HEADER TRANSFERASE 24-AUG-10 3OKA
TITLE CRYSTAL STRUCTURE OF CORYNEBACTERIUM GLUTAMICUM PIMB' IN COMPLEX WITH
TITLE 2 GDP-MAN (TRICLINIC CRYSTAL FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GDP-MANNOSE-DEPENDENT ALPHA-(1-6)-PHOSPHATIDYLINOSITOL
COMPND 3 MONOMANNOSIDE MANNOSYLTRANSFERASE;
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: GUANOSINE DIPHOSPHOMANNOSE-PHOSPHATIDYL-INOSITOL ALPHA-
COMPND 6 MANNOSYLTRANSFERASE, PHOSPHATIDYLINOSITOL ALPHA-MANNOSYLTRANSFERASE,
COMPND 7 PI ALPHA-MANNOSYLTRANSFERASE, ALPHA-MANNOSYLTRANSFERASE, ALPHA-MANT,
COMPND 8 ALPHA-D-MANNOSE-ALPHA-(1-6)-PHOSPHATIDYLMYO-INOSITOL-
COMPND 9 MANNOSYLTRANSFERASE;
COMPND 10 EC: 2.4.1.57;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 2;
COMPND 13 MOLECULE: N-TERMINAL HIS-AFFINITY TAG;
COMPND 14 CHAIN: C, D;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CORYNEBACTERIUM GLUTAMICUM;
SOURCE 3 ORGANISM_COMMON: BREVIBACTERIUM FLAVUM;
SOURCE 4 ORGANISM_TAXID: 1718;
SOURCE 5 GENE: PIMB, CGL2186, CG2400;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET16B;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 12 ORGANISM_TAXID: 562;
SOURCE 13 GENE: HIS-AFFINITY TAG;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GT-B FOLD, ALPHA-MANNOSYLTRANSFERASE, GDP-MAN BINDING, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.M.BATT,T.JABEEN,G.S.BESRA,K.FUTTERER
REVDAT 4 21-FEB-24 3OKA 1 REMARK
REVDAT 3 12-JAN-11 3OKA 1 JRNL
REVDAT 2 13-OCT-10 3OKA 1 JRNL
REVDAT 1 15-SEP-10 3OKA 0
JRNL AUTH S.M.BATT,T.JABEEN,A.K.MISHRA,N.VEERAPEN,K.KRUMBACH,
JRNL AUTH 2 L.EGGELING,G.S.BESRA,K.FUTTERER
JRNL TITL ACCEPTOR SUBSTRATE DISCRIMINATION IN
JRNL TITL 2 PHOSPHATIDYL-MYO-INOSITOL MANNOSIDE SYNTHESIS: STRUCTURAL
JRNL TITL 3 AND MUTATIONAL ANALYSIS OF MANNOSYLTRANSFERASE
JRNL TITL 4 CORYNEBACTERIUM GLUTAMICUM PIMB'.
JRNL REF J.BIOL.CHEM. V. 285 37741 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20843801
JRNL DOI 10.1074/JBC.M110.165407
REMARK 2
REMARK 2 RESOLUTION. 2.20 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 WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 33243
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1747
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1836
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 71.03
REMARK 3 BIN R VALUE (WORKING SET) : 0.2080
REMARK 3 BIN FREE R VALUE SET COUNT : 86
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5825
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 112
REMARK 3 SOLVENT ATOMS : 294
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.36000
REMARK 3 B22 (A**2) : -0.94000
REMARK 3 B33 (A**2) : 0.58000
REMARK 3 B12 (A**2) : -0.23000
REMARK 3 B13 (A**2) : -0.14000
REMARK 3 B23 (A**2) : 0.09000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.218
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.141
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.427
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6061 ; 0.008 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8273 ; 1.150 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 777 ; 5.219 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 230 ;32.537 ;22.739
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 920 ;13.186 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 45 ;16.682 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 956 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4521 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2537 ; 0.186 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4118 ; 0.295 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 345 ; 0.117 ; 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): 127 ; 0.229 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 24 ; 0.081 ; 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): 3975 ; 0.408 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6231 ; 0.691 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2352 ; 1.167 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2042 ; 1.961 ; 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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 381 1
REMARK 3 1 B 1 B 381 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 2788 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 2788 ; 0.05 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C -20 C -7 1
REMARK 3 1 D -20 D -7 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 C (A): 91 ; 0.07 ; 0.05
REMARK 3 TIGHT THERMAL 2 C (A**2): 91 ; 0.10 ; 0.50
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3OKA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1000061222.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-SEP-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : SI(311)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35191
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 43.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : 0.07300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.23800
REMARK 200 R SYM FOR SHELL (I) : 0.23800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6-26% PEG 3350, 0.1 M BIS-TRIS PH 5.5,
REMARK 280 0.1 M LITHIUM SULFATE AND 0.1 M GLYCINE, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 400
REMARK 400 COMPOUND
REMARK 400 AUTHORS EXPLAIN THAT THE EXPRESSION TAGS ARE NOT CLEAVED, BUT THERE
REMARK 400 IS NO CONTINUOUS DENSITY BETWEEN THE C-TERMINAL RESIDUE OF THE TAG
REMARK 400 AND THE N-TERMINUS OF THE ACTUAL PROTEIN SEQUENCE. WHILE A BIT
REMARK 400 ARBITRARY, THE AUTHORS GAVE THE SEQUENCE TAGS SEPARATE CHAIN IDS.
