HEADER HYDROLASE 11-AUG-15 5D6A
TITLE 2.7 ANGSTROM CRYSTAL STRUCTURE OF ABC TRANSPORTER ATPASE FROM VIBRIO
TITLE 2 VULNIFICUS IN COMPLEX WITH ADENYLYL-IMIDODIPHOSPHATE (AMP-PNP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PREDICTED ATPASE OF THE ABC CLASS;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO VULNIFICUS;
SOURCE 3 ORGANISM_TAXID: 196600;
SOURCE 4 STRAIN: YJ016;
SOURCE 5 GENE: VVA0769;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS ABC TRANSPORTER ATPASE, AMP-PNP, STRUCTURAL GENOMICS, CENTER FOR
KEYWDS 2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.MINASOV,Z.WAWRZAK,L.SHUVALOVA,I.DUBROVSKA,K.FLORES,S.GRIMSHAW,
AUTHOR 2 K.KWON,W.F.ANDERSON,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
AUTHOR 3 DISEASES (CSGID)
REVDAT 2 22-NOV-17 5D6A 1 REMARK
REVDAT 1 26-AUG-15 5D6A 0
JRNL AUTH G.MINASOV,Z.WAWRZAK,L.SHUVALOVA,I.DUBROVSKA,K.FLORES,
JRNL AUTH 2 S.GRIMSHAW,K.KWON,W.F.ANDERSON,
JRNL AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
JRNL AUTH 4 (CSGID)
JRNL TITL 2.7 ANGSTROM CRYSTAL STRUCTURE OF ABC TRANSPORTER ATPASE
JRNL TITL 2 FROM VIBRIO VULNIFICUS IN COMPLEX WITH
JRNL TITL 3 ADENYLYL-IMIDODIPHOSPHATE (AMP-PNP)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 13687
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1535
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 987
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE SET COUNT : 111
REMARK 3 BIN FREE R VALUE : 0.3240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4297
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 84
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 57.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.15000
REMARK 3 B22 (A**2) : -0.15000
REMARK 3 B33 (A**2) : 0.50000
REMARK 3 B12 (A**2) : -0.08000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.407
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.283
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.361
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.908
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4433 ; 0.004 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4210 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6006 ; 1.051 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9672 ; 0.670 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 550 ; 1.771 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 213 ;22.501 ;24.460
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 722 ; 7.764 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ; 7.935 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 666 ; 0.062 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5068 ; 0.019 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1033 ; 0.015 ; 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): 2200 ; 1.156 ; 3.470
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2199 ; 1.155 ; 3.468
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2750 ; 2.049 ; 5.203
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2751 ; 2.049 ; 5.206
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2233 ; 1.147 ; 3.596
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2234 ; 1.147 ; 3.597
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3257 ; 1.928 ; 5.346
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5039 ; 4.125 ;27.563
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5030 ; 4.086 ;27.547
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 : 6
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 -2 A 125
REMARK 3 ORIGIN FOR THE GROUP (A): -46.1405 54.7025 -5.0982
REMARK 3 T TENSOR
REMARK 3 T11: 0.1247 T22: 0.1686
REMARK 3 T33: 0.2233 T12: -0.0457
REMARK 3 T13: 0.0003 T23: 0.0813
REMARK 3 L TENSOR
REMARK 3 L11: 2.5783 L22: 4.2054
REMARK 3 L33: 2.7904 L12: -1.5642
REMARK 3 L13: -1.0956 L23: 0.9679
REMARK 3 S TENSOR
REMARK 3 S11: 0.0148 S12: -0.0410 S13: 0.3827
REMARK 3 S21: -0.0914 S22: 0.2529 S23: 0.4665
REMARK 3 S31: -0.3949 S32: -0.2305 S33: -0.2677
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 126 A 216
REMARK 3 ORIGIN FOR THE GROUP (A): -31.8481 43.0456 -11.2409
REMARK 3 T TENSOR
REMARK 3 T11: 0.1472 T22: 0.2004
