HEADER TRANSFERASE 03-DEC-14 4UCG
TITLE NMEDAH7PS R126S VARIANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: 3-DEOXY-D-ARABINO-HEPTULOSONATE 7-PHOSPHATE SYNTHASE, DAHP
COMPND 5 SYNTHASE, PHOSPHO-2-KETO-3-DEOXYHEPTONATE ALDOLASE, DAH7PS;
COMPND 6 EC: 2.5.1.54;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS;
SOURCE 3 ORGANISM_TAXID: 487;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS TRANSFERASE, SHIKIMATE PATHWAY, DAHPS, DAH7PS
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.CROSS,L.C.HEYES,S.ZHANG,A.R.NAZMI,E.J.PARKER
REVDAT 3 20-DEC-23 4UCG 1 REMARK LINK
REVDAT 2 10-FEB-16 4UCG 1 JRNL
REVDAT 1 13-JAN-16 4UCG 0
JRNL AUTH P.J.CROSS,L.C.HEYES,S.ZHANG,A.R.NAZMI
JRNL TITL THE FUNCTIONAL UNIT OF NEISSERIA MENINGITIDIS
JRNL TITL 2 3-DEOXY-D-ARABINO-HEPTULOSONATE 7-PHOSPHATE SYNTHASE IS
JRNL TITL 3 DIMERIC.
JRNL REF PLOS ONE V. 11 45187 2016
JRNL REFN ESSN 1932-6203
JRNL PMID 26828675
JRNL DOI 10.1371/JOURNAL.PONE.0145187
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 98.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 100004
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) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5260
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7301
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.99
REMARK 3 BIN R VALUE (WORKING SET) : 0.2840
REMARK 3 BIN FREE R VALUE SET COUNT : 377
REMARK 3 BIN FREE R VALUE : 0.3140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10136
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 81
REMARK 3 SOLVENT ATOMS : 735
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.24000
REMARK 3 B22 (A**2) : -0.15000
REMARK 3 B33 (A**2) : 0.38000
REMARK 3 B12 (A**2) : 0.00000
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): 0.163
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.149
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.119
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.440
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10498 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 9943 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14243 ; 1.357 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 22841 ; 0.775 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1355 ; 5.276 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 456 ;33.970 ;23.991
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1732 ;12.018 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 68 ;15.671 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1600 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12038 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2354 ; 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): 5393 ; 1.360 ; 2.529
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5392 ; 1.360 ; 2.529
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6748 ; 2.112 ; 3.784
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5105 ; 1.852 ; 2.744
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 3
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 16 A 350 6
REMARK 3 1 B 16 B 350 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 1 A (A): 4935 ; 0.25 ; 5.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 4935 ; 2.02 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 16 A 350 6
REMARK 3 1 C 16 C 350 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 2 A (A): 4890 ; 0.31 ; 5.00
REMARK 3 LOOSE THERMAL 2 A (A**2): 4890 ; 4.67 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 16 A 350 6