REMARK 400 IT WAS NOT POSSIBLE TO DETERMINE TO WHICH OF THE TWO PROTEIN CHAINS
REMARK 400 (A OR B) TAG-CHAINS C AND D BELONGED
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 MET A 1
REMARK 465 SER A 2
REMARK 465 ALA A 3
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ALA B 3
REMARK 465 MET C -24
REMARK 465 GLY C -23
REMARK 465 HIS C -22
REMARK 465 HIS C -21
REMARK 465 HIS C -20
REMARK 465 HIS C -19
REMARK 465 GLU C -7
REMARK 465 GLY C -6
REMARK 465 ARG C -5
REMARK 465 HIS C -4
REMARK 465 MET D -24
REMARK 465 GLY D -23
REMARK 465 HIS D -22
REMARK 465 HIS D -21
REMARK 465 GLY D -6
REMARK 465 ARG D -5
REMARK 465 HIS D -4
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 GLU A 47 CD OE1 OE2
REMARK 470 GLU A 48 OE1 OE2
REMARK 470 GLU A 84 CG CD OE1 OE2
REMARK 470 LYS A 136 CE NZ
REMARK 470 GLU A 140 OE1 OE2
REMARK 470 ARG A 153 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 154 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 175 CD CE NZ
REMARK 470 ARG A 176 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 183 CG CD OE1 OE2
REMARK 470 LYS A 190 CD CE NZ
REMARK 470 LYS A 191 CG CD CE NZ
REMARK 470 GLN A 253 CG CD OE1 NE2
REMARK 470 ARG A 260 NE CZ NH1 NH2
REMARK 470 GLU A 327 CG CD OE1 OE2
REMARK 470 GLU A 336 CD OE1 OE2
REMARK 470 ASP A 343 CG OD1 OD2
REMARK 470 GLU A 366 CG CD OE1 OE2
REMARK 470 GLU A 379 CG CD OE1 OE2
REMARK 470 ARG A 381 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 47 CG CD OE1 OE2
REMARK 470 GLU B 48 OE1 OE2
REMARK 470 ARG B 65 CD NE CZ NH1 NH2
REMARK 470 GLU B 84 CG CD OE1 OE2
REMARK 470 LYS B 136 CE NZ
REMARK 470 GLU B 140 CG CD OE1 OE2
REMARK 470 ARG B 154 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 156 NZ
REMARK 470 LYS B 175 CG CD CE NZ
REMARK 470 ARG B 176 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 183 CG CD OE1 OE2
REMARK 470 LYS B 190 CG CD CE NZ
REMARK 470 LYS B 191 CG CD CE NZ
REMARK 470 GLN B 253 CG CD OE1 NE2
REMARK 470 ARG B 260 CD NE CZ NH1 NH2
REMARK 470 GLU B 262 CG CD OE1 OE2
REMARK 470 GLU B 327 CG CD OE1 OE2
REMARK 470 GLU B 366 CG CD OE1 OE2
REMARK 470 GLU B 379 CG CD OE1 OE2
REMARK 470 ILE C -8 CG1 CG2 CD1
REMARK 470 HIS D -20 CG ND1 CD2 CE1 NE2
REMARK 470 GLU D -7 CG CD OE1 OE2
