HEADER TRANSFERASE 06-MAY-14 4QAV
TITLE THE STRUCTURE OF BETA-KETOACYL -(ACYL CARRIER PROTEIN) SYNTHASE II
TITLE 2 (FABF) FROM NEISSERIA MENINGITIDIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.3.1.179;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS;
SOURCE 3 ORGANISM_TAXID: 662598;
SOURCE 4 STRAIN: ALPHA14;
SOURCE 5 GENE: FABF;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS KASII, FABF, CONDENSING ENZYME, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.D.NANSON,J.K.FORWOOD
REVDAT 2 08-NOV-23 4QAV 1 REMARK LINK
REVDAT 1 04-JUN-14 4QAV 0
JRNL AUTH J.D.NANSON,J.K.FORWOOD
JRNL TITL THE STRUCTURE OF BETA-KETOACYL -(ACYL CARRIER PROTEIN)
JRNL TITL 2 SYNTHASE II (FABF) FROM NEISSERIA MENINGITIDIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1688)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.24
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 51993
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2651
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 32.2438 - 5.5944 0.99 2688 140 0.1385 0.1448
REMARK 3 2 5.5944 - 4.4442 1.00 2631 156 0.1332 0.1402
REMARK 3 3 4.4442 - 3.8835 1.00 2624 140 0.1292 0.1445
REMARK 3 4 3.8835 - 3.5289 1.00 2646 129 0.1512 0.1684
REMARK 3 5 3.5289 - 3.2762 1.00 2614 133 0.1689 0.1888
REMARK 3 6 3.2762 - 3.0832 1.00 2621 148 0.1669 0.1842
REMARK 3 7 3.0832 - 2.9289 1.00 2635 117 0.1839 0.1935
REMARK 3 8 2.9289 - 2.8015 1.00 2609 136 0.1844 0.2160
REMARK 3 9 2.8015 - 2.6937 1.00 2602 137 0.1786 0.2370
REMARK 3 10 2.6937 - 2.6008 1.00 2617 139 0.1856 0.2198
REMARK 3 11 2.6008 - 2.5195 1.00 2606 136 0.1852 0.2043
REMARK 3 12 2.5195 - 2.4475 1.00 2592 135 0.1867 0.2171
REMARK 3 13 2.4475 - 2.3831 1.00 2576 135 0.2012 0.2246
REMARK 3 14 2.3831 - 2.3250 1.00 2592 153 0.2046 0.2505
REMARK 3 15 2.3250 - 2.2721 0.99 2544 145 0.2412 0.2893
REMARK 3 16 2.2721 - 2.2238 0.99 2578 156 0.2880 0.3171
REMARK 3 17 2.2238 - 2.1793 0.98 2533 144 0.2497 0.2955
REMARK 3 18 2.1793 - 2.1382 0.98 2518 144 0.2321 0.2604
REMARK 3 19 2.1382 - 2.1000 0.96 2516 128 0.2328 0.2684
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.060
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.01
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 6138
REMARK 3 ANGLE : 0.853 8299
REMARK 3 CHIRALITY : 0.052 936
REMARK 3 PLANARITY : 0.004 1098
REMARK 3 DIHEDRAL : 12.135 2188
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESSEQ 3:414)
REMARK 3 ORIGIN FOR THE GROUP (A):-143.4734 56.1608 -5.1350
REMARK 3 T TENSOR
REMARK 3 T11: 0.1842 T22: 0.1583
REMARK 3 T33: 0.1914 T12: 0.0023
REMARK 3 T13: -0.0996 T23: -0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 2.1915 L22: 1.1823
REMARK 3 L33: 0.8803 L12: -0.3184
REMARK 3 L13: 0.3889 L23: -0.1881
REMARK 3 S TENSOR
REMARK 3 S11: -0.0756 S12: -0.1233 S13: 0.1357
REMARK 3 S21: 0.1334 S22: 0.0328 S23: -0.1486
REMARK 3 S31: -0.0830 S32: 0.0163 S33: 0.0359