REMARK 3 1 D 16 D 350 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 3 A (A): 4966 ; 0.34 ; 5.00
REMARK 3 LOOSE THERMAL 3 A (A**2): 4966 ; 3.81 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 16 A 350
REMARK 3 ORIGIN FOR THE GROUP (A): 47.7250 -14.8290 -3.1290
REMARK 3 T TENSOR
REMARK 3 T11: 0.0908 T22: 0.0580
REMARK 3 T33: 0.0218 T12: -0.0049
REMARK 3 T13: 0.0062 T23: 0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 0.3019 L22: 0.2346
REMARK 3 L33: 0.6037 L12: -0.0136
REMARK 3 L13: 0.1663 L23: 0.1230
REMARK 3 S TENSOR
REMARK 3 S11: 0.0065 S12: 0.0122 S13: 0.0312
REMARK 3 S21: 0.0553 S22: -0.0596 S23: 0.0395
REMARK 3 S31: 0.0050 S32: 0.0408 S33: 0.0531
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 17 B 349
REMARK 3 ORIGIN FOR THE GROUP (A): 32.7640 -28.6300 -31.7700
REMARK 3 T TENSOR
REMARK 3 T11: 0.0701 T22: 0.0468
REMARK 3 T33: 0.0818 T12: 0.0135
REMARK 3 T13: -0.0239 T23: -0.0538
REMARK 3 L TENSOR
REMARK 3 L11: 0.1915 L22: 0.5507
REMARK 3 L33: 0.7870 L12: -0.2634
REMARK 3 L13: 0.0957 L23: 0.2014
REMARK 3 S TENSOR
REMARK 3 S11: 0.0050 S12: 0.0570 S13: -0.0436
REMARK 3 S21: -0.0128 S22: -0.1378 S23: 0.1689
REMARK 3 S31: 0.0689 S32: -0.0285 S33: 0.1328
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 16 C 349
REMARK 3 ORIGIN FOR THE GROUP (A): -0.2880 13.3780 -0.6360
REMARK 3 T TENSOR
REMARK 3 T11: 0.0798 T22: 0.0852
REMARK 3 T33: 0.0312 T12: 0.0455
REMARK 3 T13: 0.0346 T23: 0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 0.6809 L22: 0.1516
REMARK 3 L33: 0.7450 L12: -0.1408
REMARK 3 L13: -0.1569 L23: 0.0650
REMARK 3 S TENSOR
REMARK 3 S11: 0.0318 S12: 0.1066 S13: 0.0053
REMARK 3 S21: 0.0669 S22: -0.0265 S23: 0.0412
REMARK 3 S31: -0.0662 S32: -0.0314 S33: -0.0053
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 17 D 349
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5470 20.7270 -34.6170
REMARK 3 T TENSOR
REMARK 3 T11: 0.1154 T22: 0.0827
REMARK 3 T33: 0.0203 T12: -0.0543
REMARK 3 T13: -0.0300 T23: 0.0342
REMARK 3 L TENSOR
REMARK 3 L11: 0.0480 L22: 1.6507
REMARK 3 L33: 1.3777 L12: -0.1843
REMARK 3 L13: 0.1875 L23: -0.7316
REMARK 3 S TENSOR
REMARK 3 S11: -0.0807 S12: 0.0273 S13: 0.0066
REMARK 3 S21: 0.1281 S22: 0.1126 S23: 0.1014
REMARK 3 S31: -0.1547 S32: 0.1011 S33: -0.0319
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 4UCG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1290062418.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 7.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.953
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105375
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 48.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.80
REMARK 200 R MERGE (I) : 0.15000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 14.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER MR
REMARK 200 STARTING MODEL: PDB ENTRY 4HSN
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS HCL (PH 7.3), 0.2 M
REMARK 280 TRIMETHYL-AMINO-N-OXIDE (TMAO), 600UM MNSO4 AND 15-20% (W/V) PEG
REMARK 280 2000MME
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 39.47450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.86100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 66.33000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 73.86100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.47450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 66.33000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -110.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 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 THR A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 TYR A 5