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 239 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 239 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 246 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 246 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG B 239 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG B 239 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG B 246 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG B 246 NE - CZ - NH2 ANGL. DEV. = 3.4 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 PRO A 64 47.70 -77.44
REMARK 500 LYS A 156 -127.30 53.35
REMARK 500 SER A 205 155.97 176.51
REMARK 500 PRO B 64 47.07 -76.65
REMARK 500 LYS B 156 -128.48 51.83
REMARK 500 SER B 205 155.55 173.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 GDD A 701
REMARK 610 GDD B 701
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDD A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDD B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3OKC RELATED DB: PDB
REMARK 900 PIMB' BOUND TO GDP (ORTHORHOMBIC CRYSTAL FORM)
REMARK 900 RELATED ID: 3OKP RELATED DB: PDB
REMARK 900 PIMB' BOUND TO GDP-MAN (ORTHORHOMBIC CRYSTAL FORM)
DBREF 3OKA A 1 381 UNP Q8NNK8 PIMB_CORGL 1 381
DBREF 3OKA B 1 381 UNP Q8NNK8 PIMB_CORGL 1 381
DBREF 3OKA C -24 -4 PDB 3OKA 3OKA -24 -4
DBREF 3OKA D -24 -4 PDB 3OKA 3OKA -24 -4
SEQRES 1 A 381 MET SER ALA SER ARG LYS THR LEU VAL VAL THR ASN ASP
SEQRES 2 A 381 PHE PRO PRO ARG ILE GLY GLY ILE GLN SER TYR LEU ARG
SEQRES 3 A 381 ASP PHE ILE ALA THR GLN ASP PRO GLU SER ILE VAL VAL
SEQRES 4 A 381 PHE ALA SER THR GLN ASN ALA GLU GLU ALA HIS ALA TYR
SEQRES 5 A 381 ASP LYS THR LEU ASP TYR GLU VAL ILE ARG TRP PRO ARG
SEQRES 6 A 381 SER VAL MET LEU PRO THR PRO THR THR ALA HIS ALA MET
SEQRES 7 A 381 ALA GLU ILE ILE ARG GLU ARG GLU ILE ASP ASN VAL TRP
SEQRES 8 A 381 PHE GLY ALA ALA ALA PRO LEU ALA LEU MET ALA GLY THR
SEQRES 9 A 381 ALA LYS GLN ALA GLY ALA SER LYS VAL ILE ALA SER THR
SEQRES 10 A 381 HIS GLY HIS GLU VAL GLY TRP SER MET LEU PRO GLY SER
SEQRES 11 A 381 ARG GLN SER LEU ARG LYS ILE GLY THR GLU VAL ASP VAL
SEQRES 12 A 381 LEU THR TYR ILE SER GLN TYR THR LEU ARG ARG PHE LYS
SEQRES 13 A 381 SER ALA PHE GLY SER HIS PRO THR PHE GLU HIS LEU PRO
SEQRES 14 A 381 SER GLY VAL ASP VAL LYS ARG PHE THR PRO ALA THR PRO
SEQRES 15 A 381 GLU ASP LYS SER ALA THR ARG LYS LYS LEU GLY PHE THR
SEQRES 16 A 381 ASP THR THR PRO VAL ILE ALA CYS ASN SER ARG LEU VAL
SEQRES 17 A 381 PRO ARG LYS GLY GLN ASP SER LEU ILE LYS ALA MET PRO
SEQRES 18 A 381 GLN VAL ILE ALA ALA ARG PRO ASP ALA GLN LEU LEU ILE
SEQRES 19 A 381 VAL GLY SER GLY ARG TYR GLU SER THR LEU ARG ARG LEU
SEQRES 20 A 381 ALA THR ASP VAL SER GLN ASN VAL LYS PHE LEU GLY ARG
