HEADER TRANSFERASE 09-JAN-09 3FS2
TITLE CRYSTAL STRUCTURE OF 2-DEHYDRO-3-DEOXYPHOSPHOOCTONATE ALDOLASE FROM
TITLE 2 BRUCIELLA MELITENSIS AT 1.85A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-DEHYDRO-3-DEOXYPHOSPHOOCTONATE ALDOLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PHOSPHO-2-DEHYDRO-3-DEOXYOCTONATE ALDOLASE, 3-DEOXY-D-MANNO-
COMPND 5 OCTULOSONIC ACID 8-PHOSPHATE SYNTHETASE, KDO-8-PHOSPHATE SYNTHETASE,
COMPND 6 KDO 8-P SYNTHASE, KDOPS;
COMPND 7 EC: 2.5.1.55;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BRUCELLA MELITENSIS;
SOURCE 3 ORGANISM_TAXID: 29459;
SOURCE 4 STRAIN: BIOVAR ABORTUS 2308;
SOURCE 5 GENE: 3787797, BMEI0850, KDSA;
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: AVA0421
KEYWDS SSGCID, BRUCIELLLA MELITENSIS, DAHP SYNTHETASE I, 2-DEHYDRO-3-
KEYWDS 2 DEOXYPHOSPHOOCTONATE ALDOLASE, CYTOPLASM, LIPOPOLYSACCHARIDE
KEYWDS 3 BIOSYNTHESIS, TRANSFERASE, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL
KEYWDS 4 GENOMICS CENTER FOR INFECTIOUS DISEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SSGCID,SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE
AUTHOR 2 (SSGCID)
REVDAT 3 06-SEP-23 3FS2 1 REMARK SEQADV
REVDAT 2 24-JAN-18 3FS2 1 AUTHOR JRNL
REVDAT 1 20-JAN-09 3FS2 0
JRNL AUTH SSGCID
JRNL TITL CRYSTAL STRUCTURE OF 2-DEHYDRO-3-DEOXYPHOSPHOOCTONATE
JRNL TITL 2 ALDOLASE FROM BRUCIELLA MELITENSIS AT 1.85A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0070
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 45914
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 2366
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2820
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.3250
REMARK 3 BIN FREE R VALUE SET COUNT : 169
REMARK 3 BIN FREE R VALUE : 0.3510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3767
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 313
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.18000
REMARK 3 B22 (A**2) : 0.39000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.18000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.131
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.130
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.085
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.826
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3880 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2579 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5257 ; 1.591 ; 1.981
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6341 ; 0.993 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 506 ; 5.994 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 143 ;32.924 ;24.476
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 634 ;13.109 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;18.241 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 625 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4267 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 726 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 2531 ; 1.007 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1021 ; 0.275 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4056 ; 1.773 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1349 ; 2.682 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1198 ; 4.376 ; 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 : 1.20
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
REMARK 4
REMARK 4 3FS2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-09.