REMARK 465 PRO A 6
REMARK 465 THR A 7
REMARK 465 ASP A 8
REMARK 465 ASP A 9
REMARK 465 ILE A 10
REMARK 465 LYS A 11
REMARK 465 ILE A 12
REMARK 465 LYS A 13
REMARK 465 GLU A 14
REMARK 465 SER A 351
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 TYR B 5
REMARK 465 PRO B 6
REMARK 465 THR B 7
REMARK 465 ASP B 8
REMARK 465 ASP B 9
REMARK 465 ILE B 10
REMARK 465 LYS B 11
REMARK 465 ILE B 12
REMARK 465 LYS B 13
REMARK 465 GLU B 14
REMARK 465 VAL B 15
REMARK 465 ALA B 350
REMARK 465 SER B 351
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 HIS C 3
REMARK 465 HIS C 4
REMARK 465 TYR C 5
REMARK 465 PRO C 6
REMARK 465 THR C 7
REMARK 465 ASP C 8
REMARK 465 ASP C 9
REMARK 465 ILE C 10
REMARK 465 LYS C 11
REMARK 465 ILE C 12
REMARK 465 LYS C 13
REMARK 465 GLU C 14
REMARK 465 ALA C 350
REMARK 465 SER C 351
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 HIS D 3
REMARK 465 HIS D 4
REMARK 465 TYR D 5
REMARK 465 PRO D 6
REMARK 465 THR D 7
REMARK 465 ASP D 8
REMARK 465 ASP D 9
REMARK 465 ILE D 10
REMARK 465 LYS D 11
REMARK 465 ILE D 12
REMARK 465 LYS D 13
REMARK 465 GLU D 14
REMARK 465 VAL D 15
REMARK 465 ALA D 350
REMARK 465 SER D 351
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 VAL A 15 CG1 CG2
REMARK 470 LYS A 16 CG CD CE NZ
REMARK 470 LYS A 32 CG CD CE NZ
REMARK 470 LYS A 216 CG CD CE NZ
REMARK 470 GLU A 250 CG CD OE1 OE2
REMARK 470 LYS A 275 CG CD CE NZ
REMARK 470 GLN A 293 CD OE1 NE2
REMARK 470 LYS B 16 CG CD CE NZ
REMARK 470 GLN B 43 CD OE1 NE2
REMARK 470 LYS B 54 CD CE NZ
REMARK 470 LYS B 83 CG CD CE NZ
REMARK 470 LYS B 239 CG CD CE NZ
REMARK 470 GLU B 246 CG CD OE1 OE2
REMARK 470 ARG B 274 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 275 CG CD CE NZ
REMARK 470 GLN B 293 CG CD OE1 NE2
REMARK 470 LYS B 314 CE NZ
REMARK 470 VAL C 15 CG1 CG2
REMARK 470 LYS C 16 CG CD CE NZ
REMARK 470 LYS C 32 CG CD CE NZ
REMARK 470 LYS C 54 CG CD CE NZ
REMARK 470 VAL C 104 CG1 CG2
REMARK 470 LYS C 239 CG CD CE NZ
REMARK 470 GLU C 240 CG CD OE1 OE2
REMARK 470 GLU C 246 CG CD OE1 OE2
REMARK 470 ARG C 274 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 275 CG CD CE NZ
REMARK 470 ARG C 279 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 293 CG CD OE1 NE2
REMARK 470 LYS C 314 CG CD CE NZ
REMARK 470 GLU C 316 CG CD OE1 OE2
REMARK 470 LYS D 16 CG CD CE NZ
REMARK 470 LYS D 32 CG CD CE NZ
REMARK 470 GLN D 43 CG CD OE1 NE2
REMARK 470 LYS D 216 CD CE NZ
REMARK 470 LYS D 239 CG CD CE NZ
REMARK 470 GLU D 253 CG CD OE1 OE2
REMARK 470 ARG D 274 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 275 CG CD CE NZ
REMARK 470 GLU D 282 CG CD OE1 OE2
REMARK 470 GLN D 293 CG CD OE1 NE2
REMARK 470 LYS D 314 CD CE NZ
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 B 94 NE - CZ - NH1 ANGL. DEV. = 3.3 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 THR A 103 -76.98 -128.52
REMARK 500 SER A 269 -162.24 -102.84
REMARK 500 HIS A 270 -128.88 49.47
REMARK 500 ASP A 294 -81.19 -155.65
REMARK 500 THR A 323 -125.73 -110.02
REMARK 500 THR B 103 -82.42 -127.34
REMARK 500 TYR B 155 -2.56 -140.41
REMARK 500 HIS B 270 -128.21 48.66
REMARK 500 ASP B 294 -78.72 -161.26
REMARK 500 THR B 323 -126.85 -114.48
REMARK 500 THR C 103 -86.87 -126.94
REMARK 500 HIS C 270 -133.62 58.47
REMARK 500 ASP C 294 -72.65 -155.67
REMARK 500 THR C 323 -124.54 -105.34
REMARK 500 THR D 103 -88.64 -125.54
REMARK 500 TYR D 155 -2.42 -142.34
REMARK 500 SER D 269 -162.20 -103.46
REMARK 500 HIS D 270 -128.58 49.69
REMARK 500 ASP D 294 -78.50 -164.33
REMARK 500 THR D 323 -129.19 -106.00
