HEADER LYASE 02-MAY-11 3RSF
TITLE CRYSTAL STRUCTURE OF TM0922, A FUSION OF A DOMAIN OF UNKNOWN FUNCTION
TITLE 2 AND ADP/ATP-DEPENDENT NAD(P)H-HYDRATE DEHYDRATASE FROM THERMOTOGA
TITLE 3 MARITIMA IN COMPLEX WITH P1,P4-DI(ADENOSINE-5') TETRAPHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 4.2.1.93;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: UNKNOWN PEPTIDE, PROBABLY FROM EXPRESSION HOST;
COMPND 8 CHAIN: B
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 243274;
SOURCE 4 STRAIN: MSB8;
SOURCE 5 GENE: TM0922, TM_0922;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMH1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 13 ORGANISM_TAXID: 469008;
SOURCE 14 STRAIN: BL21(DE3);
SOURCE 15 OTHER_DETAILS: UNKNOWN PEPTIDE, PROBABLY FROM EXPRESSION HOST
KEYWDS UNKNOWN FUNCTION, ADP/ATP-DEPENDENT NAD(P)H-HYDRATE DEHYDRATASE,
KEYWDS 2 LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.A.SHUMILIN,M.CYMBOROWSKI,S.A.LESLEY,W.MINOR
REVDAT 5 13-SEP-23 3RSF 1 REMARK
REVDAT 4 13-APR-22 3RSF 1 AUTHOR JRNL REMARK SEQADV
REVDAT 4 2 1 LINK
REVDAT 3 31-OCT-12 3RSF 1 JRNL
REVDAT 2 19-SEP-12 3RSF 1 JRNL VERSN
REVDAT 1 22-JUN-11 3RSF 0
JRNL AUTH I.A.SHUMILIN,M.CYMBOROWSKI,O.CHERTIHIN,K.N.JHA,J.C.HERR,
JRNL AUTH 2 S.A.LESLEY,A.JOACHIMIAK,W.MINOR
JRNL TITL IDENTIFICATION OF UNKNOWN PROTEIN FUNCTION USING METABOLITE
JRNL TITL 2 COCKTAIL SCREENING.
JRNL REF STRUCTURE V. 20 1715 2012
JRNL REFN ISSN 0969-2126
JRNL PMID 22940582
JRNL DOI 10.1016/J.STR.2012.07.016
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 26437
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) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1332
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1823
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK 3 BIN R VALUE (WORKING SET) : 0.2060
REMARK 3 BIN FREE R VALUE SET COUNT : 94
REMARK 3 BIN FREE R VALUE : 0.2880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3782
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 85
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08000
REMARK 3 B22 (A**2) : 0.08000
REMARK 3 B33 (A**2) : -0.15000
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): 0.241
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.186
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.129
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.975
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3879 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2615 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5256 ; 1.733 ; 2.000
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6427 ; 4.216 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 495 ; 5.992 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 152 ;35.652 ;24.539
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 684 ;15.853 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;15.210 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 618 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4255 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 731 ; 0.008 ; 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): 2451 ; 0.844 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1024 ; 0.000 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3954 ; 1.650 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1428 ; 2.938 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1302 ; 4.941 ; 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 : 8
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 1 A 31
REMARK 3 ORIGIN FOR THE GROUP (A): 50.0380 0.1410 69.0430
REMARK 3 T TENSOR
REMARK 3 T11: 0.0183 T22: 0.2796
REMARK 3 T33: 0.0490 T12: -0.0141
REMARK 3 T13: 0.0236 T23: -0.0912
REMARK 3 L TENSOR
REMARK 3 L11: 5.3514 L22: 5.7682
REMARK 3 L33: 2.6159 L12: 4.2177
REMARK 3 L13: 0.4440 L23: -0.0827
REMARK 3 S TENSOR
REMARK 3 S11: -0.0966 S12: 0.4428 S13: -0.3538