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESSEQ 3:414)
REMARK 3 ORIGIN FOR THE GROUP (A):-156.4754 57.6229 -31.8358
REMARK 3 T TENSOR
REMARK 3 T11: 0.2633 T22: 0.3465
REMARK 3 T33: 0.1714 T12: -0.0071
REMARK 3 T13: -0.0895 T23: 0.0532
REMARK 3 L TENSOR
REMARK 3 L11: 2.1442 L22: 1.0758
REMARK 3 L33: 0.8384 L12: -0.0601
REMARK 3 L13: 0.4061 L23: -0.0354
REMARK 3 S TENSOR
REMARK 3 S11: -0.0423 S12: 0.5681 S13: 0.1438
REMARK 3 S21: -0.2883 S22: 0.0299 S23: 0.0926
REMARK 3 S31: -0.0719 S32: 0.0644 S33: 0.0138
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4QAV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000085822.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : SILICON DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52092
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 33.230
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2GFW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 250MM SODIUM FORMATE,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 296.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.31333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 22.15667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 33.23500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 11.07833
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 55.39167
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLY A 415
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLY B 415
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 SER A 163 38.67 -150.04
REMARK 500 ALA A 164 -126.15 55.92
REMARK 500 TYR A 269 -75.11 -126.38
REMARK 500 LEU A 342 -123.05 57.34
REMARK 500 ASN A 384 -14.57 79.07
REMARK 500 SER B 163 32.90 -144.44
REMARK 500 ALA B 164 -123.76 58.72
REMARK 500 TYR B 269 -71.08 -127.65
REMARK 500 LEU B 342 -124.42 57.67
REMARK 500 ASN B 384 -11.38 82.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 501 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 301 OD1
REMARK 620 2 ASN A 301 O 71.5
REMARK 620 3 ALA A 302 O 75.8 69.7
REMARK 620 4 GLU A 349 OE1 82.0 149.8 90.3
REMARK 620 5 SER A 396 OG 86.0 82.2 150.1 110.7
REMARK 620 6 ASN A 397 O 162.4 94.4 89.7 108.3 102.7
REMARK 620 7 HOH A 622 O 128.0 160.4 113.5 48.5 96.4 66.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 501 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 301 OD1
REMARK 620 2 ASN B 301 O 74.5
REMARK 620 3 ALA B 302 O 77.3 70.0
REMARK 620 4 GLU B 349 OE1 81.2 150.1 88.0
REMARK 620 5 SER B 396 OG 87.7 84.7 153.2 111.9
REMARK 620 6 ASN B 397 O 162.6 92.1 87.7 107.5 102.3
REMARK 620 7 HOH B 641 O 127.6 157.9 110.5 48.8 96.3 66.0
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 502
DBREF 4QAV A 1 415 UNP C6S978 C6S978_NEIML 1 415
DBREF 4QAV B 1 415 UNP C6S978 C6S978_NEIML 1 415
SEQRES 1 A 415 MET SER GLN ARG ARG VAL VAL ILE THR GLY LEU GLY GLN
SEQRES 2 A 415 VAL SER PRO VAL GLY ASN THR VAL ALA GLU ALA TRP ASP
