HEADER TRANSFERASE 04-DEC-01 1KJI
TITLE CRYSTAL STRUCTURE OF GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE IN
TITLE 2 COMPLEX WITH MG-AMPPCP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GART 2; GAR TRANSFORMYLASE 2; 5'-PHOSPHORIBOSYLGLYCINAMIDE;
COMPND 5 EC: 2.1.2.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: PURT;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-22B
KEYWDS ATP-GRASP, PURINE BIOSYNTHESIS, NUCLEOTIDE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.B.THODEN,S.M.FIRESTINE,S.J.BENKOVIC,H.M.HOLDEN
REVDAT 4 11-OCT-17 1KJI 1 REMARK
REVDAT 3 24-FEB-09 1KJI 1 VERSN
REVDAT 2 01-APR-03 1KJI 1 JRNL
REVDAT 1 28-JUN-02 1KJI 0
JRNL AUTH J.B.THODEN,S.M.FIRESTINE,S.J.BENKOVIC,H.M.HOLDEN
JRNL TITL PURT-ENCODED GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE.
JRNL TITL 2 ACCOMMODATION OF ADENOSINE NUCLEOTIDE ANALOGS WITHIN THE
JRNL TITL 3 ACTIVE SITE.
JRNL REF J.BIOL.CHEM. V. 277 23898 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11953435
JRNL DOI 10.1074/JBC.M202251200
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 3 NUMBER OF REFLECTIONS : 105396
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 10541
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.1840
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 105396
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5930
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 87
REMARK 3 SOLVENT ATOMS : 944
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.011 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 2.350 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : ENGH & HUBER
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KJI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-DEC-01.
REMARK 100 THE DEPOSITION ID IS D_1000015015.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-NOV-00
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.7
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 : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GOEBEL OPTICS
REMARK 200 OPTICS : GOEBEL OPTICS
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS HI-STAR
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : FRAMBO
REMARK 200 DATA SCALING SOFTWARE : SAINT
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105396
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.21500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: TNT
REMARK 200 STARTING MODEL: PDB ENTRY 1EYZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 5000, NACL, MGCL2, MOPS, AMPPCP,
REMARK 280 PH 6.7, BATCH AT 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 31.10000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 89.60000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.10000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 89.60000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 7610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 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 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 GLY A 188
REMARK 465 ALA A 189
REMARK 465 GLY B 188
REMARK 465 ALA B 189
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 O HOH A 582 O HOH A 754 2.10