REMARK 3 S21: -0.1048 S22: 0.1908 S23: -0.3690
REMARK 3 S31: -0.2114 S32: 0.3948 S33: -0.0942
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 : A 32 A 93
REMARK 3 ORIGIN FOR THE GROUP (A): 46.0680 -14.9500 76.0840
REMARK 3 T TENSOR
REMARK 3 T11: 0.0940 T22: 0.1493
REMARK 3 T33: 0.0558 T12: 0.0727
REMARK 3 T13: -0.0090 T23: -0.0309
REMARK 3 L TENSOR
REMARK 3 L11: 4.1716 L22: 3.0222
REMARK 3 L33: 5.2023 L12: 0.2677
REMARK 3 L13: -0.6130 L23: 1.3331
REMARK 3 S TENSOR
REMARK 3 S11: -0.1919 S12: -0.1374 S13: -0.2101
REMARK 3 S21: 0.3747 S22: 0.1559 S23: 0.0037
REMARK 3 S31: 0.6384 S32: 0.3427 S33: 0.0360
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 : A 94 A 108
REMARK 3 ORIGIN FOR THE GROUP (A): 45.0580 -28.0170 74.0740
REMARK 3 T TENSOR
REMARK 3 T11: 0.7505 T22: 0.2458
REMARK 3 T33: 0.6648 T12: 0.1405
REMARK 3 T13: -0.0671 T23: 0.0301
REMARK 3 L TENSOR
REMARK 3 L11: 6.9118 L22: 8.7675
REMARK 3 L33: 6.8585 L12: 0.2882
REMARK 3 L13: -2.2214 L23: 9.7936
REMARK 3 S TENSOR
REMARK 3 S11: -0.4721 S12: 0.4000 S13: -1.9527
REMARK 3 S21: 1.3690 S22: 0.7512 S23: -0.0603
REMARK 3 S31: 1.4188 S32: 0.4783 S33: -0.2791
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 : A 109 A 209
REMARK 3 ORIGIN FOR THE GROUP (A): 41.0770 -11.3810 60.2630
REMARK 3 T TENSOR
REMARK 3 T11: 0.0073 T22: 0.1745
REMARK 3 T33: 0.0882 T12: 0.0159
REMARK 3 T13: -0.0140 T23: -0.0498
REMARK 3 L TENSOR
REMARK 3 L11: 1.5638 L22: 1.9051
REMARK 3 L33: 3.8442 L12: 0.5813
REMARK 3 L13: 0.2108 L23: 0.4376
REMARK 3 S TENSOR
REMARK 3 S11: -0.0136 S12: 0.1144 S13: -0.1228
REMARK 3 S21: -0.1209 S22: 0.0026 S23: 0.0149
REMARK 3 S31: 0.1612 S32: 0.1804 S33: 0.0110
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 210 A 262
REMARK 3 ORIGIN FOR THE GROUP (A): 17.9350 11.5220 40.9620
REMARK 3 T TENSOR
REMARK 3 T11: 0.1069 T22: 0.1070
REMARK 3 T33: 0.1408 T12: 0.0026
REMARK 3 T13: 0.0254 T23: -0.0454
REMARK 3 L TENSOR
REMARK 3 L11: 0.7123 L22: 0.9118
REMARK 3 L33: 0.2033 L12: -0.2399
REMARK 3 L13: -0.1425 L23: -0.4177
REMARK 3 S TENSOR
REMARK 3 S11: -0.0120 S12: -0.0372 S13: 0.2051
REMARK 3 S21: 0.0063 S22: 0.0848 S23: -0.0468
REMARK 3 S31: -0.0450 S32: 0.0016 S33: -0.0727
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 263 A 352
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9600 7.0090 23.6380
REMARK 3 T TENSOR
REMARK 3 T11: 0.1271 T22: 0.0970
REMARK 3 T33: 0.0201 T12: 0.0037
REMARK 3 T13: 0.0486 T23: 0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 3.5902 L22: 1.9155
REMARK 3 L33: 2.4483 L12: 0.0214
REMARK 3 L13: -0.2765 L23: 0.0492
REMARK 3 S TENSOR
REMARK 3 S11: 0.0811 S12: 0.3665 S13: 0.1267
REMARK 3 S21: -0.2760 S22: -0.0156 S23: -0.1568
REMARK 3 S31: 0.0134 S32: 0.1307 S33: -0.0655
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 353 A 461
REMARK 3 ORIGIN FOR THE GROUP (A): 31.6320 2.2250 39.6340
REMARK 3 T TENSOR
REMARK 3 T11: 0.0554 T22: 0.1367
REMARK 3 T33: 0.1249 T12: -0.0064
REMARK 3 T13: 0.0138 T23: -0.0631
REMARK 3 L TENSOR
REMARK 3 L11: 1.4818 L22: 1.4687
REMARK 3 L33: 1.4660 L12: -0.6907
REMARK 3 L13: 0.2415 L23: -0.4650
REMARK 3 S TENSOR
REMARK 3 S11: 0.0969 S12: 0.0090 S13: 0.1444
REMARK 3 S21: -0.0729 S22: -0.0443 S23: -0.1833
REMARK 3 S31: -0.0010 S32: 0.2686 S33: -0.0526
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 462 A 489
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5360 -0.5900 50.5550
REMARK 3 T TENSOR
REMARK 3 T11: 0.0716 T22: 0.1232
REMARK 3 T33: 0.1067 T12: -0.0005
REMARK 3 T13: -0.0025 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.9735 L22: 8.2383
REMARK 3 L33: 1.7518 L12: 0.5961
REMARK 3 L13: -0.0660 L23: 2.5568
REMARK 3 S TENSOR
REMARK 3 S11: -0.0374 S12: -0.1697 S13: 0.0245
REMARK 3 S21: 0.1466 S22: 0.0245 S23: 0.1279
REMARK 3 S31: -0.0335 S32: -0.0816 S33: 0.0129
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 3RSF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-11.