REMARK 3 T33: 0.0342 T12: -0.1400
REMARK 3 T13: 0.0417 T23: -0.0314
REMARK 3 L TENSOR
REMARK 3 L11: 2.3798 L22: 3.7125
REMARK 3 L33: 0.8967 L12: -1.4882
REMARK 3 L13: -0.1778 L23: 0.0889
REMARK 3 S TENSOR
REMARK 3 S11: 0.0598 S12: 0.3283 S13: 0.0838
REMARK 3 S21: -0.2401 S22: -0.0300 S23: 0.0949
REMARK 3 S31: -0.1755 S32: 0.1254 S33: -0.0298
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 217 A 340
REMARK 3 ORIGIN FOR THE GROUP (A): -26.2090 24.0653 5.2704
REMARK 3 T TENSOR
REMARK 3 T11: 0.0313 T22: 0.0837
REMARK 3 T33: 0.1844 T12: -0.0347
REMARK 3 T13: 0.0339 T23: -0.0671
REMARK 3 L TENSOR
REMARK 3 L11: 1.2055 L22: 1.3653
REMARK 3 L33: 2.4073 L12: 0.3312
REMARK 3 L13: -0.6379 L23: -0.1529
REMARK 3 S TENSOR
REMARK 3 S11: -0.0709 S12: 0.0340 S13: -0.3606
REMARK 3 S21: 0.0193 S22: 0.0763 S23: -0.1990
REMARK 3 S31: 0.1034 S32: 0.1460 S33: -0.0054
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 341 A 360
REMARK 3 ORIGIN FOR THE GROUP (A): -14.2080 13.2073 22.2978
REMARK 3 T TENSOR
REMARK 3 T11: 0.2317 T22: 0.1519
REMARK 3 T33: 0.2154 T12: -0.0048
REMARK 3 T13: -0.0086 T23: 0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.4514 L22: 0.9100
REMARK 3 L33: 6.9826 L12: -0.6377
REMARK 3 L13: 1.5330 L23: -2.1021
REMARK 3 S TENSOR
REMARK 3 S11: -0.0232 S12: -0.0841 S13: -0.0799
REMARK 3 S21: 0.0703 S22: 0.1355 S23: 0.1200
REMARK 3 S31: -0.0814 S32: 0.0727 S33: -0.1122
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 361 A 462
REMARK 3 ORIGIN FOR THE GROUP (A): -25.1998 19.0998 7.8665
REMARK 3 T TENSOR
REMARK 3 T11: 0.0933 T22: 0.1251
REMARK 3 T33: 0.2271 T12: 0.0002
REMARK 3 T13: 0.0185 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 3.7237 L22: 2.5247
REMARK 3 L33: 1.8896 L12: -1.1578
REMARK 3 L13: -0.8768 L23: 0.4171
REMARK 3 S TENSOR
REMARK 3 S11: -0.2010 S12: -0.2570 S13: -0.6023
REMARK 3 S21: 0.0406 S22: 0.1777 S23: -0.2968
REMARK 3 S31: 0.3346 S32: 0.2730 S33: 0.0233
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 463 A 551
REMARK 3 ORIGIN FOR THE GROUP (A): -42.3121 33.4952 10.8465
REMARK 3 T TENSOR
REMARK 3 T11: 0.0217 T22: 0.0600
REMARK 3 T33: 0.0507 T12: -0.0195
REMARK 3 T13: 0.0293 T23: -0.0300
REMARK 3 L TENSOR
REMARK 3 L11: 3.2246 L22: 4.4933
REMARK 3 L33: 3.4592 L12: 0.7912
REMARK 3 L13: 0.2542 L23: -1.0840
REMARK 3 S TENSOR
REMARK 3 S11: -0.2083 S12: 0.0320 S13: -0.2107
REMARK 3 S21: -0.0151 S22: 0.1736 S23: 0.1690
REMARK 3 S31: -0.0019 S32: -0.2610 S33: 0.0347
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 5D6A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1000212734.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : C(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15243
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.00
REMARK 200 R MERGE (I) : 0.11700
REMARK 200 R SYM (I) : 0.11700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.20
REMARK 200 R MERGE FOR SHELL (I) : 0.62100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000, PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 5.9 MG/ML, 0.5M SODIUM
REMARK 280 CHLORIDE, 0.01M TRIS-HCL (PH 8.3), 1MM AMPPNP; SCREEN: PACT (C2),
REMARK 280 0.1M PCB BUFFER (PH 5.0), 25% (W/V) PEG 1500, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 28.45133
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 56.90267
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 56.90267
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 28.45133
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: 7820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 28.45133
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 764 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 771 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 MSE A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 GLY A -14
REMARK 465 VAL A -13
REMARK 465 ASP A -12
REMARK 465 LEU A -11
REMARK 465 GLY A -10
REMARK 465 THR A -9
REMARK 465 GLU A -8
REMARK 465 ASN A -7
REMARK 465 LEU A -6
REMARK 465 TYR A -5
REMARK 465 PHE A -4
REMARK 465 GLN A -3
REMARK 465 GLN A 423
REMARK 465 ARG A 424
REMARK 465 HIS A 425
REMARK 465 ASN A 426
REMARK 465 GLU A 427
REMARK 465 SER A 428