REMARK 100 THE DEPOSITION ID IS D_1000050971.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 4.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : WESTBROOK NOIR
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45916
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.48100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB COORDINATE SET 1FWS, MONOMER AFTER SIDECHAIN
REMARK 200 ADJUSTMENT WITH CHAINSAW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: JCSG+ SCREEN D3: 100MM NA/K PHOSPHATE
REMARK 280 PH 6.2, 50% PEG 200, 200MM NACL, PH 5.5, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 290K, VAPOR DIFFUSION, SITTING DROP, PH 5.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 60.76500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.82000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 60.76500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.82000
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 1810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 433 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -20
REMARK 465 ALA A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 MET A -12
REMARK 465 GLY A -11
REMARK 465 THR A -10
REMARK 465 LEU A -9
REMARK 465 GLU A -8
REMARK 465 ALA A -7
REMARK 465 GLN A -6
REMARK 465 THR A -5
REMARK 465 GLN A -4
REMARK 465 GLY A -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 VAL A 2
REMARK 465 ARG A 65
REMARK 465 THR A 66
REMARK 465 SER A 67
REMARK 465 LEU A 68
REMARK 465 LYS A 69
REMARK 465 ALA A 70
REMARK 465 ALA A 71
REMARK 465 ARG A 72
REMARK 465 GLY A 73
REMARK 465 GLY A 209
REMARK 465 GLN A 210
REMARK 465 GLY A 211
REMARK 465 GLY A 212
REMARK 465 SER A 213
REMARK 465 THR A 214
REMARK 465 GLY A 215
REMARK 465 GLY A 216
REMARK 465 MET B -20
REMARK 465 ALA B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 MET B -12
REMARK 465 GLY B -11
REMARK 465 THR B -10
REMARK 465 LEU B -9
REMARK 465 GLU B -8
REMARK 465 ALA B -7
REMARK 465 GLN B -6
REMARK 465 THR B -5
REMARK 465 GLN B -4
REMARK 465 GLY B -3
REMARK 465 PRO B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 ASP B 61
REMARK 465 LYS B 62
REMARK 465 ALA B 63
REMARK 465 ASN B 64
REMARK 465 ARG B 65
REMARK 465 THR B 66
REMARK 465 SER B 67
REMARK 465 LEU B 68
REMARK 465 LYS B 69
REMARK 465 ALA B 70
REMARK 465 ALA B 71
REMARK 465 ARG B 72
REMARK 465 GLY B 73
REMARK 465 ILE B 74
REMARK 465 GLY B 75
REMARK 465 GLY B 209
REMARK 465 GLN B 210
REMARK 465 GLY B 211
REMARK 465 GLY B 212
REMARK 465 SER B 213
REMARK 465 THR B 214
REMARK 465 GLY B 215
REMARK 465 GLY B 216
REMARK 465 PRO B 248
REMARK 465 SER B 249
REMARK 465 ASP B 250
REMARK 465 GLY B 251
REMARK 465 PRO B 252
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 ASN A 64 CG OD1 ND2
REMARK 470 ILE A 74 CG1 CG2 CD1
REMARK 470 GLU A 77 CG CD OE1 OE2
REMARK 470 GLU A 81 CG CD OE1 OE2
REMARK 470 GLN A 217 CG CD OE1 NE2
REMARK 470 GLU A 219 CG CD OE1 OE2
REMARK 470 ASP A 250 CG OD1 OD2
REMARK 470 GLN B 29 CG CD OE1 NE2
REMARK 470 PHE B 60 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 77 CG CD OE1 OE2
REMARK 470 LYS B 78 CG CD CE NZ
REMARK 470 GLU B 81 CG CD OE1 OE2
REMARK 470 LYS B 88 CG CD CE NZ
REMARK 470 GLN B 217 CG CD OE1 NE2
REMARK 470 ARG B 218 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 219 CG CD OE1 OE2
REMARK 470 ASN B 253 CG OD1 ND2
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 342 O HOH A 347 2.03
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 O HOH A 342 O HOH A 342 2555 1.48