REMARK 100 THE DEPOSITION ID IS D_1000065320.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : DIAMOND [111]
REMARK 200 OPTICS : BERYLLIUM LENSES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26654
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 11.20
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : 0.08900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 33.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 9.70
REMARK 200 R MERGE FOR SHELL (I) : 0.76800
REMARK 200 R SYM FOR SHELL (I) : 0.76800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.242
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: HKL-3000 MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2AX3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA CACODYLATE, 1.6 M NA CITRATE,
REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 61.18900
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 61.18900
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 77.71700
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 61.18900
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 61.18900
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 77.71700
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 61.18900
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 61.18900
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 77.71700
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 61.18900
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 61.18900
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 77.71700
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 61.18900
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 61.18900
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 77.71700
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 61.18900
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 61.18900
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 77.71700
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 61.18900
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 61.18900
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 77.71700
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 61.18900
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 61.18900
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 77.71700
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: HEXADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 48600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 137110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -165.0 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 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 155.43400
REMARK 350 BIOMT1 6 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 155.43400
REMARK 350 BIOMT1 7 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 7 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 7 0.000000 0.000000 -1.000000 155.43400
REMARK 350 BIOMT1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 8 0.000000 0.000000 -1.000000 155.43400
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 558 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 -11
REMARK 465 GLY A -10
REMARK 465 SER A -9
REMARK 465 ASP A -8
REMARK 465 LYS A -7
REMARK 465 ILE A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 GLU A 490
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 HIS A 0 CB CG ND1 CD2 CE1 NE2
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 LYS A 77 -88.02 -98.93
REMARK 500 ASP A 147 -65.23 79.35
REMARK 500 ARG A 161 -56.32 63.99
REMARK 500 GLU A 336 56.81 -101.28
REMARK 500 ALA A 343 -126.61 56.57
REMARK 500 SER A 403 -174.63 -176.06
REMARK 500 GLN A 467 -168.64 -107.93
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 B4P A 492
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 491 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 52 OD1
REMARK 620 2 ASP A 114 O 91.5
REMARK 620 3 ASP A 114 OD2 145.6 62.6
REMARK 620 4 PHE A 117 O 76.4 155.1 117.4
REMARK 620 5 VAL A 146 O 75.1 87.3 122.1 109.9
REMARK 620 6 VAL A 148 O 128.3 125.2 86.1 78.4 72.3
REMARK 620 7 SER A 150 OG 105.1 100.1 61.8 63.4 172.6 102.6
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 491
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B4P A 492
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2AX3 RELATED DB: PDB
REMARK 900 APO-PROTEIN
REMARK 900 RELATED ID: 3RNO RELATED DB: PDB
REMARK 900 RELATED ID: 3RO7 RELATED DB: PDB
REMARK 900 RELATED ID: 3ROE RELATED DB: PDB
REMARK 900 RELATED ID: 3ROG RELATED DB: PDB
REMARK 900 RELATED ID: 3ROX RELATED DB: PDB
REMARK 900 RELATED ID: 3ROZ RELATED DB: PDB
REMARK 900 RELATED ID: 3RRB RELATED DB: PDB
REMARK 900 RELATED ID: 3RRE RELATED DB: PDB
REMARK 900 RELATED ID: 3RRF RELATED DB: PDB
REMARK 900 RELATED ID: 3RRJ RELATED DB: PDB
REMARK 900 RELATED ID: 3RS8 RELATED DB: PDB
REMARK 900 RELATED ID: 3RS9 RELATED DB: PDB
REMARK 900 RELATED ID: 3RSG RELATED DB: PDB
REMARK 900 RELATED ID: 3RSQ RELATED DB: PDB
REMARK 900 RELATED ID: 3RSS RELATED DB: PDB
REMARK 900 RELATED ID: 3RT7 RELATED DB: PDB
REMARK 900 RELATED ID: 3RT9 RELATED DB: PDB
REMARK 900 RELATED ID: 3RTA RELATED DB: PDB
REMARK 900 RELATED ID: 3RTB RELATED DB: PDB
REMARK 900 RELATED ID: 3RTC RELATED DB: PDB
REMARK 900 RELATED ID: 3RTD RELATED DB: PDB
REMARK 900 RELATED ID: 3RTE RELATED DB: PDB
REMARK 900 RELATED ID: 3RTG RELATED DB: PDB
REMARK 900 RELATED ID: 3RU2 RELATED DB: PDB
REMARK 900 RELATED ID: 3RU3 RELATED DB: PDB
DBREF 3RSF A 1 490 UNP Q9X024 Q9X024_THEMA 1 490
DBREF 3RSF B 1 7 PDB 3RSF 3RSF 1 7
SEQADV 3RSF MET A -11 UNP Q9X024 EXPRESSION TAG
SEQADV 3RSF GLY A -10 UNP Q9X024 EXPRESSION TAG
SEQADV 3RSF SER A -9 UNP Q9X024 EXPRESSION TAG
SEQADV 3RSF ASP A -8 UNP Q9X024 EXPRESSION TAG
SEQADV 3RSF LYS A -7 UNP Q9X024 EXPRESSION TAG
SEQADV 3RSF ILE A -6 UNP Q9X024 EXPRESSION TAG
SEQADV 3RSF HIS A -5 UNP Q9X024 EXPRESSION TAG
SEQADV 3RSF HIS A -4 UNP Q9X024 EXPRESSION TAG