REMARK 500 O LEU B 125 O HOH B 694 2.15
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 NH2 ARG B 191 NH2 ARG B 191 2555 2.01
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 GLU A 30 CD GLU A 30 OE2 0.078
REMARK 500 GLU A 72 CD GLU A 72 OE2 0.072
REMARK 500 GLU A 96 CD GLU A 96 OE2 0.071
REMARK 500 GLU A 138 CD GLU A 138 OE2 0.067
REMARK 500 GLU A 274 CD GLU A 274 OE2 0.068
REMARK 500 GLU A 279 CD GLU A 279 OE2 0.067
REMARK 500 GLU B 82 CD GLU B 82 OE2 0.072
REMARK 500 GLU B 96 CD GLU B 96 OE2 0.082
REMARK 500 GLU B 97 CD GLU B 97 OE2 0.068
REMARK 500 GLU B 143 CD GLU B 143 OE2 0.075
REMARK 500 GLU B 172 CD GLU B 172 OE2 0.069
REMARK 500 GLU B 195 CD GLU B 195 OE2 0.069
REMARK 500 GLU B 226 CD GLU B 226 OE2 0.068
REMARK 500 GLU B 245 CD GLU B 245 OE2 0.071
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 ARG A 9 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ASP A 89 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 CYS A 104 N - CA - CB ANGL. DEV. = 9.8 DEGREES
REMARK 500 ASP A 136 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ARG A 186 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 191 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ASP A 201 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP A 201 CB - CG - OD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ASP A 213 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 227 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 227 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP A 229 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 246 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 252 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ASP A 286 CB - CG - OD1 ANGL. DEV. = 9.7 DEGREES
REMARK 500 ASP A 286 CB - CG - OD2 ANGL. DEV. = -9.8 DEGREES
REMARK 500 ASP A 296 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 347 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP A 359 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG A 362 CG - CD - NE ANGL. DEV. = 17.7 DEGREES
REMARK 500 ARG A 362 CD - NE - CZ ANGL. DEV. = 11.5 DEGREES
REMARK 500 ARG A 362 NH1 - CZ - NH2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 ARG A 362 NE - CZ - NH2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ASP A 376 CB - CG - OD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ARG A 380 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 380 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 33 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ASP B 42 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG B 69 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP B 89 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 89 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 CYS B 104 N - CA - CB ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG B 142 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ASP B 147 CB - CG - OD1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ASP B 147 CB - CG - OD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ARG B 191 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 191 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP B 201 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP B 201 CB - CG - OD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 GLU B 203 CB - CA - C ANGL. DEV. = -14.1 DEGREES
