ASN GLY GLU PRO
SEQRES 7 A 502 PHE ASP ALA GLU ALA ALA ALA GLU ASN PHE ARG ALA VAL
SEQRES 8 A 502 LEU ASP ASN ARG GLN ARG HIS ALA TRP LEU GLU LEU ALA
SEQRES 9 A 502 ASN GLN ILE VAL ASP VAL LYS ALA LEU SER LYS THR GLU
SEQRES 10 A 502 LEU GLN ILE THR LEU LYS SER ALA TYR TYR PRO PHE LEU
SEQRES 11 A 502 GLN GLU LEU ALA LEU PRO ARG PRO PHE ARG PHE ILE ALA
SEQRES 12 A 502 PRO SER GLN PHE LYS ASN HIS GLU THR MET ASN GLY ILE
SEQRES 13 A 502 LYS ALA PRO ILE GLY THR GLY PRO TRP ILE LEU GLN GLU
SEQRES 14 A 502 SER LYS LEU ASN GLN TYR ASP VAL PHE VAL ARG ASN GLU
SEQRES 15 A 502 ASN TYR TRP GLY GLU LYS PRO ALA ILE LYS LYS ILE THR
SEQRES 16 A 502 PHE ASN VAL ILE PRO ASP PRO THR THR ARG ALA VAL ALA
SEQRES 17 A 502 PHE GLU THR GLY ASP ILE ASP LEU LEU TYR GLY ASN GLU
SEQRES 18 A 502 GLY LEU LEU PRO LEU ASP THR PHE ALA ARG PHE SER GLN
SEQRES 19 A 502 ASN PRO ALA TYR HIS THR GLN LEU SER GLN PRO ILE GLU
SEQRES 20 A 502 THR VAL MET LEU ALA LEU ASN THR ALA LYS ALA PRO THR
SEQRES 21 A 502 ASN GLU LEU ALA VAL ARG GLU ALA LEU ASN TYR ALA VAL
SEQRES 22 A 502 ASN LYS LYS SER LEU ILE ASP ASN ALA LEU TYR GLY THR
SEQRES 23 A 502 GLN GLN VAL ALA ASP THR LEU PHE ALA PRO SER VAL PRO
SEQRES 24 A 502 TYR ALA ASN LEU GLY LEU LYS PRO SER GLN TYR ASP PRO
SEQRES 25 A 502 GLN LYS ALA LYS ALA LEU LEU GLU LYS ALA GLY TRP THR
SEQRES 26 A 502 LEU PRO ALA GLY LYS ASP ILE ARG GLU LYS ASN GLY GLN
SEQRES 27 A 502 PRO LEU ARG ILE GLU LEU SER PHE ILE GLY THR ASP ALA
SEQRES 28 A 502 LEU SER LYS SER MET ALA GLU ILE ILE GLN ALA ASP MET
SEQRES 29 A 502 ARG GLN ILE GLY ALA ASP VAL SER LEU ILE GLY GLU GLU
SEQRES 30 A 502 GLU SER SER ILE TYR ALA ARG GLN ARG ASP GLY ARG PHE
SEQRES 31 A 502 GLY MET ILE PHE HIS ARG THR TRP GLY ALA PRO TYR ASP
SEQRES 32 A 502 PRO HIS ALA PHE LEU SER SER MET ARG VAL PRO SER HIS
SEQRES 33 A 502 ALA ASP PHE GLN ALA GLN GLN GLY LEU ALA ASP LYS PRO
SEQRES 34 A 502 LEU ILE ASP LYS GLU ILE GLY GLU VAL LEU ALA THR HIS
SEQRES 35 A 502 ASP GLU THR GLN ARG GLN ALA LEU TYR ARG ASP ILE LEU
SEQRES 36 A 502 THR ARG LEU HIS ASP GLU ALA VAL TYR LEU PRO ILE SER
SEQRES 37 A 502 TYR ILE SER MET MET VAL VAL SER LYS PRO GLU LEU GLY
SEQRES 38 A 502 ASN ILE PRO TYR ALA PRO ILE ALA THR GLU ILE PRO PHE
SEQRES 39 A 502 GLU GLN ILE LYS PRO VAL LYS PRO
SEQRES 1 B 502 ALA ALA PRO ASP GLU ILE THR THR ALA TRP PRO VAL ASN
SEQRES 2 B 502 VAL GLY PRO LEU ASN PRO HIS LEU TYR THR PRO ASN GLN