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 PEG A 1354
REMARK 610 PEG A 1355
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 MN A1351 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 63 SG
REMARK 620 2 HIS A 270 NE2 172.7
REMARK 620 3 GLU A 304 OE2 88.7 84.2
REMARK 620 4 ASP A 324 OD2 92.7 93.1 125.6
REMARK 620 5 PEP A1352 O1 101.1 76.3 86.0 146.0
REMARK 620 6 HOH A2039 O 80.1 104.1 140.4 92.9 59.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B1350 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 63 SG
REMARK 620 2 HIS B 270 NE2 174.9
REMARK 620 3 GLU B 304 OE2 87.9 87.3
REMARK 620 4 ASP B 324 OD2 92.4 91.5 123.2
REMARK 620 5 PEP B1351 O1 101.0 77.6 91.2 143.6
REMARK 620 6 HOH B2022 O 81.7 101.5 145.7 89.9 59.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C1350 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 63 SG
REMARK 620 2 HIS C 270 NE2 164.4
REMARK 620 3 GLU C 304 OE2 96.1 83.7
REMARK 620 4 ASP C 324 OD2 98.2 92.0 138.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN D1350 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 63 SG
REMARK 620 2 HIS D 270 NE2 175.9
REMARK 620 3 GLU D 304 OE2 88.5 90.1
REMARK 620 4 ASP D 324 OD2 93.6 90.3 131.0
REMARK 620 5 HOH D2019 O 86.8 91.3 131.9 97.1
REMARK 620 N 1 2 3 4
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "DA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 1350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 1350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 1350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1351
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEP A 1352
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEP B 1351
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEP D 1351
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEP C 1351
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1352
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1353
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1352
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1353
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1354
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1355
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1354
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UC5 RELATED DB: PDB
REMARK 900 NEISSERIA MENINGITIDIS DAH7PS-PHENYLALANINE REGULATED
DBREF 4UCG A 1 351 UNP Q9K169 Q9K169_NEIMB 1 351
DBREF 4UCG B 1 351 UNP Q9K169 Q9K169_NEIMB 1 351
DBREF 4UCG C 1 351 UNP Q9K169 Q9K169_NEIMB 1 351
DBREF 4UCG D 1 351 UNP Q9K169 Q9K169_NEIMB 1 351
SEQADV 4UCG SER A 126 UNP Q9K169 ARG 126 ENGINEERED MUTATION
SEQADV 4UCG SER B 126 UNP Q9K169 ARG 126 ENGINEERED MUTATION
SEQADV 4UCG SER C 126 UNP Q9K169 ARG 126 ENGINEERED MUTATION
SEQADV 4UCG SER D 126 UNP Q9K169 ARG 126 ENGINEERED MUTATION
SEQRES 1 A 351 MET THR HIS HIS TYR PRO THR ASP ASP ILE LYS ILE LYS
SEQRES 2 A 351 GLU VAL LYS GLU LEU LEU PRO PRO ILE ALA HIS LEU TYR
SEQRES 3 A 351 GLU LEU PRO ILE SER LYS GLU ALA SER GLY LEU VAL HIS
SEQRES 4 A 351 ARG THR ARG GLN GLU ILE SER ASP LEU VAL HIS GLY ARG
SEQRES 5 A 351 ASP LYS ARG LEU LEU VAL ILE ILE GLY PRO CYS SER ILE
SEQRES 6 A 351 HIS ASP PRO LYS ALA ALA LEU GLU TYR ALA GLU ARG LEU
SEQRES 7 A 351 LEU LYS LEU ARG LYS GLN TYR GLU ASN GLU LEU LEU ILE
SEQRES 8 A 351 VAL MET ARG VAL TYR PHE GLU LYS PRO ARG THR THR VAL
SEQRES 9 A 351 GLY TRP LYS GLY LEU ILE ASN ASP PRO HIS LEU ASP GLY
SEQRES 10 A 351 THR PHE ASP ILE ASN PHE GLY LEU SER GLN ALA ARG SER
SEQRES 11 A 351 LEU LEU LEU SER LEU ASN ASN MET GLY MET PRO ALA SER