SEQRES 3 A 415 THR LEU LEU ALA GLY LYS SER GLY ILE GLY ALA ILE THR
SEQRES 4 A 415 ARG PHE ASP ALA SER ASP ILE ASN SER ARG VAL ALA GLY
SEQRES 5 A 415 GLU VAL ARG GLY PHE ASP ILE GLY GLN TYR ILE SER ALA
SEQRES 6 A 415 LYS GLU ALA ARG ARG MET ASP VAL PHE ILE HIS TYR GLY
SEQRES 7 A 415 ILE ALA ALA ALA LEU GLN ALA ILE ALA ASP SER GLY LEU
SEQRES 8 A 415 ASP ASP VAL GLU ASN LEU ASP LYS ASP ARG ILE GLY VAL
SEQRES 9 A 415 ASN ILE GLY SER GLY ILE GLY GLY LEU PRO SER ILE GLU
SEQRES 10 A 415 VAL THR GLY LYS ALA VAL ILE GLU GLY GLY ALA ARG LYS
SEQRES 11 A 415 ILE ASN PRO PHE PHE ILE PRO GLY SER LEU ILE ASN LEU
SEQRES 12 A 415 ILE SER GLY HIS VAL THR ILE LEU LYS GLY TYR ARG GLY
SEQRES 13 A 415 PRO SER TYR GLY MET VAL SER ALA CYS THR THR GLY ALA
SEQRES 14 A 415 HIS ALA ILE GLY ASN SER ALA ARG LEU ILE LYS TYR GLY
SEQRES 15 A 415 ASP ALA ASP ILE MET VAL ALA GLY GLY ALA GLU GLY ALA
SEQRES 16 A 415 ILE SER THR LEU GLY VAL GLY GLY PHE ALA ALA MET LYS
SEQRES 17 A 415 ALA LEU SER THR ARG ASN ASP ASP PRO ALA THR ALA SER
SEQRES 18 A 415 ARG PRO TRP ASP LYS GLY ARG ASP GLY PHE VAL ILE GLY
SEQRES 19 A 415 GLU GLY ALA GLY ILE LEU VAL LEU GLU GLU LEU GLU HIS
SEQRES 20 A 415 ALA LYS LYS ARG GLY ALA LYS ILE TYR ALA GLU ILE VAL
SEQRES 21 A 415 GLY PHE GLY MET SER SER ASP ALA TYR HIS ILE THR ALA
SEQRES 22 A 415 PRO ASN GLU GLU GLY PRO ALA LEU ALA VAL THR ARG ALA
SEQRES 23 A 415 LEU LYS ASP ALA GLY ILE ASN PRO GLU ASP VAL ASP TYR
SEQRES 24 A 415 VAL ASN ALA HIS GLY THR SER THR PRO LEU GLY ASP ALA
SEQRES 25 A 415 ASN GLU THR LYS ALA LEU LYS ARG ALA PHE GLY GLU HIS
SEQRES 26 A 415 ALA TYR LYS THR VAL VAL SER SER THR LYS SER MET THR
SEQRES 27 A 415 GLY HIS LEU LEU GLY ALA ALA GLY GLY VAL GLU ALA VAL
SEQRES 28 A 415 TYR SER ILE LEU ALA ILE HIS ASP GLY LYS ILE PRO PRO
SEQRES 29 A 415 THR ILE ASN ILE PHE GLU GLN ASP VAL GLU ALA GLY CYS
SEQRES 30 A 415 ASP LEU ASP TYR CYS ALA ASN GLU ALA ARG ASP ALA GLU
SEQRES 31 A 415 ILE ASP VAL ALA ILE SER ASN SER PHE GLY PHE GLY GLY
SEQRES 32 A 415 THR ASN GLY THR LEU VAL PHE LYS ARG PHE LYS GLY
SEQRES 1 B 415 MET SER GLN ARG ARG VAL VAL ILE THR GLY LEU GLY GLN
SEQRES 2 B 415 VAL SER PRO VAL GLY ASN THR VAL ALA GLU ALA TRP ASP
SEQRES 3 B 415 THR LEU LEU ALA GLY LYS SER GLY ILE GLY ALA ILE THR
SEQRES 4 B 415 ARG PHE ASP ALA SER ASP ILE ASN SER ARG VAL ALA GLY
SEQRES 5 B 415 GLU VAL ARG GLY PHE ASP ILE GLY GLN TYR ILE SER ALA
SEQRES 6 B 415 LYS GLU ALA ARG ARG MET ASP VAL PHE ILE HIS TYR GLY
SEQRES 7 B 415 ILE ALA ALA ALA LEU GLN ALA ILE ALA ASP SER GLY LEU
SEQRES 8 B 415 ASP ASP VAL GLU ASN LEU ASP LYS ASP ARG ILE GLY VAL
SEQRES 9 B 415 ASN ILE GLY SER GLY ILE GLY GLY LEU PRO SER ILE GLU
SEQRES 10 B 415 VAL THR GLY LYS ALA VAL ILE GLU GLY GLY ALA ARG LYS
SEQRES 11 B 415 ILE ASN PRO PHE PHE ILE PRO GLY SER LEU ILE ASN LEU
SEQRES 12 B 415 ILE SER GLY HIS VAL THR ILE LEU LYS GLY TYR ARG GLY
SEQRES 13 B 415 PRO SER TYR GLY MET VAL SER ALA CYS THR THR GLY ALA