SEQRES 3 B 502 MET PHE ALA GLN SER MET VAL TYR GLU PRO LEU VAL LYS
SEQRES 4 B 502 TYR GLN ALA ASP GLY SER VAL ILE PRO TRP LEU ALA LYS
SEQRES 5 B 502 SER TRP THR HIS SER GLU ASP GLY LYS THR TRP THR PHE
SEQRES 6 B 502 THR LEU ARG ASP ASP VAL LYS PHE SER ASN GLY GLU PRO
SEQRES 7 B 502 PHE ASP ALA GLU ALA ALA ALA GLU ASN PHE ARG ALA VAL
SEQRES 8 B 502 LEU ASP ASN ARG GLN ARG HIS ALA TRP LEU GLU LEU ALA
SEQRES 9 B 502 ASN GLN ILE VAL ASP VAL LYS ALA LEU SER LYS THR GLU
SEQRES 10 B 502 LEU GLN ILE THR LEU LYS SER ALA TYR TYR PRO PHE LEU
SEQRES 11 B 502 GLN GLU LEU ALA LEU PRO ARG PRO PHE ARG PHE ILE ALA
SEQRES 12 B 502 PRO SER GLN PHE LYS ASN HIS GLU THR MET ASN GLY ILE
SEQRES 13 B 502 LYS ALA PRO ILE GLY THR GLY PRO TRP ILE LEU GLN GLU
SEQRES 14 B 502 SER LYS LEU ASN GLN TYR ASP VAL PHE VAL ARG ASN GLU
SEQRES 15 B 502 ASN TYR TRP GLY GLU LYS PRO ALA ILE LYS LYS ILE THR
SEQRES 16 B 502 PHE ASN VAL ILE PRO ASP PRO THR THR ARG ALA VAL ALA
SEQRES 17 B 502 PHE GLU THR GLY ASP ILE ASP LEU LEU TYR GLY ASN GLU
SEQRES 18 B 502 GLY LEU LEU PRO LEU ASP THR PHE ALA ARG PHE SER GLN
SEQRES 19 B 502 ASN PRO ALA TYR HIS THR GLN LEU SER GLN PRO ILE GLU
SEQRES 20 B 502 THR VAL MET LEU ALA LEU ASN THR ALA LYS ALA PRO THR
SEQRES 21 B 502 ASN GLU LEU ALA VAL ARG GLU ALA LEU ASN TYR ALA VAL
SEQRES 22 B 502 ASN LYS LYS SER LEU ILE ASP ASN ALA LEU TYR GLY THR
SEQRES 23 B 502 GLN GLN VAL ALA ASP THR LEU PHE ALA PRO SER VAL PRO
SEQRES 24 B 502 TYR ALA ASN LEU GLY LEU LYS PRO SER GLN TYR ASP PRO
SEQRES 25 B 502 GLN LYS ALA LYS ALA LEU LEU GLU LYS ALA GLY TRP THR
SEQRES 26 B 502 LEU PRO ALA GLY LYS ASP ILE ARG GLU LYS ASN GLY GLN
SEQRES 27 B 502 PRO LEU ARG ILE GLU LEU SER PHE ILE GLY THR ASP ALA
SEQRES 28 B 502 LEU SER LYS SER MET ALA GLU ILE ILE GLN ALA ASP MET
SEQRES 29 B 502 ARG GLN ILE GLY ALA ASP VAL SER LEU ILE GLY GLU GLU
SEQRES 30 B 502 GLU SER SER ILE TYR ALA ARG GLN ARG ASP GLY ARG PHE
SEQRES 31 B 502 GLY MET ILE PHE HIS ARG THR TRP GLY ALA PRO TYR ASP
SEQRES 32 B 502 PRO HIS ALA PHE LEU SER SER MET ARG VAL PRO SER HIS
SEQRES 33 B 502 ALA ASP PHE GLN ALA GLN GLN GLY LEU ALA ASP LYS PRO
SEQRES 34 B 502 LEU ILE ASP LYS GLU ILE GLY GLU VAL LEU ALA THR HIS
SEQRES 35 B 502 ASP GLU THR GLN ARG GLN ALA LEU TYR ARG ASP ILE LEU
SEQRES 36 B 502 THR ARG LEU HIS ASP GLU ALA VAL TYR LEU PRO ILE SER