SEQRES 12 A 351 THR GLU PHE LEU ASP MET ILE THR PRO GLN TYR TYR ALA
SEQRES 13 A 351 ASP LEU ILE SER TRP GLY ALA ILE GLY ALA ARG THR THR
SEQRES 14 A 351 GLU SER GLN VAL HIS ARG GLU LEU ALA SER GLY LEU SER
SEQRES 15 A 351 CYS PRO VAL GLY PHE LYS ASN GLY THR ASP GLY ASN LEU
SEQRES 16 A 351 LYS ILE ALA ILE ASP ALA ILE GLY ALA ALA SER HIS SER
SEQRES 17 A 351 HIS HIS PHE LEU SER VAL THR LYS ALA GLY HIS SER ALA
SEQRES 18 A 351 ILE VAL HIS THR GLY GLY ASN PRO ASP CYS HIS VAL ILE
SEQRES 19 A 351 LEU ARG GLY GLY LYS GLU PRO ASN TYR ASP ALA GLU HIS
SEQRES 20 A 351 VAL SER GLU ALA ALA GLU GLN LEU ARG ALA ALA GLY VAL
SEQRES 21 A 351 THR ASP LYS LEU MET ILE ASP CYS SER HIS ALA ASN SER
SEQRES 22 A 351 ARG LYS ASP TYR THR ARG GLN MET GLU VAL ALA GLN ASP
SEQRES 23 A 351 ILE ALA ALA GLN LEU GLU GLN ASP GLY GLY ASN ILE MET
SEQRES 24 A 351 GLY VAL MET VAL GLU SER HIS LEU VAL GLU GLY ARG GLN
SEQRES 25 A 351 ASP LYS PRO GLU VAL TYR GLY LYS SER ILE THR ASP ALA
SEQRES 26 A 351 CYS ILE GLY TRP GLY ALA THR GLU GLU LEU LEU ALA LEU
SEQRES 27 A 351 LEU ALA GLY ALA ASN LYS LYS ARG MET ALA ARG ALA SER
SEQRES 1 B 351 MET THR HIS HIS TYR PRO THR ASP ASP ILE LYS ILE LYS
SEQRES 2 B 351 GLU VAL LYS GLU LEU LEU PRO PRO ILE ALA HIS LEU TYR
SEQRES 3 B 351 GLU LEU PRO ILE SER LYS GLU ALA SER GLY LEU VAL HIS
SEQRES 4 B 351 ARG THR ARG GLN GLU ILE SER ASP LEU VAL HIS GLY ARG
SEQRES 5 B 351 ASP LYS ARG LEU LEU VAL ILE ILE GLY PRO CYS SER ILE
SEQRES 6 B 351 HIS ASP PRO LYS ALA ALA LEU GLU TYR ALA GLU ARG LEU
SEQRES 7 B 351 LEU LYS LEU ARG LYS GLN TYR GLU ASN GLU LEU LEU ILE
SEQRES 8 B 351 VAL MET ARG VAL TYR PHE GLU LYS PRO ARG THR THR VAL
SEQRES 9 B 351 GLY TRP LYS GLY LEU ILE ASN ASP PRO HIS LEU ASP GLY
SEQRES 10 B 351 THR PHE ASP ILE ASN PHE GLY LEU SER GLN ALA ARG SER
SEQRES 11 B 351 LEU LEU LEU SER LEU ASN ASN MET GLY MET PRO ALA SER
SEQRES 12 B 351 THR GLU PHE LEU ASP MET ILE THR PRO GLN TYR TYR ALA
SEQRES 13 B 351 ASP LEU ILE SER TRP GLY ALA ILE GLY ALA ARG THR THR
SEQRES 14 B 351 GLU SER GLN VAL HIS ARG GLU LEU ALA SER GLY LEU SER
SEQRES 15 B 351 CYS PRO VAL GLY PHE LYS ASN GLY THR ASP GLY ASN LEU
SEQRES 16 B 351 LYS ILE ALA ILE ASP ALA ILE GLY ALA ALA SER HIS SER
SEQRES 17 B 351 HIS HIS PHE LEU SER VAL THR LYS ALA GLY HIS SER ALA
SEQRES 18 B 351 ILE VAL HIS THR GLY GLY ASN PRO ASP CYS HIS VAL ILE
SEQRES 19 B 351 LEU ARG GLY GLY LYS GLU PRO ASN TYR ASP ALA GLU HIS
SEQRES 20 B 351 VAL SER GLU ALA ALA GLU GLN LEU ARG ALA ALA GLY VAL
SEQRES 21 B 351 THR ASP LYS LEU MET ILE ASP CYS SER HIS ALA ASN SER
SEQRES 22 B 351 ARG LYS ASP TYR THR ARG GLN MET GLU VAL ALA GLN ASP
SEQRES 23 B 351 ILE ALA ALA GLN LEU GLU GLN ASP GLY GLY ASN ILE MET
SEQRES 24 B 351 GLY VAL MET VAL GLU SER HIS LEU VAL GLU GLY ARG GLN
SEQRES 25 B 351 ASP LYS PRO GLU VAL TYR GLY LYS SER ILE THR ASP ALA
SEQRES 26 B 351 CYS ILE GLY TRP GLY ALA THR GLU GLU LEU LEU ALA LEU
SEQRES 27 B 351 LEU ALA GLY ALA ASN LYS LYS ARG MET ALA ARG ALA SER
SEQRES 1 C 351 MET THR HIS HIS TYR PRO THR ASP ASP ILE LYS ILE LYS
SEQRES 2 C 351 GLU VAL LYS GLU LEU LEU PRO PRO ILE ALA HIS LEU TYR
SEQRES 3 C 351 GLU LEU PRO ILE SER LYS GLU ALA SER GLY LEU VAL HIS
SEQRES 4 C 351 ARG THR ARG GLN GLU ILE SER ASP LEU VAL HIS GLY ARG
SEQRES 5 C 351 ASP LYS ARG LEU LEU VAL ILE ILE GLY PRO CYS SER ILE
SEQRES 6 C 351 HIS ASP PRO LYS ALA ALA LEU GLU TYR ALA GLU ARG LEU
SEQRES 7 C 351 LEU LYS LEU ARG LYS GLN TYR GLU ASN GLU LEU LEU ILE
SEQRES 8 C 351 VAL MET ARG VAL TYR PHE GLU LYS PRO ARG THR THR VAL
SEQRES 9 C 351 GLY TRP LYS GLY LEU ILE ASN ASP PRO HIS LEU ASP GLY
SEQRES 10 C 351 THR PHE ASP ILE ASN PHE GLY LEU SER GLN ALA ARG SER