REMARK 500 ASP B 286 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP B 296 CB - CG - OD1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ASP B 296 CB - CG - OD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 ARG B 363 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG B 363 NE - CZ - NH2 ANGL. DEV. = -3.7 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 LEU A 8 -9.67 81.02
REMARK 500 ALA A 87 73.13 -66.34
REMARK 500 GLU A 97 7.91 -66.73
REMARK 500 ARG A 186 -19.41 -18.76
REMARK 500 SER A 278 -63.94 -109.79
REMARK 500 ARG A 283 175.59 174.09
REMARK 500 LEU A 330 -179.78 -171.69
REMARK 500 ASN A 334 60.64 -160.65
REMARK 500 ASP A 359 73.20 -153.19
REMARK 500 LEU B 8 -9.13 82.47
REMARK 500 ALA B 85 62.85 -66.62
REMARK 500 GLU B 123 -72.06 -84.38
REMARK 500 SER B 161 21.44 48.06
REMARK 500 LEU B 174 -39.91 -38.38
REMARK 500 ARG B 186 -62.38 -92.10
REMARK 500 SER B 278 -63.71 -103.70
REMARK 500 ARG B 283 175.88 177.60
REMARK 500 TYR B 318 40.96 -94.43
REMARK 500 ASN B 334 56.52 -154.22
REMARK 500 ASP B 359 74.06 -154.53
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 MG A 393 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ACP A 1 O3G
REMARK 620 2 ACP A 1 O2B 89.8
REMARK 620 3 HOH A 509 O 107.7 96.7
REMARK 620 4 GLU A 279 OE1 93.2 87.2 158.6
REMARK 620 5 GLU A 279 OE2 148.0 90.4 104.0 54.9
REMARK 620 6 HOH A 536 O 93.1 168.8 92.6 81.9 81.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 394 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ACP A 1 O2A
REMARK 620 2 GLU A 267 OE1 151.0
REMARK 620 3 GLU A 267 OE2 94.0 57.1
REMARK 620 4 GLU A 279 OE1 86.7 88.2 84.8
REMARK 620 5 HOH A 465 O 85.3 95.5 88.8 169.3
REMARK 620 6 ACP A 1 O2G 116.0 92.9 150.0 95.7 94.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 395 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 521 O
REMARK 620 2 HOH B 651 O 162.4
REMARK 620 3 HOH B 456 O 95.4 101.3
REMARK 620 4 ALA A 53 O 89.3 80.2 145.0
REMARK 620 5 ALA B 53 O 74.4 103.9 77.0 137.1
REMARK 620 6 HOH B 745 O 84.5 80.3 131.9 83.0 56.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 396 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 637 O
REMARK 620 2 GLU A 95 OE1 119.9
REMARK 620 3 HOH A 567 O 115.4 111.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 393 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ACP B 396 O3G
REMARK 620 2 GLU B 279 OE1 97.8
REMARK 620 3 ACP B 396 O2B 80.6 105.7
REMARK 620 4 HOH B 547 O 95.7 163.0 86.6
REMARK 620 5 HOH B 470 O 89.3 83.5 167.1 86.4
REMARK 620 6 GLU B 279 OE2 157.1 60.6 111.1 104.4 81.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 394 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 635 O
REMARK 620 2 ACP B 396 O2G 95.2
REMARK 620 3 GLU B 267 OE1 92.5 88.9
REMARK 620 4 ACP B 396 O2A 102.1 122.4 143.4
REMARK 620 5 GLU B 279 OE1 165.6 89.2 73.9 86.9
REMARK 620 6 GLU B 267 OE2 75.4 136.6 50.3 100.9 92.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 395 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 101 O
REMARK 620 2 PRO B 103 O 82.2
REMARK 620 3 ASN B 100 ND2 91.0 156.3