SEQRES 21 A 381 LEU GLU TYR GLN ASP MET ILE ASN THR LEU ALA ALA ALA
SEQRES 22 A 381 ASP ILE PHE ALA MET PRO ALA ARG THR ARG GLY GLY GLY
SEQRES 23 A 381 LEU ASP VAL GLU GLY LEU GLY ILE VAL TYR LEU GLU ALA
SEQRES 24 A 381 GLN ALA CYS GLY VAL PRO VAL ILE ALA GLY THR SER GLY
SEQRES 25 A 381 GLY ALA PRO GLU THR VAL THR PRO ALA THR GLY LEU VAL
SEQRES 26 A 381 VAL GLU GLY SER ASP VAL ASP LYS LEU SER GLU LEU LEU
SEQRES 27 A 381 ILE GLU LEU LEU ASP ASP PRO ILE ARG ARG ALA ALA MET
SEQRES 28 A 381 GLY ALA ALA GLY ARG ALA HIS VAL GLU ALA GLU TRP SER
SEQRES 29 A 381 TRP GLU ILE MET GLY GLU ARG LEU THR ASN ILE LEU GLN
SEQRES 30 A 381 SER GLU PRO ARG
SEQRES 1 B 381 MET SER ALA SER ARG LYS THR LEU VAL VAL THR ASN ASP
SEQRES 2 B 381 PHE PRO PRO ARG ILE GLY GLY ILE GLN SER TYR LEU ARG
SEQRES 3 B 381 ASP PHE ILE ALA THR GLN ASP PRO GLU SER ILE VAL VAL
SEQRES 4 B 381 PHE ALA SER THR GLN ASN ALA GLU GLU ALA HIS ALA TYR
SEQRES 5 B 381 ASP LYS THR LEU ASP TYR GLU VAL ILE ARG TRP PRO ARG
SEQRES 6 B 381 SER VAL MET LEU PRO THR PRO THR THR ALA HIS ALA MET
SEQRES 7 B 381 ALA GLU ILE ILE ARG GLU ARG GLU ILE ASP ASN VAL TRP
SEQRES 8 B 381 PHE GLY ALA ALA ALA PRO LEU ALA LEU MET ALA GLY THR
SEQRES 9 B 381 ALA LYS GLN ALA GLY ALA SER LYS VAL ILE ALA SER THR
SEQRES 10 B 381 HIS GLY HIS GLU VAL GLY TRP SER MET LEU PRO GLY SER
SEQRES 11 B 381 ARG GLN SER LEU ARG LYS ILE GLY THR GLU VAL ASP VAL
SEQRES 12 B 381 LEU THR TYR ILE SER GLN TYR THR LEU ARG ARG PHE LYS
SEQRES 13 B 381 SER ALA PHE GLY SER HIS PRO THR PHE GLU HIS LEU PRO
SEQRES 14 B 381 SER GLY VAL ASP VAL LYS ARG PHE THR PRO ALA THR PRO
SEQRES 15 B 381 GLU ASP LYS SER ALA THR ARG LYS LYS LEU GLY PHE THR
SEQRES 16 B 381 ASP THR THR PRO VAL ILE ALA CYS ASN SER ARG LEU VAL
SEQRES 17 B 381 PRO ARG LYS GLY GLN ASP SER LEU ILE LYS ALA MET PRO
SEQRES 18 B 381 GLN VAL ILE ALA ALA ARG PRO ASP ALA GLN LEU LEU ILE
SEQRES 19 B 381 VAL GLY SER GLY ARG TYR GLU SER THR LEU ARG ARG LEU
SEQRES 20 B 381 ALA THR ASP VAL SER GLN ASN VAL LYS PHE LEU GLY ARG
SEQRES 21 B 381 LEU GLU TYR GLN ASP MET ILE ASN THR LEU ALA ALA ALA
SEQRES 22 B 381 ASP ILE PHE ALA MET PRO ALA ARG THR ARG GLY GLY GLY
SEQRES 23 B 381 LEU ASP VAL GLU GLY LEU GLY ILE VAL TYR LEU GLU ALA
SEQRES 24 B 381 GLN ALA CYS GLY VAL PRO VAL ILE ALA GLY THR SER GLY
SEQRES 25 B 381 GLY ALA PRO GLU THR VAL THR PRO ALA THR GLY LEU VAL
SEQRES 26 B 381 VAL GLU GLY SER ASP VAL ASP LYS LEU SER GLU LEU LEU
SEQRES 27 B 381 ILE GLU LEU LEU ASP ASP PRO ILE ARG ARG ALA ALA MET
SEQRES 28 B 381 GLY ALA ALA GLY ARG ALA HIS VAL GLU ALA GLU TRP SER