SEQRES 37 B 502 TYR ILE SER MET MET VAL VAL SER LYS PRO GLU LEU GLY
SEQRES 38 B 502 ASN ILE PRO TYR ALA PRO ILE ALA THR GLU ILE PRO PHE
SEQRES 39 B 502 GLU GLN ILE LYS PRO VAL LYS PRO
SEQRES 1 C 502 ALA ALA PRO ASP GLU ILE THR THR ALA TRP PRO VAL ASN
SEQRES 2 C 502 VAL GLY PRO LEU ASN PRO HIS LEU TYR THR PRO ASN GLN
SEQRES 3 C 502 MET PHE ALA GLN SER MET VAL TYR GLU PRO LEU VAL LYS
SEQRES 4 C 502 TYR GLN ALA ASP GLY SER VAL ILE PRO TRP LEU ALA LYS
SEQRES 5 C 502 SER TRP THR HIS SER GLU ASP GLY LYS THR TRP THR PHE
SEQRES 6 C 502 THR LEU ARG ASP ASP VAL LYS PHE SER ASN GLY GLU PRO
SEQRES 7 C 502 PHE ASP ALA GLU ALA ALA ALA GLU ASN PHE ARG ALA VAL
SEQRES 8 C 502 LEU ASP ASN ARG GLN ARG HIS ALA TRP LEU GLU LEU ALA
SEQRES 9 C 502 ASN GLN ILE VAL ASP VAL LYS ALA LEU SER LYS THR GLU
SEQRES 10 C 502 LEU GLN ILE THR LEU LYS SER ALA TYR TYR PRO PHE LEU
SEQRES 11 C 502 GLN GLU LEU ALA LEU PRO ARG PRO PHE ARG PHE ILE ALA
SEQRES 12 C 502 PRO SER GLN PHE LYS ASN HIS GLU THR MET ASN GLY ILE
SEQRES 13 C 502 LYS ALA PRO ILE GLY THR GLY PRO TRP ILE LEU GLN GLU
SEQRES 14 C 502 SER LYS LEU ASN GLN TYR ASP VAL PHE VAL ARG ASN GLU
SEQRES 15 C 502 ASN TYR TRP GLY GLU LYS PRO ALA ILE LYS LYS ILE THR
SEQRES 16 C 502 PHE ASN VAL ILE PRO ASP PRO THR THR ARG ALA VAL ALA
SEQRES 17 C 502 PHE GLU THR GLY ASP ILE ASP LEU LEU TYR GLY ASN GLU
SEQRES 18 C 502 GLY LEU LEU PRO LEU ASP THR PHE ALA ARG PHE SER GLN
SEQRES 19 C 502 ASN PRO ALA TYR HIS THR GLN LEU SER GLN PRO ILE GLU
SEQRES 20 C 502 THR VAL MET LEU ALA LEU ASN THR ALA LYS ALA PRO THR
SEQRES 21 C 502 ASN GLU LEU ALA VAL ARG GLU ALA LEU ASN TYR ALA VAL
SEQRES 22 C 502 ASN LYS LYS SER LEU ILE ASP ASN ALA LEU TYR GLY THR
SEQRES 23 C 502 GLN GLN VAL ALA ASP THR LEU PHE ALA PRO SER VAL PRO
SEQRES 24 C 502 TYR ALA ASN LEU GLY LEU LYS PRO SER GLN TYR ASP PRO
SEQRES 25 C 502 GLN LYS ALA LYS ALA LEU LEU GLU LYS ALA GLY TRP THR
SEQRES 26 C 502 LEU PRO ALA GLY LYS ASP ILE ARG GLU LYS ASN GLY GLN
SEQRES 27 C 502 PRO LEU ARG ILE GLU LEU SER PHE ILE GLY THR ASP ALA
SEQRES 28 C 502 LEU SER LYS SER MET ALA GLU ILE ILE GLN ALA ASP MET
SEQRES 29 C 502 ARG GLN ILE GLY ALA ASP VAL SER LEU ILE GLY GLU GLU
SEQRES 30 C 502 GLU SER SER ILE TYR ALA ARG GLN ARG ASP GLY ARG PHE
SEQRES 31 C 502 GLY MET ILE PHE HIS ARG THR TRP GLY ALA PRO TYR ASP
SEQRES 32 C 502 PRO HIS ALA PHE LEU SER SER MET ARG VAL PRO SER HIS