SEQADV 3RSF HIS A -3 UNP Q9X024 EXPRESSION TAG
SEQADV 3RSF HIS A -2 UNP Q9X024 EXPRESSION TAG
SEQADV 3RSF HIS A -1 UNP Q9X024 EXPRESSION TAG
SEQADV 3RSF HIS A 0 UNP Q9X024 EXPRESSION TAG
SEQRES 1 A 502 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 A 502 LYS GLU ILE ASP GLU LEU THR ILE LYS GLU TYR GLY VAL
SEQRES 3 A 502 ASP SER ARG ILE LEU MET GLU ARG ALA GLY ILE SER VAL
SEQRES 4 A 502 VAL LEU ALA MET GLU GLU GLU LEU GLY ASN LEU SER ASP
SEQRES 5 A 502 TYR ARG PHE LEU VAL LEU CYS GLY GLY GLY ASN ASN GLY
SEQRES 6 A 502 GLY ASP GLY PHE VAL VAL ALA ARG ASN LEU LEU GLY VAL
SEQRES 7 A 502 VAL LYS ASP VAL LEU VAL VAL PHE LEU GLY LYS LYS LYS
SEQRES 8 A 502 THR PRO ASP CYS GLU TYR ASN TYR GLY LEU TYR LYS LYS
SEQRES 9 A 502 PHE GLY GLY LYS VAL VAL GLU GLN PHE GLU PRO SER ILE
SEQRES 10 A 502 LEU ASN GLU PHE ASP VAL VAL VAL ASP ALA ILE PHE GLY
SEQRES 11 A 502 THR GLY LEU ARG GLY GLU ILE THR GLY GLU TYR ALA GLU
SEQRES 12 A 502 ILE ILE ASN LEU VAL ASN LYS SER GLY LYS VAL VAL VAL
SEQRES 13 A 502 SER VAL ASP VAL PRO SER GLY ILE ASP SER ASN THR GLY
SEQRES 14 A 502 LYS VAL LEU ARG THR ALA VAL LYS ALA ASP LEU THR VAL
SEQRES 15 A 502 THR PHE GLY VAL PRO LYS ILE GLY HIS ILE LEU PHE PRO
SEQRES 16 A 502 GLY ARG ASP LEU THR GLY LYS LEU LYS VAL ALA ASN ILE
SEQRES 17 A 502 GLY HIS PRO VAL HIS LEU ILE ASN SER ILE ASN ARG TYR
SEQRES 18 A 502 VAL ILE THR ARG GLU MET VAL ARG SER LEU LEU PRO GLU
SEQRES 19 A 502 ARG PRO ARG ASP SER HIS LYS GLY THR TYR GLY LYS VAL
SEQRES 20 A 502 LEU ILE ILE ALA GLY SER ARG LEU TYR SER GLY ALA PRO
SEQRES 21 A 502 VAL LEU SER GLY MET GLY SER LEU LYS VAL GLY THR GLY
SEQRES 22 A 502 LEU VAL LYS LEU ALA VAL PRO PHE PRO GLN ASN LEU ILE
SEQRES 23 A 502 ALA THR SER ARG PHE PRO GLU LEU ILE SER VAL PRO ILE
SEQRES 24 A 502 ASP THR GLU LYS GLY PHE PHE SER LEU GLN ASN LEU GLN
SEQRES 25 A 502 GLU CYS LEU GLU LEU SER LYS ASP VAL ASP VAL VAL ALA
SEQRES 26 A 502 ILE GLY PRO GLY LEU GLY ASN ASN GLU HIS VAL ARG GLU
SEQRES 27 A 502 PHE VAL ASN GLU PHE LEU LYS THR LEU GLU LYS PRO ALA
SEQRES 28 A 502 VAL ILE ASP ALA ASP ALA ILE ASN VAL LEU ASP THR SER
SEQRES 29 A 502 VAL LEU LYS GLU ARG LYS SER PRO ALA VAL LEU THR PRO
SEQRES 30 A 502 HIS PRO GLY GLU MET ALA ARG LEU VAL LYS LYS THR VAL
SEQRES 31 A 502 GLY ASP VAL LYS TYR ASN TYR GLU LEU ALA GLU GLU PHE
SEQRES 32 A 502 ALA LYS GLU ASN ASP CYS VAL LEU VAL LEU LYS SER ALA
SEQRES 33 A 502 THR THR ILE VAL THR ASP GLY GLU LYS THR LEU PHE ASN
SEQRES 34 A 502 ILE THR GLY ASN THR GLY LEU SER LYS GLY GLY SER GLY
SEQRES 35 A 502 ASP VAL LEU THR GLY MET ILE ALA GLY PHE ILE ALA GLN
SEQRES 36 A 502 GLY LEU SER PRO LEU GLU ALA SER THR VAL SER VAL TYR
SEQRES 37 A 502 LEU HIS GLY PHE ALA ALA GLU LEU PHE GLU GLN ASP GLU
SEQRES 38 A 502 ARG GLY LEU THR ALA SER GLU LEU LEU ARG LEU ILE PRO
SEQRES 39 A 502 GLU ALA ILE ARG ARG LEU LYS GLU
SEQRES 1 B 7 ALA ALA TRP LEU PHE GLU ALA
HET K A 491 1
HET B4P A 492 35
HETNAM K POTASSIUM ION
HETNAM B4P BIS(ADENOSINE)-5'-TETRAPHOSPHATE