SEQRES 29 B 381 TRP GLU ILE MET GLY GLU ARG LEU THR ASN ILE LEU GLN
SEQRES 30 B 381 SER GLU PRO ARG
SEQRES 1 C 21 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 C 21 SER GLY HIS ILE GLU GLY ARG HIS
SEQRES 1 D 21 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 D 21 SER GLY HIS ILE GLU GLY ARG HIS
HET SO4 A 601 5
HET SO4 A 602 5
HET SO4 A 603 5
HET GDD A 701 28
HET GOL A 801 6
HET SO4 B 601 5
HET SO4 B 602 5
HET SO4 B 603 5
HET SO4 B 604 5
HET GDD B 701 28
HET SO4 C 700 5
HET SO4 D 702 5
HET SO4 D 701 5
HETNAM SO4 SULFATE ION
HETNAM GDD GUANOSINE-5'-DIPHOSPHATE-ALPHA-D-MANNOSE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 SO4 10(O4 S 2-)
FORMUL 8 GDD 2(C16 H25 N5 O16 P2)
FORMUL 9 GOL C3 H8 O3
FORMUL 18 HOH *294(H2 O)
HELIX 1 1 GLY A 19 THR A 31 1 13
HELIX 2 2 GLN A 32 GLU A 35 5 4
HELIX 3 3 ASN A 45 LYS A 54 1 10
HELIX 4 4 THR A 71 ARG A 85 1 15
HELIX 5 5 PRO A 97 LEU A 100 5 4
HELIX 6 6 MET A 101 ALA A 108 1 8
HELIX 7 7 GLY A 129 VAL A 141 1 13
HELIX 8 8 SER A 148 LYS A 156 1 9
HELIX 9 9 THR A 181 GLY A 193 1 13
HELIX 10 10 VAL A 208 LYS A 211 5 4
HELIX 11 11 GLY A 212 ARG A 227 1 16
HELIX 12 12 TYR A 240 ALA A 248 1 9
HELIX 13 13 THR A 249 GLN A 253 5 5
HELIX 14 14 GLU A 262 ALA A 273 1 12
HELIX 15 15 ARG A 283 LEU A 287 5 5
HELIX 16 16 GLY A 293 CYS A 302 1 10
HELIX 17 17 GLY A 313 VAL A 318 5 6
HELIX 18 18 ASP A 330 ASP A 343 1 14
HELIX 19 19 ASP A 344 TRP A 363 1 20
HELIX 20 20 SER A 364 SER A 378 1 15
HELIX 21 21 GLY B 19 THR B 31 1 13
HELIX 22 22 GLN B 32 GLU B 35 5 4
HELIX 23 23 ASN B 45 THR B 55 1 11
HELIX 24 24 THR B 71 ARG B 85 1 15
HELIX 25 25 PRO B 97 LEU B 100 5 4
HELIX 26 26 MET B 101 ALA B 108 1 8
HELIX 27 27 GLY B 129 VAL B 141 1 13
HELIX 28 28 SER B 148 LYS B 156 1 9
HELIX 29 29 THR B 181 GLY B 193 1 13
HELIX 30 30 VAL B 208 LYS B 211 5 4
HELIX 31 31 GLY B 212 ARG B 227 1 16
HELIX 32 32 TYR B 240 ALA B 248 1 9
HELIX 33 33 THR B 249 GLN B 253 5 5
HELIX 34 34 GLU B 262 ALA B 272 1 11
HELIX 35 35 ARG B 283 LEU B 287 5 5
HELIX 36 36 GLY B 293 CYS B 302 1 10
HELIX 37 37 GLY B 313 VAL B 318 5 6
HELIX 38 38 ASP B 330 ASP B 343 1 14
HELIX 39 39 ASP B 344 TRP B 363 1 20
HELIX 40 40 SER B 364 SER B 378 1 15
SHEET 1 A 7 GLU A 59 TRP A 63 0
SHEET 2 A 7 ILE A 37 SER A 42 1 N VAL A 39 O ILE A 61
SHEET 3 A 7 THR A 7 THR A 11 1 N VAL A 9 O PHE A 40
SHEET 4 A 7 ASN A 89 PHE A 92 1 O TRP A 91 N LEU A 8
SHEET 5 A 7 LYS A 112 SER A 116 1 O ILE A 114 N PHE A 92
SHEET 6 A 7 VAL A 143 TYR A 146 1 O VAL A 143 N ALA A 115