SEQRES 11 C 351 LEU LEU LEU SER LEU ASN ASN MET GLY MET PRO ALA SER
SEQRES 12 C 351 THR GLU PHE LEU ASP MET ILE THR PRO GLN TYR TYR ALA
SEQRES 13 C 351 ASP LEU ILE SER TRP GLY ALA ILE GLY ALA ARG THR THR
SEQRES 14 C 351 GLU SER GLN VAL HIS ARG GLU LEU ALA SER GLY LEU SER
SEQRES 15 C 351 CYS PRO VAL GLY PHE LYS ASN GLY THR ASP GLY ASN LEU
SEQRES 16 C 351 LYS ILE ALA ILE ASP ALA ILE GLY ALA ALA SER HIS SER
SEQRES 17 C 351 HIS HIS PHE LEU SER VAL THR LYS ALA GLY HIS SER ALA
SEQRES 18 C 351 ILE VAL HIS THR GLY GLY ASN PRO ASP CYS HIS VAL ILE
SEQRES 19 C 351 LEU ARG GLY GLY LYS GLU PRO ASN TYR ASP ALA GLU HIS
SEQRES 20 C 351 VAL SER GLU ALA ALA GLU GLN LEU ARG ALA ALA GLY VAL
SEQRES 21 C 351 THR ASP LYS LEU MET ILE ASP CYS SER HIS ALA ASN SER
SEQRES 22 C 351 ARG LYS ASP TYR THR ARG GLN MET GLU VAL ALA GLN ASP
SEQRES 23 C 351 ILE ALA ALA GLN LEU GLU GLN ASP GLY GLY ASN ILE MET
SEQRES 24 C 351 GLY VAL MET VAL GLU SER HIS LEU VAL GLU GLY ARG GLN
SEQRES 25 C 351 ASP LYS PRO GLU VAL TYR GLY LYS SER ILE THR ASP ALA
SEQRES 26 C 351 CYS ILE GLY TRP GLY ALA THR GLU GLU LEU LEU ALA LEU
SEQRES 27 C 351 LEU ALA GLY ALA ASN LYS LYS ARG MET ALA ARG ALA SER
SEQRES 1 D 351 MET THR HIS HIS TYR PRO THR ASP ASP ILE LYS ILE LYS
SEQRES 2 D 351 GLU VAL LYS GLU LEU LEU PRO PRO ILE ALA HIS LEU TYR
SEQRES 3 D 351 GLU LEU PRO ILE SER LYS GLU ALA SER GLY LEU VAL HIS
SEQRES 4 D 351 ARG THR ARG GLN GLU ILE SER ASP LEU VAL HIS GLY ARG
SEQRES 5 D 351 ASP LYS ARG LEU LEU VAL ILE ILE GLY PRO CYS SER ILE
SEQRES 6 D 351 HIS ASP PRO LYS ALA ALA LEU GLU TYR ALA GLU ARG LEU
SEQRES 7 D 351 LEU LYS LEU ARG LYS GLN TYR GLU ASN GLU LEU LEU ILE
SEQRES 8 D 351 VAL MET ARG VAL TYR PHE GLU LYS PRO ARG THR THR VAL
SEQRES 9 D 351 GLY TRP LYS GLY LEU ILE ASN ASP PRO HIS LEU ASP GLY
SEQRES 10 D 351 THR PHE ASP ILE ASN PHE GLY LEU SER GLN ALA ARG SER
SEQRES 11 D 351 LEU LEU LEU SER LEU ASN ASN MET GLY MET PRO ALA SER
SEQRES 12 D 351 THR GLU PHE LEU ASP MET ILE THR PRO GLN TYR TYR ALA
SEQRES 13 D 351 ASP LEU ILE SER TRP GLY ALA ILE GLY ALA ARG THR THR
SEQRES 14 D 351 GLU SER GLN VAL HIS ARG GLU LEU ALA SER GLY LEU SER
SEQRES 15 D 351 CYS PRO VAL GLY PHE LYS ASN GLY THR ASP GLY ASN LEU
SEQRES 16 D 351 LYS ILE ALA ILE ASP ALA ILE GLY ALA ALA SER HIS SER
SEQRES 17 D 351 HIS HIS PHE LEU SER VAL THR LYS ALA GLY HIS SER ALA
SEQRES 18 D 351 ILE VAL HIS THR GLY GLY ASN PRO ASP CYS HIS VAL ILE
SEQRES 19 D 351 LEU ARG GLY GLY LYS GLU PRO ASN TYR ASP ALA GLU HIS
SEQRES 20 D 351 VAL SER GLU ALA ALA GLU GLN LEU ARG ALA ALA GLY VAL
SEQRES 21 D 351 THR ASP LYS LEU MET ILE ASP CYS SER HIS ALA ASN SER
SEQRES 22 D 351 ARG LYS ASP TYR THR ARG GLN MET GLU VAL ALA GLN ASP
SEQRES 23 D 351 ILE ALA ALA GLN LEU GLU GLN ASP GLY GLY ASN ILE MET
SEQRES 24 D 351 GLY VAL MET VAL GLU SER HIS LEU VAL GLU GLY ARG GLN
SEQRES 25 D 351 ASP LYS PRO GLU VAL TYR GLY LYS SER ILE THR ASP ALA
SEQRES 26 D 351 CYS ILE GLY TRP GLY ALA THR GLU GLU LEU LEU ALA LEU
SEQRES 27 D 351 LEU ALA GLY ALA ASN LYS LYS ARG MET ALA ARG ALA SER
HET MN A1351 1
HET PEP A1352 10
HET SO4 A1353 5
HET PEG A1354 4
HET PEG A1355 4
HET MN B1350 1
HET PEP B1351 10
HET SO4 B1352 5
HET PEG B1353 7
HET PEG B1354 7
HET MN C1350 1
HET PEP C1351 10
HET MN D1350 1
HET PEP D1351 10
HET SO4 D1352 5
HETNAM MN MANGANESE (II) ION
HETNAM PEP PHOSPHOENOLPYRUVATE
HETNAM SO4 SULFATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 5 MN 4(MN 2+)
FORMUL 6 PEP 4(C3 H5 O6 P)
FORMUL 7 SO4 3(O4 S 2-)
FORMUL 8 PEG 4(C4 H10 O3)
FORMUL 20 HOH *735(H2 O)
HELIX 1 1 PRO A 20 LEU A 28 1 9
HELIX 2 2 SER A 31 HIS A 50 1 20
HELIX 3 3 ASP A 67 TYR A 85 1 19