REMARK 500 O HOH A 402 O HOH B 376 2555 2.18
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 LEU A 21 CA - CB - CG ANGL. DEV. = 18.2 DEGREES
REMARK 500 ARG A 272 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 LEU B 21 CA - CB - CG ANGL. DEV. = 16.2 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 21 137.97 -39.22
REMARK 500 GLU A 31 -133.31 -112.49
REMARK 500 ALA A 63 -38.45 -138.95
REMARK 500 GLU B 31 -81.77 -100.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 61 LYS A 62 -146.04
REMARK 500 ALA A 63 ASN A 64 148.44
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 PG4 A 279
REMARK 610 PG4 A 280
REMARK 610 PG4 B 279
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 278
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 280
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 278
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 279
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: BRABA.00102.A RELATED DB: TARGETDB
DBREF 3FS2 A 1 277 UNP Q8YHF1 KDSA_BRUME 1 277
DBREF 3FS2 B 1 277 UNP Q8YHF1 KDSA_BRUME 1 277
SEQADV 3FS2 MET A -20 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 ALA A -19 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 HIS A -18 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 HIS A -17 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 HIS A -16 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 HIS A -15 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 HIS A -14 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 HIS A -13 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 MET A -12 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 GLY A -11 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 THR A -10 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 LEU A -9 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 GLU A -8 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 ALA A -7 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 GLN A -6 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 THR A -5 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 GLN A -4 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 GLY A -3 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 PRO A -2 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 GLY A -1 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 SER A 0 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 PHE A 236 UNP Q8YHF1 LEU 236 CONFLICT
SEQADV 3FS2 MET B -20 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 ALA B -19 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 HIS B -18 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 HIS B -17 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 HIS B -16 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 HIS B -15 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 HIS B -14 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 HIS B -13 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 MET B -12 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 GLY B -11 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 THR B -10 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 LEU B -9 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 GLU B -8 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 ALA B -7 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 GLN B -6 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 THR B -5 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 GLN B -4 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 GLY B -3 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 PRO B -2 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 GLY B -1 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 SER B 0 UNP Q8YHF1 EXPRESSION TAG