SEQRES 33 C 502 ALA ASP PHE GLN ALA GLN GLN GLY LEU ALA ASP LYS PRO
SEQRES 34 C 502 LEU ILE ASP LYS GLU ILE GLY GLU VAL LEU ALA THR HIS
SEQRES 35 C 502 ASP GLU THR GLN ARG GLN ALA LEU TYR ARG ASP ILE LEU
SEQRES 36 C 502 THR ARG LEU HIS ASP GLU ALA VAL TYR LEU PRO ILE SER
SEQRES 37 C 502 TYR ILE SER MET MET VAL VAL SER LYS PRO GLU LEU GLY
SEQRES 38 C 502 ASN ILE PRO TYR ALA PRO ILE ALA THR GLU ILE PRO PHE
SEQRES 39 C 502 GLU GLN ILE LYS PRO VAL LYS PRO
HET NI A 503 1
HET ACT A 504 4
HET ACT A 505 4
HET ACT A 506 4
HET ACT A 507 4
HET SO4 A 508 5
HET CL A 509 1
HET CL A 510 1
HET HCT A 511 13
HET GOL A 512 6
HET GOL A 513 6
HET GOL A 514 6
HET GOL A 515 6
HET NI B 503 1
HET ACT B 504 4
HET ACT B 505 4
HET ACT B 506 4
HET ACT B 507 4
HET CL B 508 1
HET CL B 509 1
HET CL B 510 1
HET HCT B 511 13
HET GOL B 512 6
HET GOL B 513 6
HET GOL B 514 6
HET GOL B 515 6
HET NI C 503 1
HET ACT C 504 4
HET ACT C 505 4
HET ACT C 506 4
HET CL C 507 1
HET CL C 508 1
HET HCT C 509 13
HETNAM NI NICKEL (II) ION
HETNAM ACT ACETATE ION
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM HCT (2R)-BUTANE-1,2,4-TRICARBOXYLIC ACID
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 NI 3(NI 2+)
FORMUL 5 ACT 11(C2 H3 O2 1-)
FORMUL 9 SO4 O4 S 2-
FORMUL 10 CL 7(CL 1-)
FORMUL 12 HCT 3(C7 H10 O6)
FORMUL 13 GOL 8(C3 H8 O3)
FORMUL 37 HOH *265(H2 O)
HELIX 1 1 GLN A 26 TYR A 34 1 9
HELIX 2 2 ASP A 80 ASP A 93 1 14
HELIX 3 3 ASN A 94 ALA A 99 5 6
HELIX 4 4 LEU A 101 GLN A 106 1 6
HELIX 5 5 PRO A 128 ALA A 134 1 7
HELIX 6 6 ALA A 143 PHE A 147 5 5
HELIX 7 7 ASP A 201 THR A 211 1 11
HELIX 8 8 PRO A 225 GLN A 234 1 10
HELIX 9 9 GLU A 262 VAL A 273 1 12
HELIX 10 10 ASN A 274 LEU A 283 1 10
HELIX 11 11 ASP A 311 ALA A 322 1 12
HELIX 12 12 ASP A 350 GLN A 366 1 17
HELIX 13 13 GLU A 377 GLY A 388 1 12
HELIX 14 14 PRO A 404 MET A 411 1 8
HELIX 15 15 HIS A 416 GLN A 423 1 8
HELIX 16 16 ASP A 427 THR A 441 1 15
HELIX 17 17 ASP A 443 GLU A 461 1 19
HELIX 18 18 PRO A 478 GLY A 481 5 4
HELIX 19 19 PRO A 493 ILE A 497 5 5
HELIX 20 20 GLN B 26 TYR B 34 1 9
HELIX 21 21 ASP B 80 ASP B 93 1 14
HELIX 22 22 ASN B 94 ALA B 99 5 6
HELIX 23 23 LEU B 101 GLN B 106 1 6
HELIX 24 24 PRO B 128 ALA B 134 1 7
HELIX 25 25 ALA B 143 PHE B 147 5 5
HELIX 26 26 ASP B 201 THR B 211 1 11
HELIX 27 27 PRO B 225 GLN B 234 1 10
HELIX 28 28 GLU B 262 VAL B 273 1 12