REMARK 620 4 HOH B 690 O 150.2 87.0 108.9
REMARK 620 5 HOH B 461 O 74.1 125.6 73.1 90.3
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 393
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 394
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 393
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 394
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 395
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 396
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 395
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 397
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP B 396
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPO A 398
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 399
DBREF 1KJI A 2 392 UNP P33221 PURT_ECOLI 1 391
DBREF 1KJI B 2 392 UNP P33221 PURT_ECOLI 1 391
SEQRES 1 A 391 THR LEU LEU GLY THR ALA LEU ARG PRO ALA ALA THR ARG
SEQRES 2 A 391 VAL MET LEU LEU GLY SER GLY GLU LEU GLY LYS GLU VAL
SEQRES 3 A 391 ALA ILE GLU CYS GLN ARG LEU GLY VAL GLU VAL ILE ALA
SEQRES 4 A 391 VAL ASP ARG TYR ALA ASP ALA PRO ALA MET HIS VAL ALA
SEQRES 5 A 391 HIS ARG SER HIS VAL ILE ASN MET LEU ASP GLY ASP ALA
SEQRES 6 A 391 LEU ARG ARG VAL VAL GLU LEU GLU LYS PRO HIS TYR ILE
SEQRES 7 A 391 VAL PRO GLU ILE GLU ALA ILE ALA THR ASP MET LEU ILE
SEQRES 8 A 391 GLN LEU GLU GLU GLU GLY LEU ASN VAL VAL PRO CYS ALA
SEQRES 9 A 391 ARG ALA THR LYS LEU THR MET ASN ARG GLU GLY ILE ARG
SEQRES 10 A 391 ARG LEU ALA ALA GLU GLU LEU GLN LEU PRO THR SER THR
SEQRES 11 A 391 TYR ARG PHE ALA ASP SER GLU SER LEU PHE ARG GLU ALA
SEQRES 12 A 391 VAL ALA ASP ILE GLY TYR PRO CYS ILE VAL LYS PRO VAL
SEQRES 13 A 391 MET SER SER SER GLY LYS GLY GLN THR PHE ILE ARG SER
SEQRES 14 A 391 ALA GLU GLN LEU ALA GLN ALA TRP LYS TYR ALA GLN GLN
SEQRES 15 A 391 GLY GLY ARG ALA GLY ALA GLY ARG VAL ILE VAL GLU GLY
SEQRES 16 A 391 VAL VAL LYS PHE ASP PHE GLU ILE THR LEU LEU THR VAL
SEQRES 17 A 391 SER ALA VAL ASP GLY VAL HIS PHE CYS ALA PRO VAL GLY
SEQRES 18 A 391 HIS ARG GLN GLU ASP GLY ASP TYR ARG GLU SER TRP GLN
SEQRES 19 A 391 PRO GLN GLN MET SER PRO LEU ALA LEU GLU ARG ALA GLN
SEQRES 20 A 391 GLU ILE ALA ARG LYS VAL VAL LEU ALA LEU GLY GLY TYR
SEQRES 21 A 391 GLY LEU PHE GLY VAL GLU LEU PHE VAL CYS GLY ASP GLU
SEQRES 22 A 391 VAL ILE PHE SER GLU VAL SER PRO ARG PRO HIS ASP THR
SEQRES 23 A 391 GLY MET VAL THR LEU ILE SER GLN ASP LEU SER GLU PHE
SEQRES 24 A 391 ALA LEU HIS VAL ARG ALA PHE LEU GLY LEU PRO VAL GLY
SEQRES 25 A 391 GLY ILE ARG GLN TYR GLY PRO ALA ALA SER ALA VAL ILE
SEQRES 26 A 391 LEU PRO GLN LEU THR SER GLN ASN VAL THR PHE ASP ASN
SEQRES 27 A 391 VAL GLN ASN ALA VAL GLY ALA ASP LEU GLN ILE ARG LEU
SEQRES 28 A 391 PHE GLY LYS PRO GLU ILE ASP GLY SER ARG ARG LEU GLY
SEQRES 29 A 391 VAL ALA LEU ALA THR ALA GLU SER VAL VAL ASP ALA ILE
SEQRES 30 A 391 GLU ARG ALA LYS HIS ALA ALA GLY GLN VAL LYS VAL GLN
SEQRES 31 A 391 GLY
SEQRES 1 B 391 THR LEU LEU GLY THR ALA LEU ARG PRO ALA ALA THR ARG
SEQRES 2 B 391 VAL MET LEU LEU GLY SER GLY GLU LEU GLY LYS GLU VAL
SEQRES 3 B 391 ALA ILE GLU CYS GLN ARG LEU GLY VAL GLU VAL ILE ALA
SEQRES 4 B 391 VAL ASP ARG TYR ALA ASP ALA PRO ALA MET HIS VAL ALA
SEQRES 5 B 391 HIS ARG SER HIS VAL ILE ASN MET LEU ASP GLY ASP ALA