SEQADV 3FS2 PHE B 236 UNP Q8YHF1 LEU 236 CONFLICT
SEQRES 1 A 298 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 A 298 ALA GLN THR GLN GLY PRO GLY SER MET VAL THR ALA ASN
SEQRES 3 A 298 SER THR VAL LYS VAL GLY ASN VAL THR PHE SER ASN SER
SEQRES 4 A 298 ALA PRO LEU ALA LEU ILE ALA GLY PRO CYS GLN MET GLU
SEQRES 5 A 298 THR ARG ASP HIS ALA PHE GLU MET ALA GLY ARG LEU LYS
SEQRES 6 A 298 GLU MET THR ASP LYS LEU GLY ILE GLY LEU VAL TYR LYS
SEQRES 7 A 298 SER SER PHE ASP LYS ALA ASN ARG THR SER LEU LYS ALA
SEQRES 8 A 298 ALA ARG GLY ILE GLY LEU GLU LYS ALA LEU GLU VAL PHE
SEQRES 9 A 298 SER ASP LEU LYS LYS GLU TYR GLY PHE PRO VAL LEU THR
SEQRES 10 A 298 ASP ILE HIS THR GLU GLU GLN CYS ALA ALA VAL ALA PRO
SEQRES 11 A 298 VAL VAL ASP VAL LEU GLN ILE PRO ALA PHE LEU CYS ARG
SEQRES 12 A 298 GLN THR ASP LEU LEU ILE ALA ALA ALA ARG THR GLY ARG
SEQRES 13 A 298 VAL VAL ASN VAL LYS LYS GLY GLN PHE LEU ALA PRO TRP
SEQRES 14 A 298 ASP MET LYS ASN VAL LEU ALA LYS ILE THR GLU SER GLY
SEQRES 15 A 298 ASN PRO ASN VAL LEU ALA THR GLU ARG GLY VAL SER PHE
SEQRES 16 A 298 GLY TYR ASN THR LEU VAL SER ASP MET ARG ALA LEU PRO
SEQRES 17 A 298 ILE MET ALA GLY LEU GLY ALA PRO VAL ILE PHE ASP ALA
SEQRES 18 A 298 THR HIS SER VAL GLN GLN PRO GLY GLY GLN GLY GLY SER
SEQRES 19 A 298 THR GLY GLY GLN ARG GLU PHE VAL GLU THR LEU ALA ARG
SEQRES 20 A 298 ALA ALA VAL ALA VAL GLY VAL ALA GLY PHE PHE ILE GLU
SEQRES 21 A 298 THR HIS GLU ASP PRO ASP ASN ALA PRO SER ASP GLY PRO
SEQRES 22 A 298 ASN MET VAL PRO ILE ASP LYS MET PRO ALA LEU LEU GLU
SEQRES 23 A 298 LYS LEU MET ALA PHE ASP ARG ILE ALA LYS ALA LEU
SEQRES 1 B 298 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 B 298 ALA GLN THR GLN GLY PRO GLY SER MET VAL THR ALA ASN
SEQRES 3 B 298 SER THR VAL LYS VAL GLY ASN VAL THR PHE SER ASN SER
SEQRES 4 B 298 ALA PRO LEU ALA LEU ILE ALA GLY PRO CYS GLN MET GLU
SEQRES 5 B 298 THR ARG ASP HIS ALA PHE GLU MET ALA GLY ARG LEU LYS
SEQRES 6 B 298 GLU MET THR ASP LYS LEU GLY ILE GLY LEU VAL TYR LYS
SEQRES 7 B 298 SER SER PHE ASP LYS ALA ASN ARG THR SER LEU LYS ALA
SEQRES 8 B 298 ALA ARG GLY ILE GLY LEU GLU LYS ALA LEU GLU VAL PHE
SEQRES 9 B 298 SER ASP LEU LYS LYS GLU TYR GLY PHE PRO VAL LEU THR
SEQRES 10 B 298 ASP ILE HIS THR GLU GLU GLN CYS ALA ALA VAL ALA PRO
SEQRES 11 B 298 VAL VAL ASP VAL LEU GLN ILE PRO ALA PHE LEU CYS ARG
SEQRES 12 B 298 GLN THR ASP LEU LEU ILE ALA ALA ALA ARG THR GLY ARG
SEQRES 13 B 298 VAL VAL ASN VAL LYS LYS GLY GLN PHE LEU ALA PRO TRP
SEQRES 14 B 298 ASP MET LYS ASN VAL LEU ALA LYS ILE THR GLU SER GLY
SEQRES 15 B 298 ASN PRO ASN VAL LEU ALA THR GLU ARG GLY VAL SER PHE
SEQRES 16 B 298 GLY TYR ASN THR LEU VAL SER ASP MET ARG ALA LEU PRO
SEQRES 17 B 298 ILE MET ALA GLY LEU GLY ALA PRO VAL ILE PHE ASP ALA
SEQRES 18 B 298 THR HIS SER VAL GLN GLN PRO GLY GLY GLN GLY GLY SER
SEQRES 19 B 298 THR GLY GLY GLN ARG GLU PHE VAL GLU THR LEU ALA ARG
SEQRES 20 B 298 ALA ALA VAL ALA VAL GLY VAL ALA GLY PHE PHE ILE GLU
SEQRES 21 B 298 THR HIS GLU ASP PRO ASP ASN ALA PRO SER ASP GLY PRO
SEQRES 22 B 298 ASN MET VAL PRO ILE ASP LYS MET PRO ALA LEU LEU GLU
SEQRES 23 B 298 LYS LEU MET ALA PHE ASP ARG ILE ALA LYS ALA LEU
HET PO4 A 278 5