SEQRES 14 B 415 HIS ALA ILE GLY ASN SER ALA ARG LEU ILE LYS TYR GLY
SEQRES 15 B 415 ASP ALA ASP ILE MET VAL ALA GLY GLY ALA GLU GLY ALA
SEQRES 16 B 415 ILE SER THR LEU GLY VAL GLY GLY PHE ALA ALA MET LYS
SEQRES 17 B 415 ALA LEU SER THR ARG ASN ASP ASP PRO ALA THR ALA SER
SEQRES 18 B 415 ARG PRO TRP ASP LYS GLY ARG ASP GLY PHE VAL ILE GLY
SEQRES 19 B 415 GLU GLY ALA GLY ILE LEU VAL LEU GLU GLU LEU GLU HIS
SEQRES 20 B 415 ALA LYS LYS ARG GLY ALA LYS ILE TYR ALA GLU ILE VAL
SEQRES 21 B 415 GLY PHE GLY MET SER SER ASP ALA TYR HIS ILE THR ALA
SEQRES 22 B 415 PRO ASN GLU GLU GLY PRO ALA LEU ALA VAL THR ARG ALA
SEQRES 23 B 415 LEU LYS ASP ALA GLY ILE ASN PRO GLU ASP VAL ASP TYR
SEQRES 24 B 415 VAL ASN ALA HIS GLY THR SER THR PRO LEU GLY ASP ALA
SEQRES 25 B 415 ASN GLU THR LYS ALA LEU LYS ARG ALA PHE GLY GLU HIS
SEQRES 26 B 415 ALA TYR LYS THR VAL VAL SER SER THR LYS SER MET THR
SEQRES 27 B 415 GLY HIS LEU LEU GLY ALA ALA GLY GLY VAL GLU ALA VAL
SEQRES 28 B 415 TYR SER ILE LEU ALA ILE HIS ASP GLY LYS ILE PRO PRO
SEQRES 29 B 415 THR ILE ASN ILE PHE GLU GLN ASP VAL GLU ALA GLY CYS
SEQRES 30 B 415 ASP LEU ASP TYR CYS ALA ASN GLU ALA ARG ASP ALA GLU
SEQRES 31 B 415 ILE ASP VAL ALA ILE SER ASN SER PHE GLY PHE GLY GLY
SEQRES 32 B 415 THR ASN GLY THR LEU VAL PHE LYS ARG PHE LYS GLY
HET K A 501 1
HET FMT A 502 3
HET FMT A 503 3
HET K B 501 1
HET FMT B 502 3
HETNAM K POTASSIUM ION
HETNAM FMT FORMIC ACID
FORMUL 3 K 2(K 1+)
FORMUL 4 FMT 3(C H2 O2)
FORMUL 8 HOH *469(H2 O)
HELIX 1 1 THR A 20 ALA A 30 1 11
HELIX 2 2 ASP A 58 TYR A 62 5 5
HELIX 3 3 SER A 64 ARG A 69 1 6
HELIX 4 4 ASP A 72 GLY A 90 1 19
HELIX 5 5 LEU A 91 VAL A 94 5 4
HELIX 6 6 ASP A 98 ASP A 100 5 3
HELIX 7 7 GLY A 112 GLY A 127 1 16
HELIX 8 8 ALA A 128 ILE A 131 5 4
HELIX 9 9 ASN A 142 GLY A 153 1 12
HELIX 10 10 SER A 163 CYS A 165 5 3
HELIX 11 11 THR A 166 GLY A 182 1 17
HELIX 12 12 SER A 197 MET A 207 1 11
HELIX 13 13 ASP A 216 ALA A 220 5 5
HELIX 14 14 LEU A 245 ARG A 251 1 7
HELIX 15 15 GLU A 276 GLY A 291 1 16
HELIX 16 16 ASN A 293 VAL A 297 5 5
HELIX 17 17 THR A 307 GLY A 323 1 17
HELIX 18 18 GLU A 324 LYS A 328 5 5
HELIX 19 19 THR A 334 GLY A 339 1 6
HELIX 20 20 LEU A 341 GLY A 343 5 3
HELIX 21 21 ALA A 344 GLY A 360 1 17
HELIX 22 22 ASP A 372 GLY A 376 5 5
HELIX 23 23 THR B 20 ALA B 30 1 11
HELIX 24 24 ASP B 58 TYR B 62 5 5
HELIX 25 25 SER B 64 ARG B 69 1 6
HELIX 26 26 ASP B 72 GLY B 90 1 19
HELIX 27 27 LEU B 91 VAL B 94 5 4
HELIX 28 28 ASP B 98 ASP B 100 5 3
HELIX 29 29 GLY B 112 GLY B 127 1 16
HELIX 30 30 ALA B 128 ILE B 131 5 4
HELIX 31 31 ASN B 142 GLY B 153 1 12
HELIX 32 32 SER B 163 CYS B 165 5 3
HELIX 33 33 THR B 166 GLY B 182 1 17
HELIX 34 34 SER B 197 ALA B 206 1 10
HELIX 35 35 ASP B 216 ALA B 220 5 5
HELIX 36 36 LEU B 245 ARG B 251 1 7
HELIX 37 37 GLU B 276 GLY B 291 1 16
HELIX 38 38 ASN B 293 VAL B 297 5 5
HELIX 39 39 THR B 307 GLY B 323 1 17