FORMUL 3 K K 1+
FORMUL 4 B4P C20 H28 N10 O19 P4
FORMUL 5 HOH *85(H2 O)
HELIX 1 1 MET A 1 GLU A 11 1 11
HELIX 2 2 ASP A 15 GLY A 36 1 22
HELIX 3 3 GLY A 50 LEU A 64 1 15
HELIX 4 4 THR A 80 PHE A 93 1 14
HELIX 5 5 GLU A 102 PHE A 109 5 8
HELIX 6 6 THR A 126 SER A 139 1 14
HELIX 7 7 LYS A 176 LEU A 181 1 6
HELIX 8 8 PRO A 183 GLY A 189 1 7
HELIX 9 9 PRO A 199 SER A 205 1 7
HELIX 10 10 THR A 212 LEU A 220 1 9
HELIX 11 11 HIS A 228 TYR A 232 5 5
HELIX 12 12 GLY A 246 VAL A 258 1 13
HELIX 13 13 GLN A 271 PHE A 279 1 9
HELIX 14 14 SER A 295 GLN A 297 5 3
HELIX 15 15 ASN A 298 LYS A 307 1 10
HELIX 16 16 ASN A 321 LEU A 335 1 15
HELIX 17 17 ASP A 342 LEU A 349 1 8
HELIX 18 18 ASP A 350 ARG A 357 1 8
HELIX 19 19 HIS A 366 LYS A 375 1 10
HELIX 20 20 THR A 377 LYS A 382 1 6
HELIX 21 21 ASN A 384 ASP A 396 1 13
HELIX 22 22 ASN A 421 SER A 425 5 5
HELIX 23 23 GLY A 428 GLN A 443 1 16
HELIX 24 24 SER A 446 LEU A 464 1 19
HELIX 25 25 ASP A 468 LEU A 472 5 5
HELIX 26 26 THR A 473 LYS A 489 1 17
SHEET 1 A 8 VAL A 97 VAL A 98 0
SHEET 2 A 8 ASP A 69 PHE A 74 1 N PHE A 74 O VAL A 98
SHEET 3 A 8 ARG A 42 CYS A 47 1 N PHE A 43 O ASP A 69
SHEET 4 A 8 VAL A 111 ALA A 115 1 O VAL A 111 N LEU A 44
SHEET 5 A 8 VAL A 142 VAL A 146 1 O VAL A 144 N ASP A 114
SHEET 6 A 8 LEU A 168 PHE A 172 1 O LEU A 168 N SER A 145
SHEET 7 A 8 LYS A 190 ALA A 194 1 O ALA A 194 N THR A 171
SHEET 8 A 8 PHE B 5 GLU B 6 -1 O GLU B 6 N VAL A 193
SHEET 1 B10 ARG A 208 VAL A 210 0
SHEET 2 B10 THR A 414 ASN A 417 1 O PHE A 416 N TYR A 209
SHEET 3 B10 THR A 406 THR A 409 -1 N VAL A 408 O LEU A 415
SHEET 4 B10 VAL A 398 LEU A 401 -1 N LEU A 401 O ILE A 407
SHEET 5 B10 ALA A 361 LEU A 363 1 N LEU A 363 O VAL A 400
SHEET 6 B10 ALA A 339 ILE A 341 1 N ILE A 341 O VAL A 362
SHEET 7 B10 VAL A 311 ILE A 314 1 N ILE A 314 O VAL A 340
SHEET 8 B10 LYS A 234 ILE A 238 1 N ILE A 238 O ALA A 313
SHEET 9 B10 LEU A 262 PRO A 268 1 O LYS A 264 N ILE A 237
SHEET 10 B10 ILE A 283 ILE A 287 1 O VAL A 285 N LEU A 265
LINK OD1 ASN A 52 K K A 491 1555 1555 2.97
LINK O ASP A 114 K K A 491 1555 1555 3.04
LINK OD2 ASP A 114 K K A 491 1555 1555 3.35
LINK O PHE A 117 K K A 491 1555 1555 2.94
LINK O VAL A 146 K K A 491 1555 1555 2.99
LINK O VAL A 148 K K A 491 1555 1555 2.86
LINK OG SER A 150 K K A 491 1555 1555 3.06
CISPEP 1 PHE A 182 PRO A 183 0 4.33
CISPEP 2 PHE A 269 PRO A 270 0 0.43
SITE 1 AC1 6 ASN A 52 ASP A 114 PHE A 117 VAL A 146
SITE 2 AC1 6 VAL A 148 SER A 150
SITE 1 AC2 15 LYS A 10 GLY A 50 ASN A 51 ASN A 52
SITE 2 AC2 15 PHE A 117 GLY A 118 THR A 119 GLY A 120
SITE 3 AC2 15 ARG A 122 GLY A 123 GLU A 124 TYR A 129
SITE 4 AC2 15 LYS A 375 HOH A 501 HOH A 526
CRYST1 122.378 122.378 155.434 90.00 90.00 90.00 I 4 2 2 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 0.008171 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008171 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006434 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