SHEET 7 A 7 THR A 164 HIS A 167 1 O THR A 164 N LEU A 144
SHEET 1 B 6 VAL A 255 GLY A 259 0
SHEET 2 B 6 GLN A 231 VAL A 235 1 N ILE A 234 O LYS A 256
SHEET 3 B 6 VAL A 200 ASN A 204 1 N ILE A 201 O LEU A 233
SHEET 4 B 6 ILE A 275 MET A 278 1 O ALA A 277 N ALA A 202
SHEET 5 B 6 VAL A 306 GLY A 309 1 O ILE A 307 N MET A 278
SHEET 6 B 6 GLY A 323 VAL A 326 1 O VAL A 326 N ALA A 308
SHEET 1 C 7 GLU B 59 TRP B 63 0
SHEET 2 C 7 ILE B 37 SER B 42 1 N VAL B 39 O ILE B 61
SHEET 3 C 7 THR B 7 THR B 11 1 N VAL B 9 O PHE B 40
SHEET 4 C 7 ASN B 89 PHE B 92 1 O TRP B 91 N LEU B 8
SHEET 5 C 7 LYS B 112 SER B 116 1 O ILE B 114 N PHE B 92
SHEET 6 C 7 VAL B 143 TYR B 146 1 O VAL B 143 N ALA B 115
SHEET 7 C 7 THR B 164 HIS B 167 1 O THR B 164 N LEU B 144
SHEET 1 D 6 VAL B 255 GLY B 259 0
SHEET 2 D 6 GLN B 231 VAL B 235 1 N ILE B 234 O LYS B 256
SHEET 3 D 6 VAL B 200 ASN B 204 1 N ILE B 201 O LEU B 233
SHEET 4 D 6 ILE B 275 MET B 278 1 O ILE B 275 N ALA B 202
SHEET 5 D 6 VAL B 306 GLY B 309 1 O ILE B 307 N PHE B 276
SHEET 6 D 6 GLY B 323 VAL B 326 1 O VAL B 326 N ALA B 308
CISPEP 1 PRO A 15 PRO A 16 0 7.98
CISPEP 2 ALA A 96 PRO A 97 0 1.52
CISPEP 3 PRO B 15 PRO B 16 0 7.51
CISPEP 4 ALA B 96 PRO B 97 0 1.82
SITE 1 AC1 6 ARG A 206 ARG A 210 ARG A 239 HOH A 387
SITE 2 AC1 6 HOH A 437 HIS D -19
SITE 1 AC2 6 LYS A 54 PRO A 209 ARG A 239 ARG A 283
SITE 2 AC2 6 HOH A 451 HIS D -19
SITE 1 AC3 5 PRO A 128 GLY A 129 SER A 130 ARG A 131
SITE 2 AC3 5 GLN A 132
SITE 1 AC4 11 ARG A 206 ARG A 210 LYS A 211 VAL A 235
SITE 2 AC4 11 GLY A 236 ARG A 260 LEU A 261 MET A 266
SITE 3 AC4 11 GLU A 298 HOH A 533 HOH A 536
SITE 1 AC5 4 THR A 71 THR A 73 GLU A 360 HOH A 535
SITE 1 AC6 4 ARG B 206 ARG B 210 ARG B 239 HOH B 389
SITE 1 AC7 3 LYS B 54 ARG B 239 ARG B 283
SITE 1 AC8 5 PRO B 128 GLY B 129 SER B 130 ARG B 131
SITE 2 AC8 5 GLN B 132
SITE 1 AC9 4 HIS B 50 LYS B 54 HIS C -17 HIS C -18
SITE 1 BC1 11 ARG B 206 LYS B 211 VAL B 235 GLY B 236
SITE 2 BC1 11 ARG B 260 LEU B 261 TYR B 263 MET B 266
SITE 3 BC1 11 GLU B 298 HOH B 507 HOH B 510
SITE 1 BC2 3 HIS C -15 HIS C -14 HIS C -16
SITE 1 BC3 5 HIS A 50 LYS A 54 HIS D -17 HIS D -19
SITE 2 BC3 5 HIS D -18
SITE 1 BC4 3 HIS D -14 HIS D -15 HIS D -16
CRYST1 44.070 50.020 85.300 92.05 92.68 89.94 P 1 2
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 0.022691 -0.000023 0.001064 0.00000
SCALE2 0.000000 0.019992 0.000717 0.00000
SCALE3 0.000000 0.000000 0.011744 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