SEQRES 6 B 391 LEU ARG ARG VAL VAL GLU LEU GLU LYS PRO HIS TYR ILE
SEQRES 7 B 391 VAL PRO GLU ILE GLU ALA ILE ALA THR ASP MET LEU ILE
SEQRES 8 B 391 GLN LEU GLU GLU GLU GLY LEU ASN VAL VAL PRO CYS ALA
SEQRES 9 B 391 ARG ALA THR LYS LEU THR MET ASN ARG GLU GLY ILE ARG
SEQRES 10 B 391 ARG LEU ALA ALA GLU GLU LEU GLN LEU PRO THR SER THR
SEQRES 11 B 391 TYR ARG PHE ALA ASP SER GLU SER LEU PHE ARG GLU ALA
SEQRES 12 B 391 VAL ALA ASP ILE GLY TYR PRO CYS ILE VAL LYS PRO VAL
SEQRES 13 B 391 MET SER SER SER GLY LYS GLY GLN THR PHE ILE ARG SER
SEQRES 14 B 391 ALA GLU GLN LEU ALA GLN ALA TRP LYS TYR ALA GLN GLN
SEQRES 15 B 391 GLY GLY ARG ALA GLY ALA GLY ARG VAL ILE VAL GLU GLY
SEQRES 16 B 391 VAL VAL LYS PHE ASP PHE GLU ILE THR LEU LEU THR VAL
SEQRES 17 B 391 SER ALA VAL ASP GLY VAL HIS PHE CYS ALA PRO VAL GLY
SEQRES 18 B 391 HIS ARG GLN GLU ASP GLY ASP TYR ARG GLU SER TRP GLN
SEQRES 19 B 391 PRO GLN GLN MET SER PRO LEU ALA LEU GLU ARG ALA GLN
SEQRES 20 B 391 GLU ILE ALA ARG LYS VAL VAL LEU ALA LEU GLY GLY TYR
SEQRES 21 B 391 GLY LEU PHE GLY VAL GLU LEU PHE VAL CYS GLY ASP GLU
SEQRES 22 B 391 VAL ILE PHE SER GLU VAL SER PRO ARG PRO HIS ASP THR
SEQRES 23 B 391 GLY MET VAL THR LEU ILE SER GLN ASP LEU SER GLU PHE
SEQRES 24 B 391 ALA LEU HIS VAL ARG ALA PHE LEU GLY LEU PRO VAL GLY
SEQRES 25 B 391 GLY ILE ARG GLN TYR GLY PRO ALA ALA SER ALA VAL ILE
SEQRES 26 B 391 LEU PRO GLN LEU THR SER GLN ASN VAL THR PHE ASP ASN
SEQRES 27 B 391 VAL GLN ASN ALA VAL GLY ALA ASP LEU GLN ILE ARG LEU
SEQRES 28 B 391 PHE GLY LYS PRO GLU ILE ASP GLY SER ARG ARG LEU GLY
SEQRES 29 B 391 VAL ALA LEU ALA THR ALA GLU SER VAL VAL ASP ALA ILE
SEQRES 30 B 391 GLU ARG ALA LYS HIS ALA ALA GLY GLN VAL LYS VAL GLN
SEQRES 31 B 391 GLY
HET MG A 393 1
HET MG A 394 1
HET NA A 395 1
HET NA A 396 1
HET CL A 397 1
HET ACP A 1 31
HET MPO A 398 13
HET EDO A 399 4
HET MG B 393 1
HET MG B 394 1
HET NA B 395 1
HET ACP B 396 31
HETNAM MG MAGNESIUM ION
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETNAM ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER
HETNAM MPO 3[N-MORPHOLINO]PROPANE SULFONIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETSYN ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 MG 4(MG 2+)
FORMUL 5 NA 3(NA 1+)
FORMUL 7 CL CL 1-
FORMUL 8 ACP 2(C11 H18 N5 O12 P3)
FORMUL 9 MPO C7 H15 N O4 S
FORMUL 10 EDO C2 H6 O2
FORMUL 15 HOH *944(H2 O)
HELIX 1 1 GLY A 21 ARG A 33 1 13
HELIX 2 2 ALA A 47 ALA A 53 5 7
HELIX 3 3 ASP A 63 LYS A 75 1 13
HELIX 4 4 ALA A 87 GLU A 97 1 11
HELIX 5 5 CYS A 104 MET A 112 1 9
HELIX 6 6 ASN A 113 GLU A 123 1 11
HELIX 7 7 SER A 137 GLY A 149 1 13
HELIX 8 8 SER A 170 GLU A 172 5 3
HELIX 9 9 GLN A 173 GLY A 184 1 12
HELIX 10 10 SER A 240 GLY A 259 1 20
HELIX 11 11 HIS A 285 MET A 289 5 5
HELIX 12 12 VAL A 290 GLN A 295 1 6
HELIX 13 13 SER A 298 LEU A 308 1 11
HELIX 14 14 ASN A 339 ALA A 343 5 5
HELIX 15 15 SER A 373 VAL A 388 1 16
HELIX 16 16 GLY B 21 ARG B 33 1 13
HELIX 17 17 ALA B 47 VAL B 52 1 6
HELIX 18 18 ASP B 63 LYS B 75 1 13
HELIX 19 19 ALA B 87 GLU B 97 1 11
HELIX 20 20 CYS B 104 MET B 112 1 9
HELIX 21 21 ASN B 113 GLU B 123 1 11
HELIX 22 22 SER B 137 GLY B 149 1 13
HELIX 23 23 SER B 170 GLU B 172 5 3
HELIX 24 24 GLN B 173 GLY B 184 1 12