HELIX 29 29 ASN B 274 ASN B 281 1 8
HELIX 30 30 ASP B 311 ALA B 322 1 12
HELIX 31 31 ASP B 350 GLN B 366 1 17
HELIX 32 32 GLU B 377 GLY B 388 1 12
HELIX 33 33 PRO B 404 SER B 410 1 7
HELIX 34 34 MET B 411 VAL B 413 5 3
HELIX 35 35 ALA B 417 GLN B 422 1 6
HELIX 36 36 ASP B 427 THR B 441 1 15
HELIX 37 37 ASP B 443 GLU B 461 1 19
HELIX 38 38 PRO B 478 GLY B 481 5 4
HELIX 39 39 PRO B 493 ILE B 497 5 5
HELIX 40 40 GLN C 26 TYR C 34 1 9
HELIX 41 41 ASP C 80 ASP C 93 1 14
HELIX 42 42 ASN C 94 ALA C 99 5 6
HELIX 43 43 LEU C 101 GLN C 106 1 6
HELIX 44 44 PRO C 128 ALA C 134 1 7
HELIX 45 45 ALA C 143 PHE C 147 5 5
HELIX 46 46 ASP C 201 THR C 211 1 11
HELIX 47 47 PRO C 225 GLN C 234 1 10
HELIX 48 48 GLU C 262 VAL C 273 1 12
HELIX 49 49 ASN C 274 ASN C 281 1 8
HELIX 50 50 ASP C 311 ALA C 322 1 12
HELIX 51 51 ASP C 350 GLN C 366 1 17
HELIX 52 52 GLU C 377 GLY C 388 1 12
HELIX 53 53 PRO C 404 MET C 411 1 8
HELIX 54 54 ALA C 417 GLN C 422 1 6
HELIX 55 55 ASP C 427 LEU C 439 1 13
HELIX 56 56 ASP C 443 GLU C 461 1 19
HELIX 57 57 PRO C 478 GLY C 481 5 4
HELIX 58 58 PRO C 493 ILE C 497 5 5
SHEET 1 A 4 GLU A 5 TRP A 10 0
SHEET 2 A 4 LYS A 193 VAL A 198 1 O THR A 195 N THR A 8
SHEET 3 A 4 TYR A 175 ARG A 180 -1 N ASP A 176 O PHE A 196
SHEET 4 A 4 TRP A 165 LYS A 171 -1 N GLU A 169 O VAL A 177
SHEET 1 B 2 VAL A 38 TYR A 40 0
SHEET 2 B 2 VAL A 46 PRO A 48 -1 O ILE A 47 N LYS A 39
SHEET 1 C 4 ALA A 51 HIS A 56 0
SHEET 2 C 4 THR A 62 LEU A 67 -1 O THR A 64 N THR A 55
SHEET 3 C 4 GLU A 117 LEU A 122 -1 O ILE A 120 N TRP A 63
SHEET 4 C 4 ILE A 107 ALA A 112 -1 N VAL A 108 O THR A 121
SHEET 1 D 3 LEU A 216 GLY A 219 0
SHEET 2 D 3 TYR A 464 SER A 476 -1 O VAL A 475 N LEU A 217
SHEET 3 D 3 GLN A 288 VAL A 289 -1 N GLN A 288 O TYR A 469
SHEET 1 E 6 LEU A 216 GLY A 219 0
SHEET 2 E 6 TYR A 464 SER A 476 -1 O VAL A 475 N LEU A 217
SHEET 3 E 6 HIS A 239 LEU A 253 -1 N HIS A 239 O SER A 476
SHEET 4 E 6 MET A 392 ARG A 396 -1 O HIS A 395 N MET A 250
SHEET 5 E 6 ARG A 341 ILE A 347 1 N GLU A 343 O MET A 392
SHEET 6 E 6 ASP A 370 GLU A 376 1 O ASP A 370 N ILE A 342
SHEET 1 F 2 GLU A 334 LYS A 335 0
SHEET 2 F 2 GLN A 338 PRO A 339 -1 O GLN A 338 N LYS A 335
SHEET 1 G 4 GLU B 5 TRP B 10 0
SHEET 2 G 4 LYS B 193 VAL B 198 1 O THR B 195 N THR B 8
SHEET 3 G 4 TYR B 175 ARG B 180 -1 N PHE B 178 O ILE B 194
SHEET 4 G 4 TRP B 165 LYS B 171 -1 N LYS B 171 O TYR B 175