HELIX 4 4 ASP A 120 MET A 138 1 19
HELIX 5 5 THR A 151 ALA A 156 1 6
HELIX 6 6 ASP A 157 ILE A 159 5 3
HELIX 7 7 SER A 171 LEU A 181 1 11
HELIX 8 8 LEU A 195 SER A 206 1 12
HELIX 9 9 ASP A 244 ALA A 258 1 15
HELIX 10 10 SER A 269 SER A 273 5 5
HELIX 11 11 ASP A 276 THR A 278 5 3
HELIX 12 12 ARG A 279 ASP A 294 1 16
HELIX 13 13 GLY A 328 ARG A 349 1 22
HELIX 14 14 PRO B 20 LEU B 28 1 9
HELIX 15 15 SER B 31 HIS B 50 1 20
HELIX 16 16 ASP B 67 TYR B 85 1 19
HELIX 17 17 ASP B 120 MET B 138 1 19
HELIX 18 18 THR B 151 ALA B 156 1 6
HELIX 19 19 ASP B 157 ILE B 159 5 3
HELIX 20 20 SER B 171 GLY B 180 1 10
HELIX 21 21 LEU B 195 HIS B 207 1 13
HELIX 22 22 ASP B 244 ALA B 258 1 15
HELIX 23 23 ASP B 276 THR B 278 5 3
HELIX 24 24 ARG B 279 ASP B 294 1 16
HELIX 25 25 GLY B 328 ARG B 349 1 22
HELIX 26 26 PRO C 20 LEU C 28 1 9
HELIX 27 27 SER C 31 HIS C 50 1 20
HELIX 28 28 ASP C 67 TYR C 85 1 19
HELIX 29 29 ASP C 120 GLY C 139 1 20
HELIX 30 30 THR C 151 ALA C 156 1 6
HELIX 31 31 ASP C 157 ILE C 159 5 3
HELIX 32 32 SER C 171 LEU C 181 1 11
HELIX 33 33 LEU C 195 HIS C 207 1 13
HELIX 34 34 ASP C 244 ALA C 258 1 15
HELIX 35 35 SER C 269 ARG C 274 5 6
HELIX 36 36 ASP C 276 THR C 278 5 3
HELIX 37 37 ARG C 279 ASP C 294 1 16
HELIX 38 38 GLY C 328 ALA C 348 1 21
HELIX 39 39 PRO D 20 LEU D 28 1 9
HELIX 40 40 SER D 31 HIS D 50 1 20
HELIX 41 41 ASP D 67 TYR D 85 1 19
HELIX 42 42 ASP D 120 MET D 138 1 19
HELIX 43 43 ILE D 150 TYR D 155 5 6
HELIX 44 44 TYR D 155 ASP D 157 5 3
HELIX 45 45 SER D 171 LEU D 181 1 11
HELIX 46 46 LEU D 195 HIS D 207 1 13
HELIX 47 47 ASP D 244 ALA D 258 1 15
HELIX 48 48 SER D 269 SER D 273 5 5
HELIX 49 49 ASP D 276 THR D 278 5 3
HELIX 50 50 ARG D 279 ASP D 294 1 16
HELIX 51 51 GLY D 328 ARG D 349 1 22
SHEET 1 AA 9 LEU A 56 GLY A 61 0
SHEET 2 AA 9 LEU A 89 ARG A 94 1 O LEU A 90 N VAL A 58
SHEET 3 AA 9 ALA A 142 GLU A 145 1 N SER A 143 O MET A 93
SHEET 4 AA 9 TRP A 161 ILE A 164 1 O TRP A 161 N THR A 144
SHEET 5 AA 9 VAL A 185 LYS A 188 1 O GLY A 186 N ILE A 164
SHEET 6 AA 9 CYS A 231 LEU A 235 1 O HIS A 232 N PHE A 187
SHEET 7 AA 9 LEU A 264 ASP A 267 1 O MET A 265 N LEU A 235
SHEET 8 AA 9 ILE A 298 GLU A 304 1 N MET A 299 O LEU A 264
SHEET 9 AA 9 LEU A 56 GLY A 61 1 O LEU A 57 N VAL A 301
SHEET 1 AB 2 HIS A 210 VAL A 214 0
SHEET 2 AB 2 SER A 220 HIS A 224 -1 O ALA A 221 N SER A 213
SHEET 1 BA 9 LEU B 56 GLY B 61 0
SHEET 2 BA 9 LEU B 89 ARG B 94 1 O LEU B 90 N VAL B 58
SHEET 3 BA 9 ALA B 142 GLU B 145 1 N SER B 143 O MET B 93
SHEET 4 BA 9 TRP B 161 ILE B 164 1 O TRP B 161 N THR B 144
SHEET 5 BA 9 VAL B 185 LYS B 188 1 O GLY B 186 N ILE B 164
SHEET 6 BA 9 CYS B 231 LEU B 235 1 O HIS B 232 N PHE B 187
SHEET 7 BA 9 LEU B 264 ASP B 267 1 O MET B 265 N LEU B 235
SHEET 8 BA 9 ILE B 298 GLU B 304 1 N MET B 299 O LEU B 264
SHEET 9 BA 9 LEU B 56 GLY B 61 1 O LEU B 57 N VAL B 301
SHEET 1 BB 2 HIS B 210 VAL B 214 0
SHEET 2 BB 2 SER B 220 HIS B 224 -1 O ALA B 221 N SER B 213
SHEET 1 CA 9 LEU C 56 GLY C 61 0
SHEET 2 CA 9 LEU C 89 ARG C 94 1 O LEU C 90 N VAL C 58
SHEET 3 CA 9 ALA C 142 GLU C 145 1 N SER C 143 O MET C 93
SHEET 4 CA 9 TRP C 161 ILE C 164 1 O TRP C 161 N THR C 144
SHEET 5 CA 9 VAL C 185 LYS C 188 1 O GLY C 186 N ILE C 164
SHEET 6 CA 9 CYS C 231 LEU C 235 1 O HIS C 232 N PHE C 187
SHEET 7 CA 9 LEU C 264 ASP C 267 1 O MET C 265 N LEU C 235
SHEET 8 CA 9 ILE C 298 GLU C 304 1 N MET C 299 O LEU C 264
SHEET 9 CA 9 LEU C 56 GLY C 61 1 O LEU C 57 N VAL C 301
SHEET 1 CB 2 HIS C 210 VAL C 214 0
SHEET 2 CB 2 SER C 220 HIS C 224 -1 O ALA C 221 N SER C 213
SHEET 1 DA 9 LEU D 56 GLY D 61 0