HELIX 25 25 SER B 240 GLY B 259 1 20
HELIX 26 26 HIS B 285 MET B 289 5 5
HELIX 27 27 VAL B 290 GLN B 295 1 6
HELIX 28 28 SER B 298 LEU B 308 1 11
HELIX 29 29 ASN B 339 ALA B 343 5 5
HELIX 30 30 SER B 373 VAL B 388 1 16
SHEET 1 A 5 ARG A 55 VAL A 58 0
SHEET 2 A 5 GLU A 37 ASP A 42 1 N ALA A 40 O ARG A 55
SHEET 3 A 5 ARG A 14 LEU A 18 1 N LEU A 17 O ILE A 39
SHEET 4 A 5 TYR A 78 PRO A 81 1 O TYR A 78 N MET A 16
SHEET 5 A 5 ASN A 100 VAL A 101 1 O ASN A 100 N ILE A 79
SHEET 1 B 4 TYR A 132 ALA A 135 0
SHEET 2 B 4 VAL A 192 GLY A 196 -1 O VAL A 194 N ARG A 133
SHEET 3 B 4 CYS A 152 PRO A 156 -1 N LYS A 155 O ILE A 193
SHEET 4 B 4 THR A 166 ILE A 168 -1 O ILE A 168 N CYS A 152
SHEET 1 C 4 GLU A 274 SER A 281 0
SHEET 2 C 4 GLY A 262 CYS A 271 -1 N CYS A 271 O GLU A 274
SHEET 3 C 4 PHE A 202 ALA A 211 -1 N LEU A 206 O VAL A 266
SHEET 4 C 4 GLY A 214 PHE A 217 -1 O HIS A 216 N VAL A 209
SHEET 1 D 8 GLU A 274 SER A 281 0
SHEET 2 D 8 GLY A 262 CYS A 271 -1 N CYS A 271 O GLU A 274
SHEET 3 D 8 PHE A 202 ALA A 211 -1 N LEU A 206 O VAL A 266
SHEET 4 D 8 VAL A 221 GLU A 226 -1 O VAL A 221 N THR A 205
SHEET 5 D 8 ASP A 229 GLN A 235 -1 O ARG A 231 N ARG A 224
SHEET 6 D 8 ALA A 321 ILE A 326 -1 O SER A 323 N SER A 233
SHEET 7 D 8 GLY A 365 THR A 370 -1 O ALA A 367 N ALA A 324
SHEET 8 D 8 LEU A 348 LEU A 352 -1 N GLN A 349 O LEU A 368
SHEET 1 E 2 GLN A 329 SER A 332 0
SHEET 2 E 2 ILE A 358 SER A 361 -1 O GLY A 360 N LEU A 330
SHEET 1 F 2 THR A 336 ASP A 338 0
SHEET 2 F 2 LYS A 389 GLN A 391 -1 O GLN A 391 N THR A 336
SHEET 1 G 4 ARG B 55 VAL B 58 0
SHEET 2 G 4 GLU B 37 ASP B 42 1 N ALA B 40 O ARG B 55
SHEET 3 G 4 ARG B 14 LEU B 18 1 N VAL B 15 O GLU B 37
SHEET 4 G 4 TYR B 78 PRO B 81 1 O VAL B 80 N MET B 16
SHEET 1 H 4 TYR B 132 ALA B 135 0
SHEET 2 H 4 VAL B 192 GLY B 196 -1 O VAL B 194 N ARG B 133
SHEET 3 H 4 CYS B 152 PRO B 156 -1 N ILE B 153 O GLU B 195
SHEET 4 H 4 THR B 166 ILE B 168 -1 O ILE B 168 N CYS B 152
SHEET 1 I 4 GLU B 274 SER B 281 0
SHEET 2 I 4 GLY B 262 CYS B 271 -1 N PHE B 269 O ILE B 276
SHEET 3 I 4 PHE B 202 ALA B 211 -1 N LEU B 206 O VAL B 266
SHEET 4 I 4 GLY B 214 PHE B 217 -1 O GLY B 214 N ALA B 211
SHEET 1 J 8 GLU B 274 SER B 281 0
SHEET 2 J 8 GLY B 262 CYS B 271 -1 N PHE B 269 O ILE B 276
SHEET 3 J 8 PHE B 202 ALA B 211 -1 N LEU B 206 O VAL B 266
SHEET 4 J 8 VAL B 221 GLU B 226 -1 O VAL B 221 N THR B 205
SHEET 5 J 8 ASP B 229 GLN B 235 -1 O ARG B 231 N ARG B 224
SHEET 6 J 8 ALA B 321 ILE B 326 -1 O SER B 323 N SER B 233
SHEET 7 J 8 GLY B 365 THR B 370 -1 O ALA B 369 N ALA B 322
SHEET 8 J 8 LEU B 348 LEU B 352 -1 N GLN B 349 O LEU B 368
SHEET 1 K 2 GLN B 329 SER B 332 0
SHEET 2 K 2 ILE B 358 SER B 361 -1 O GLY B 360 N LEU B 330
SHEET 1 L 2 THR B 336 ASP B 338 0
SHEET 2 L 2 LYS B 389 GLN B 391 -1 O LYS B 389 N ASP B 338
LINK O3G ACP A 1 MG MG A 393 1555 1555 2.05
LINK O2B ACP A 1 MG MG A 393 1555 1555 1.96
LINK MG MG A 393 O HOH A 509 1555 1555 1.84
LINK MG MG A 393 OE1 GLU A 279 1555 1555 2.38
LINK MG MG A 393 OE2 GLU A 279 1555 1555 2.46
LINK MG MG A 393 O HOH A 536 1555 1555 2.54
LINK MG MG A 394 O2A ACP A 1 1555 1555 2.08
LINK MG MG A 394 OE1 GLU A 267 1555 1555 2.24
LINK MG MG A 394 OE2 GLU A 267 1555 1555 2.36
LINK MG MG A 394 OE1 GLU A 279 1555 1555 2.12