SHEET 1 H 2 VAL B 38 TYR B 40 0
SHEET 2 H 2 VAL B 46 PRO B 48 -1 O ILE B 47 N LYS B 39
SHEET 1 I 4 ALA B 51 HIS B 56 0
SHEET 2 I 4 THR B 62 LEU B 67 -1 O THR B 64 N THR B 55
SHEET 3 I 4 GLU B 117 LEU B 122 -1 O ILE B 120 N TRP B 63
SHEET 4 I 4 ILE B 107 ALA B 112 -1 N VAL B 108 O THR B 121
SHEET 1 J 3 LEU B 216 ASN B 220 0
SHEET 2 J 3 MET B 472 SER B 476 -1 O VAL B 475 N LEU B 217
SHEET 3 J 3 HIS B 239 LEU B 242 -1 N HIS B 239 O SER B 476
SHEET 1 K 5 ASP B 370 GLU B 376 0
SHEET 2 K 5 ARG B 341 ILE B 347 1 N LEU B 344 O ILE B 374
SHEET 3 K 5 MET B 392 ARG B 396 1 O MET B 392 N GLU B 343
SHEET 4 K 5 GLU B 247 LEU B 253 -1 N MET B 250 O HIS B 395
SHEET 5 K 5 TYR B 464 ILE B 470 -1 O LEU B 465 N LEU B 251
SHEET 1 L 2 GLU B 334 LYS B 335 0
SHEET 2 L 2 GLN B 338 PRO B 339 -1 O GLN B 338 N LYS B 335
SHEET 1 M 4 ILE C 6 TRP C 10 0
SHEET 2 M 4 LYS C 193 VAL C 198 1 O THR C 195 N THR C 8
SHEET 3 M 4 TYR C 175 ARG C 180 -1 N PHE C 178 O ILE C 194
SHEET 4 M 4 TRP C 165 LYS C 171 -1 N ILE C 166 O VAL C 179
SHEET 1 N 2 VAL C 38 TYR C 40 0
SHEET 2 N 2 VAL C 46 PRO C 48 -1 O ILE C 47 N LYS C 39
SHEET 1 O 4 SER C 53 HIS C 56 0
SHEET 2 O 4 THR C 62 THR C 66 -1 O THR C 66 N SER C 53
SHEET 3 O 4 GLU C 117 LEU C 122 -1 O LEU C 118 N PHE C 65
SHEET 4 O 4 ILE C 107 ALA C 112 -1 N VAL C 108 O THR C 121
SHEET 1 P 3 LEU C 216 ASN C 220 0
SHEET 2 P 3 MET C 472 SER C 476 -1 O MET C 473 N GLY C 219
SHEET 3 P 3 HIS C 239 LEU C 242 -1 N HIS C 239 O SER C 476
SHEET 1 Q 6 GLN C 288 VAL C 289 0
SHEET 2 Q 6 TYR C 464 ILE C 470 -1 O TYR C 469 N GLN C 288
SHEET 3 Q 6 GLU C 247 LEU C 253 -1 N VAL C 249 O ILE C 467
SHEET 4 Q 6 MET C 392 ARG C 396 -1 O ILE C 393 N ALA C 252
SHEET 5 Q 6 ARG C 341 ILE C 347 1 N GLU C 343 O MET C 392
SHEET 6 Q 6 ASP C 370 GLU C 376 1 O SER C 372 N LEU C 344
SHEET 1 R 2 GLU C 334 LYS C 335 0
SHEET 2 R 2 GLN C 338 PRO C 339 -1 O GLN C 338 N LYS C 335
LINK NI NI A 503 O6 HCT A 511 1555 1555 2.14
LINK NE2 HIS B 416 NI NI B 503 1555 1555 2.25
LINK NI NI B 503 O6 HCT B 511 1555 1555 1.95
LINK NI NI B 503 O3 HCT B 511 1555 1555 2.24
LINK NI NI B 503 O1 HCT B 511 1555 1555 2.07
LINK NE2 HIS C 416 NI NI C 503 1555 1555 2.39
LINK NI NI C 503 O6 HCT C 509 1555 1555 2.41
CISPEP 1 PRO A 3 ASP A 4 0 19.15
CISPEP 2 THR A 23 PRO A 24 0 4.78
CISPEP 3 ARG A 137 PRO A 138 0 7.55
CISPEP 4 ALA A 258 PRO A 259 0 -6.96