SHEET 2 DA 9 LEU D 89 ARG D 94 1 O LEU D 90 N VAL D 58
SHEET 3 DA 9 ALA D 142 GLU D 145 1 N SER D 143 O MET D 93
SHEET 4 DA 9 ILE D 159 ILE D 164 1 N SER D 160 O ALA D 142
SHEET 5 DA 9 VAL D 185 LYS D 188 1 O GLY D 186 N ILE D 164
SHEET 6 DA 9 CYS D 231 LEU D 235 1 O HIS D 232 N PHE D 187
SHEET 7 DA 9 LEU D 264 ASP D 267 1 O MET D 265 N LEU D 235
SHEET 8 DA 9 ILE D 298 GLU D 304 1 N MET D 299 O LEU D 264
SHEET 9 DA 9 LEU D 56 GLY D 61 1 O LEU D 57 N VAL D 301
SHEET 1 DB 2 HIS D 210 VAL D 214 0
SHEET 2 DB 2 SER D 220 HIS D 224 -1 O ALA D 221 N SER D 213
LINK SG CYS A 63 MN MN A1351 1555 1555 2.57
LINK NE2 HIS A 270 MN MN A1351 1555 1555 2.38
LINK OE2 GLU A 304 MN MN A1351 1555 1555 2.07
LINK OD2 ASP A 324 MN MN A1351 1555 1555 2.00
LINK MN MN A1351 O1 PEP A1352 1555 1555 2.80
LINK MN MN A1351 O HOH A2039 1555 1555 2.08
LINK SG CYS B 63 MN MN B1350 1555 1555 2.59
LINK NE2 HIS B 270 MN MN B1350 1555 1555 2.37
LINK OE2 GLU B 304 MN MN B1350 1555 1555 2.03
LINK OD2 ASP B 324 MN MN B1350 1555 1555 1.98
LINK MN MN B1350 O1 PEP B1351 1555 1555 2.55
LINK MN MN B1350 O HOH B2022 1555 1555 2.17
LINK SG CYS C 63 MN MN C1350 1555 1555 2.53
LINK NE2 HIS C 270 MN MN C1350 1555 1555 2.52
LINK OE2 GLU C 304 MN MN C1350 1555 1555 2.12
LINK OD2 ASP C 324 MN MN C1350 1555 1555 2.24
LINK SG CYS D 63 MN MN D1350 1555 1555 2.53
LINK NE2 HIS D 270 MN MN D1350 1555 1555 2.36
LINK OE2 GLU D 304 MN MN D1350 1555 1555 2.21
LINK OD2 ASP D 324 MN MN D1350 1555 1555 2.23
LINK MN MN D1350 O HOH D2019 1555 1555 2.17
SITE 1 AC1 6 CYS B 63 HIS B 270 GLU B 304 ASP B 324
SITE 2 AC1 6 PEP B1351 HOH B2022
SITE 1 AC2 5 CYS C 63 HIS C 270 GLU C 304 ASP C 324
SITE 2 AC2 5 PEP C1351
SITE 1 AC3 6 CYS D 63 HIS D 270 GLU D 304 ASP D 324
SITE 2 AC3 6 PEP D1351 HOH D2019
SITE 1 AC4 6 CYS A 63 HIS A 270 GLU A 304 ASP A 324
SITE 2 AC4 6 PEP A1352 HOH A2039
SITE 1 AC5 17 ARG A 94 TYR A 96 LYS A 99 GLU A 145
SITE 2 AC5 17 GLY A 165 ALA A 166 ARG A 167 LYS A 188
SITE 3 AC5 17 ARG A 236 HIS A 270 GLU A 304 MN A1351
SITE 4 AC5 17 HOH A2039 HOH A2076 HOH A2116 HOH A2133
SITE 5 AC5 17 HOH A2138
SITE 1 AC6 16 ARG B 94 TYR B 96 LYS B 99 GLU B 145
SITE 2 AC6 16 GLY B 165 ALA B 166 ARG B 167 LYS B 188
SITE 3 AC6 16 ARG B 236 HIS B 270 GLU B 304 MN B1350
SITE 4 AC6 16 HOH B2022 HOH B2048 HOH B2081 HOH B2093
SITE 1 AC7 14 ARG D 94 TYR D 96 LYS D 99 GLU D 145
SITE 2 AC7 14 GLY D 165 ALA D 166 ARG D 167 LYS D 188
SITE 3 AC7 14 ARG D 236 HIS D 270 MN D1350 HOH D2019
SITE 4 AC7 14 HOH D2046 HOH D2077
SITE 1 AC8 14 ARG C 94 TYR C 96 LYS C 99 GLU C 145
SITE 2 AC8 14 GLY C 165 ALA C 166 ARG C 167 LYS C 188
SITE 3 AC8 14 ARG C 236 HIS C 270 MN C1350 HOH C2074
SITE 4 AC8 14 HOH C2104 HOH C2116
SITE 1 AC9 3 ARG B 101 THR B 102 HOH B2056
SITE 1 BC1 4 ARG A 101 THR A 102 HOH A2085 HOH A2242
SITE 1 BC2 2 ARG D 101 THR D 102
SITE 1 BC3 5 TRP B 106 ASP B 112 LEU B 115 ASP B 116
SITE 2 BC3 5 GLY B 117
SITE 1 BC4 7 LEU A 19 ALA A 23 GLU A 27 PEG A1355
SITE 2 BC4 7 LEU C 19 ALA C 23 GLU C 27
SITE 1 BC5 5 TYR A 26 GLU A 27 PEG A1354 LEU C 19
SITE 2 BC5 5 ASN C 122
SITE 1 BC6 5 ALA A 221 ILE A 222 LYS B 16 GLU B 17
SITE 2 BC6 5 LEU B 18
CRYST1 78.949 132.660 147.722 90.00 90.00 90.00 P 21 21 21 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012666 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007538 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006769 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 -0.052162 -0.998636 -0.002101 20.63235 1
MTRIX2 2 -0.998595 0.052140 0.009493 19.83943 1
MTRIX3 2 -0.009370 0.002593 -0.999953 -34.71185 1
(ATOM LINES ARE NOT SHOWN.)
END