LINK MG MG A 394 O HOH A 465 1555 1555 2.20
LINK MG MG A 394 O2G ACP A 1 1555 1555 2.10
LINK NA NA A 395 O HOH A 521 1555 1555 2.42
LINK NA NA A 395 O HOH B 651 1555 1555 2.38
LINK NA NA A 395 O HOH B 456 1555 1555 2.47
LINK NA NA A 396 O HOH A 637 1555 1555 2.58
LINK MG MG B 393 O3G ACP B 396 1555 1555 2.10
LINK MG MG B 393 OE1 GLU B 279 1555 1555 2.11
LINK MG MG B 393 O2B ACP B 396 1555 1555 2.05
LINK MG MG B 393 O HOH B 547 1555 1555 1.71
LINK MG MG B 393 O HOH B 470 1555 1555 2.85
LINK MG MG B 393 OE2 GLU B 279 1555 1555 2.27
LINK MG MG B 394 O HOH B 635 1555 1555 2.45
LINK MG MG B 394 O2G ACP B 396 1555 1555 1.90
LINK MG MG B 394 OE1 GLU B 267 1555 1555 2.81
LINK MG MG B 394 O2A ACP B 396 1555 1555 1.85
LINK MG MG B 394 OE1 GLU B 279 1555 1555 2.27
LINK MG MG B 394 OE2 GLU B 267 1555 1555 2.29
LINK NA NA B 395 O VAL B 101 1555 1555 2.48
LINK NA NA B 395 O PRO B 103 1555 1555 2.49
LINK NA NA B 395 ND2 ASN B 100 1555 1555 2.47
LINK NA NA B 395 O HOH B 690 1555 1555 2.46
LINK O ALA A 53 NA NA A 395 1555 1555 2.68
LINK OE1 GLU A 95 NA NA A 396 1555 1555 2.69
LINK O ALA B 53 NA NA A 395 1555 1555 2.98
LINK NA NA A 395 O HOH B 745 1555 1555 2.88
LINK NA NA A 396 O HOH A 567 1555 1555 2.64
LINK NA NA B 395 O HOH B 461 1555 1555 2.92
CISPEP 1 VAL A 102 PRO A 103 0 -0.66
CISPEP 2 TYR A 150 PRO A 151 0 -0.70
CISPEP 3 GLN A 235 PRO A 236 0 -2.33
CISPEP 4 VAL B 102 PRO B 103 0 1.35
CISPEP 5 TYR B 150 PRO B 151 0 -1.29
CISPEP 6 GLN B 235 PRO B 236 0 -1.25
SITE 1 AC1 4 ACP A 1 GLU A 279 HOH A 509 HOH A 536
SITE 1 AC2 4 ACP A 1 GLU A 267 GLU A 279 HOH A 465
SITE 1 AC3 4 GLU B 279 ACP B 396 HOH B 470 HOH B 547
SITE 1 AC4 4 GLU B 267 GLU B 279 ACP B 396 HOH B 635
SITE 1 AC5 7 ALA A 53 HOH A 453 HOH A 521 ALA B 53
SITE 2 AC5 7 HOH B 456 HOH B 651 HOH B 745
SITE 1 AC6 5 GLU A 95 ASN A 100 VAL A 101 HOH A 567
SITE 2 AC6 5 HOH A 637
SITE 1 AC7 5 ASN B 100 VAL B 101 PRO B 103 HOH B 461
SITE 2 AC7 5 HOH B 690
SITE 1 AC8 6 ARG A 43 VAL A 58 ARG A 119 ARG A 133
SITE 2 AC8 6 PHE A 134 HOH A 590
SITE 1 AC9 26 ARG A 114 ILE A 153 LYS A 155 SER A 160
SITE 2 AC9 26 SER A 161 GLY A 162 GLN A 165 GLU A 195
SITE 3 AC9 26 GLY A 196 VAL A 198 GLU A 203 GLN A 225
SITE 4 AC9 26 GLU A 267 PHE A 269 GLU A 279 MG A 393
SITE 5 AC9 26 MG A 394 HOH A 432 HOH A 465 HOH A 475
SITE 6 AC9 26 HOH A 485 HOH A 509 HOH A 562 HOH A 563
SITE 7 AC9 26 HOH A 644 HOH A 758
SITE 1 BC1 20 ARG B 114 SER B 130 LYS B 155 SER B 159
SITE 2 BC1 20 SER B 160 SER B 161 GLY B 162 GLU B 195
SITE 3 BC1 20 GLY B 196 VAL B 198 GLU B 203 GLU B 267
SITE 4 BC1 20 GLU B 279 MG B 393 MG B 394 HOH B 547
SITE 5 BC1 20 HOH B 553 HOH B 572 HOH B 635 HOH B 767
SITE 1 BC2 13 ASP A 46 MET A 50 HIS A 51 ARG A 55
SITE 2 BC2 13 SER A 56 GLU A 143 HOH A 437 HOH A 453
SITE 3 BC2 13 HOH A 468 HOH A 685 HOH A 727 LEU B 8
SITE 4 BC2 13 HIS B 54
SITE 1 BC3 6 ASP A 63 THR A 129 SER A 130 THR A 131
SITE 2 BC3 6 TYR A 132 HOH A 502
CRYST1 62.200 179.200 76.200 90.00 90.00 90.00 P 21 21 2 8
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 0.016077 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005580 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013123 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