HELIX 40 40 GLU B 324 LYS B 328 5 5
HELIX 41 41 THR B 334 GLY B 339 1 6
HELIX 42 42 LEU B 341 GLY B 343 5 3
HELIX 43 43 ALA B 344 GLY B 360 1 17
HELIX 44 44 ASP B 372 GLY B 376 5 5
SHEET 1 A20 VAL A 330 SER A 332 0
SHEET 2 A20 TYR A 299 ASN A 301 1 N VAL A 300 O VAL A 330
SHEET 3 A20 VAL A 393 GLY A 400 1 O ILE A 395 N ASN A 301
SHEET 4 A20 THR A 404 LYS A 411 -1 O PHE A 410 N ALA A 394
SHEET 5 A20 ALA A 257 SER A 266 -1 N GLU A 258 O LYS A 411
SHEET 6 A20 VAL A 6 VAL A 14 -1 N ILE A 8 O ALA A 257
SHEET 7 A20 GLY A 236 GLU A 244 -1 O ALA A 237 N VAL A 14
SHEET 8 A20 ILE A 186 GLU A 193 -1 N ALA A 189 O LEU A 240
SHEET 9 A20 ILE A 102 GLY A 107 1 N ASN A 105 O VAL A 188
SHEET 10 A20 SER A 158 VAL A 162 1 O TYR A 159 N VAL A 104
SHEET 11 A20 SER B 158 VAL B 162 -1 O GLY B 160 N VAL A 162
SHEET 12 A20 ILE B 102 GLY B 107 1 N VAL B 104 O TYR B 159
SHEET 13 A20 ILE B 186 GLU B 193 1 O VAL B 188 N ASN B 105
SHEET 14 A20 GLY B 236 GLU B 244 -1 O LEU B 240 N ALA B 189
SHEET 15 A20 VAL B 6 VAL B 14 -1 N VAL B 14 O ALA B 237
SHEET 16 A20 ALA B 257 SER B 266 -1 O ALA B 257 N ILE B 8
SHEET 17 A20 THR B 404 LYS B 411 -1 O LYS B 411 N GLU B 258
SHEET 18 A20 VAL B 393 GLY B 400 -1 N ALA B 394 O PHE B 410
SHEET 19 A20 TYR B 299 ASN B 301 1 N ASN B 301 O ILE B 395
SHEET 20 A20 VAL B 330 SER B 332 1 O VAL B 330 N VAL B 300
SHEET 1 B 2 ILE A 35 ALA A 37 0
SHEET 2 B 2 VAL A 50 GLY A 52 -1 O ALA A 51 N GLY A 36
SHEET 1 C 2 LYS A 361 ILE A 362 0
SHEET 2 C 2 ARG A 387 ASP A 388 -1 O ARG A 387 N ILE A 362
SHEET 1 D 2 ILE B 35 ALA B 37 0
SHEET 2 D 2 VAL B 50 GLY B 52 -1 O ALA B 51 N GLY B 36
SHEET 1 E 2 LYS B 361 ILE B 362 0
SHEET 2 E 2 ARG B 387 ASP B 388 -1 O ARG B 387 N ILE B 362
LINK OD1 ASN A 301 K K A 501 1555 1555 2.68
LINK O ASN A 301 K K A 501 1555 1555 2.82
LINK O ALA A 302 K K A 501 1555 1555 2.92
LINK OE1 GLU A 349 K K A 501 1555 1555 2.70
LINK OG SER A 396 K K A 501 1555 1555 2.85
LINK O ASN A 397 K K A 501 1555 1555 2.68
LINK K K A 501 O HOH A 622 1555 1555 3.40
LINK OD1 ASN B 301 K K B 501 1555 1555 2.78
LINK O ASN B 301 K K B 501 1555 1555 2.78
LINK O ALA B 302 K K B 501 1555 1555 2.92
LINK OE1 GLU B 349 K K B 501 1555 1555 2.69
LINK OG SER B 396 K K B 501 1555 1555 2.86
LINK O ASN B 397 K K B 501 1555 1555 2.75
LINK K K B 501 O HOH B 641 1555 1555 3.45
SITE 1 AC1 5 ASN A 301 ALA A 302 GLU A 349 SER A 396
SITE 2 AC1 5 ASN A 397
SITE 1 AC2 2 ARG A 222 HOH A 662
SITE 1 AC3 6 ARG A 49 PRO A 133 THR A 212 ASN A 214
SITE 2 AC3 6 HOH A 739 HOH A 762
SITE 1 AC4 5 ASN B 301 ALA B 302 GLU B 349 SER B 396
SITE 2 AC4 5 ASN B 397
SITE 1 AC5 4 ARG B 70 HOH B 607 HOH B 706 HOH B 792
CRYST1 153.489 153.489 66.470 90.00 90.00 120.00 P 65 12
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 0.006515 0.003762 0.000000 0.00000
SCALE2 0.000000 0.007523 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015044 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