CISPEP 5 ALA A 400 PRO A 401 0 2.53
CISPEP 6 ASP A 403 PRO A 404 0 -5.09
CISPEP 7 THR B 23 PRO B 24 0 6.16
CISPEP 8 ARG B 137 PRO B 138 0 2.02
CISPEP 9 ALA B 258 PRO B 259 0 -4.36
CISPEP 10 TYR B 284 GLY B 285 0 22.55
CISPEP 11 GLY B 285 THR B 286 0 20.28
CISPEP 12 ALA B 400 PRO B 401 0 -2.15
CISPEP 13 ASP B 403 PRO B 404 0 0.27
CISPEP 14 THR C 23 PRO C 24 0 9.18
CISPEP 15 ARG C 137 PRO C 138 0 3.96
CISPEP 16 ALA C 258 PRO C 259 0 -9.59
CISPEP 17 ALA C 400 PRO C 401 0 -6.00
CISPEP 18 ASP C 403 PRO C 404 0 3.12
SITE 1 AC1 1 HIS B 416
SITE 1 AC2 1 HIS C 416
SITE 1 AC3 5 THR C 292 LEU C 293 LEU C 455 HIS C 459
SITE 2 AC3 5 TYR C 464
SITE 1 AC4 4 LYS C 330 ASP C 331 ILE C 332 ARG C 365
SITE 1 AC5 2 SER A 57 GLU A 58
SITE 1 AC6 6 GLU B 221 LEU B 226 PHE B 229 LEU B 283
SITE 2 AC6 6 THR B 286 MET B 473
SITE 1 AC7 5 GLN C 385 HIS C 395 ARG C 396 TRP C 398
SITE 2 AC7 5 HIS C 416
SITE 1 AC8 3 GLN A 288 THR B 286 GLN B 288
SITE 1 AC9 2 ARG B 341 LYS C 433
SITE 1 BC1 4 TYR B 271 LYS B 306 PRO B 307 HIS B 459
SITE 1 BC2 6 THR B 8 ALA B 9 LEU B 216 LEU B 217
SITE 2 BC2 6 TYR B 218 LEU B 223
SITE 1 BC3 5 ASP A 93 ASN A 94 ARG A 95 GLN A 96
SITE 2 BC3 5 GLN C 446
SITE 1 BC4 3 GLN A 361 SER A 372 LEU A 373
SITE 1 BC5 2 THR B 441 HIS B 442
SITE 1 BC6 2 LEU B 293 HIS B 459
SITE 1 BC7 5 TYR B 22 ARG B 97 ARG B 137 TRP B 398
SITE 2 BC7 5 HIS B 416
SITE 1 BC8 6 TYR A 22 ARG A 97 TRP A 100 ARG A 137
SITE 2 BC8 6 TRP A 398 HIS A 416
SITE 1 BC9 8 TYR C 22 MET C 27 ARG C 97 TRP C 100
SITE 2 BC9 8 ARG C 137 ARG C 396 TRP C 398 HIS C 416
SITE 1 CC1 7 ASN A 274 LYS A 276 ASP A 280 LYS A 316
SITE 2 CC1 7 GLU A 320 LEU A 326 ARG A 333
SITE 1 CC2 4 PRO B 48 LYS B 52 SER B 53 TRP B 54
SITE 1 CC3 4 THR A 349 GLU A 376 GLU A 377 GLU A 378
SITE 1 CC4 7 ASN B 254 ALA B 256 LYS B 257 ASP B 387
SITE 2 CC4 7 GLY B 388 GLN B 420 GLN B 423
SITE 1 CC5 2 SER B 57 GLU B 58
SITE 1 CC6 6 ALA A 42 ASP A 43 GLN B 41 ALA B 42
SITE 2 CC6 6 TYR B 485 PRO B 487
SITE 1 CC7 2 LYS B 354 GLU B 358
SITE 1 CC8 5 ARG A 389 GLU B 358 GLN B 361 SER B 372
SITE 2 CC8 5 LEU B 373
CRYST1 158.570 158.570 134.940 90.00 90.00 120.00 P 62 18
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 0.006306 0.003641 0.000000 0.00000
SCALE2 0.000000 0.007282 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007411 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