HET PG4 A 279 10
HET PG4 A 280 10
HET PO4 B 278 5
HET PG4 B 279 10
HETNAM PO4 PHOSPHATE ION
HETNAM PG4 TETRAETHYLENE GLYCOL
FORMUL 3 PO4 2(O4 P 3-)
FORMUL 4 PG4 3(C8 H18 O5)
FORMUL 8 HOH *313(H2 O)
HELIX 1 1 THR A 32 GLY A 51 1 20
HELIX 2 2 GLY A 75 GLY A 91 1 17
HELIX 3 3 THR A 100 ALA A 108 1 9
HELIX 4 4 PRO A 117 CYS A 121 5 5
HELIX 5 5 GLN A 123 THR A 133 1 11
HELIX 6 6 ALA A 146 TRP A 148 5 3
HELIX 7 7 ASP A 149 GLU A 159 1 11
HELIX 8 8 ARG A 184 GLY A 191 1 8
HELIX 9 9 ALA A 200 VAL A 204 1 5
HELIX 10 10 GLN A 217 GLU A 219 5 3
HELIX 11 11 PHE A 220 GLY A 232 1 13
HELIX 12 12 ASP A 243 ALA A 247 5 5
HELIX 13 13 ASP A 250 MET A 254 5 5
HELIX 14 14 LYS A 259 LYS A 275 1 17
HELIX 15 15 THR B 32 GLY B 51 1 20
HELIX 16 16 LEU B 76 GLY B 91 1 16
HELIX 17 17 THR B 100 ALA B 108 1 9
HELIX 18 18 PRO B 117 CYS B 121 5 5
HELIX 19 19 GLN B 123 THR B 133 1 11
HELIX 20 20 ALA B 146 TRP B 148 5 3
HELIX 21 21 ASP B 149 GLU B 159 1 11
HELIX 22 22 ARG B 184 LEU B 192 1 9
HELIX 23 23 ALA B 200 VAL B 204 1 5
HELIX 24 24 GLN B 217 GLU B 219 5 3
HELIX 25 25 PHE B 220 GLY B 232 1 13
HELIX 26 26 ASP B 243 ALA B 247 5 5
HELIX 27 27 LYS B 259 LEU B 277 1 19
SHEET 1 A 2 VAL A 8 VAL A 10 0
SHEET 2 A 2 VAL A 13 PHE A 15 -1 O PHE A 15 N VAL A 8
SHEET 1 B10 VAL A 255 PRO A 256 0
SHEET 2 B10 GLY A 235 HIS A 241 1 N GLU A 239 O VAL A 255
SHEET 3 B10 VAL A 196 ASP A 199 1 N PHE A 198 O PHE A 237
SHEET 4 B10 VAL A 165 GLU A 169 1 N ALA A 167 O ILE A 197
SHEET 5 B10 VAL A 136 LYS A 140 1 N VAL A 139 O LEU A 166
SHEET 6 B10 VAL A 113 ILE A 116 1 N LEU A 114 O VAL A 136
SHEET 7 B10 VAL A 94 ASP A 97 1 N THR A 96 O GLN A 115
SHEET 8 B10 LEU A 54 LYS A 57 1 N TYR A 56 O LEU A 95
SHEET 9 B10 ALA A 22 GLY A 26 1 N LEU A 23 O VAL A 55
SHEET 10 B10 GLY A 235 HIS A 241 1 O PHE A 236 N ILE A 24
SHEET 1 C 2 VAL A 172 SER A 173 0
SHEET 2 C 2 LEU A 179 VAL A 180 -1 O VAL A 180 N VAL A 172
SHEET 1 D 2 THR B 7 VAL B 10 0
SHEET 2 D 2 VAL B 13 SER B 16 -1 O VAL B 13 N VAL B 10
SHEET 1 E10 VAL B 255 PRO B 256 0
SHEET 2 E10 GLY B 235 HIS B 241 1 N GLU B 239 O VAL B 255
SHEET 3 E10 VAL B 196 ASP B 199 1 N PHE B 198 O PHE B 237
SHEET 4 E10 VAL B 165 GLU B 169 1 N GLU B 169 O ILE B 197
SHEET 5 E10 VAL B 136 LYS B 140 1 N VAL B 139 O THR B 168
SHEET 6 E10 VAL B 113 ILE B 116 1 N LEU B 114 O VAL B 136
SHEET 7 E10 VAL B 94 ASP B 97 1 N THR B 96 O GLN B 115
SHEET 8 E10 LEU B 54 LYS B 57 1 N TYR B 56 O LEU B 95
SHEET 9 E10 ALA B 22 GLY B 26 1 N LEU B 23 O VAL B 55
SHEET 10 E10 GLY B 235 HIS B 241 1 O PHE B 236 N ILE B 24
SHEET 1 F 2 VAL B 172 SER B 173 0
SHEET 2 F 2 LEU B 179 VAL B 180 -1 O VAL B 180 N VAL B 172
CISPEP 1 LYS A 62 ALA A 63 0 -9.39
SITE 1 AC1 9 PRO A 117 ALA A 118 LYS A 140 ARG A 170
SITE 2 AC1 9 HIS A 202 HOH A 320 HOH A 373 HOH A 375
SITE 3 AC1 9 HOH A 391
SITE 1 AC2 10 LYS A 87 LYS A 88 GLU A 89 TYR A 90
SITE 2 AC2 10 GLY A 91 HOH A 316 HOH A 346 PRO B 20
SITE 3 AC2 10 ARG B 272 HOH B 419
SITE 1 AC3 7 ALA A 131 ARG A 132 GLY A 134 GLY A 161
SITE 2 AC3 7 ASN A 246 ALA A 247 PRO A 248
SITE 1 AC4 7 PRO B 117 ALA B 118 LYS B 140 ARG B 170
SITE 2 AC4 7 HIS B 202 HOH B 346 HOH B 347
SITE 1 AC5 7 ASN A 12 GLY A 51 GLY A 53 ILE A 273
SITE 2 AC5 7 GLU B 265 HOH B 301 HOH B 315
CRYST1 121.530 75.640 74.650 90.00 126.00 90.00 C 1 2 1 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 0.008228 0.000000 0.005979 0.00000
SCALE2 0.000000 0.013221 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016559 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