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 PHE A 28 -174.14 -69.41
REMARK 500 ARG A 127 -28.64 -150.42
REMARK 500 PHE A 244 34.58 70.10
REMARK 500 HIS A 289 52.66 30.53
REMARK 500 TYR A 295 -53.24 -125.31
REMARK 500 ASP A 307 57.57 -145.76
REMARK 500 ASP A 312 79.72 -154.86
REMARK 500 SER A 314 -178.15 -69.93
REMARK 500 VAL A 356 56.15 -119.81
REMARK 500 LYS A 358 -104.07 -106.73
REMARK 500 MSE A 385 -111.04 -115.42
REMARK 500 ASN A 504 72.91 -156.90
REMARK 500 LEU A 513 36.31 -96.65
REMARK 500 ASP A 515 -42.38 69.24
REMARK 500 ALA A 516 32.73 -97.56
REMARK 500 ASP A 526 58.93 -113.88
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 NA A 601 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP A 602 O3G
REMARK 620 2 ANP A 602 O2B 77.4
REMARK 620 3 SER A 314 OG 69.0 140.6
REMARK 620 4 SER A 316 OG 63.6 139.3 10.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP A 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CSGID-IDP91330 RELATED DB: TARGETTRACK
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE HAS NOT YET BEEN DEPOSITED TO UNIPROT. SEE WP_
REMARK 999 011081233.1 DATABASE REFERENCE
DBREF 5D6A A 1 551 UNP Q7MEA1 Q7MEA1_VIBVY 23 573
SEQADV 5D6A MSE A -23 UNP Q7MEA1 INITIATING METHIONINE
SEQADV 5D6A HIS A -22 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A HIS A -21 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A HIS A -20 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A HIS A -19 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A HIS A -18 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A HIS A -17 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A SER A -16 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A SER A -15 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A GLY A -14 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A VAL A -13 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A ASP A -12 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A LEU A -11 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A GLY A -10 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A THR A -9 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A GLU A -8 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A ASN A -7 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A LEU A -6 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A TYR A -5 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A PHE A -4 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A GLN A -3 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A SER A -2 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A ASN A -1 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A ALA A 0 UNP Q7MEA1 EXPRESSION TAG
SEQADV 5D6A GLY A 264 UNP Q7MEA1 SER 286 SEE REMARK 999
SEQADV 5D6A LYS A 303 UNP Q7MEA1 ARG 325 SEE REMARK 999
SEQADV 5D6A SER A 510 UNP Q7MEA1 ASN 532 SEE REMARK 999
SEQRES 1 A 575 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 575 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MSE ASP
SEQRES 3 A 575 GLN LEU ILE ALA LYS LEU LYS LYS LEU GLU LYS GLN ASN
SEQRES 4 A 575 TYR ARG ALA TYR GLN GLN ILE LYS GLY GLN TYR ASN PHE
SEQRES 5 A 575 THR ASP PHE ASP LEU PHE ILE ASP HIS ILE GLN SER ASP
SEQRES 6 A 575 PRO TYR ALA SER ALA SER ARG PHE ARG ALA PHE ARG ALA
SEQRES 7 A 575 TRP SER LEU THR GLY LEU SER TRP LEU LYS GLU GLU SER
SEQRES 8 A 575 ALA ALA PHE GLN LEU GLY ALA ARG ASP PHE ILE ALA ARG
SEQRES 9 A 575 SER PHE ALA GLU PHE ALA LYS GLN GLU ASN ALA ILE ALA
SEQRES 10 A 575 ILE SER LEU HIS GLY GLN THR VAL LEU ASP SER THR SER
SEQRES 11 A 575 VAL LEU PHE THR GLU GLU GLY ILE GLU LEU ARG PHE ARG
SEQRES 12 A 575 VAL ASN LEU PRO ALA GLU GLY ARG ASP ILE LEU ALA LYS
SEQRES 13 A 575 LYS ALA ILE ASN ILE ILE THR PHE HIS LEU PRO LYS PHE
SEQRES 14 A 575 ILE ARG ARG SER THR ILE GLU ARG GLU LEU ASP LYS GLU
SEQRES 15 A 575 ALA LEU LEU THR HIS CYS GLN VAL VAL GLU ASP GLN GLU
SEQRES 16 A 575 ALA LEU ARG GLU GLN LEU GLU VAL ASN GLY LEU VAL SER
SEQRES 17 A 575 PHE VAL ALA ASN GLY SER ILE LEU PRO ARG VAL ALA GLY
SEQRES 18 A 575 ASN CYS ASP LEU PRO MSE LYS ASP ALA VAL GLU PHE THR
SEQRES 19 A 575 ALA PRO GLU SER LEU GLN VAL THR LEU HIS ALA PRO ASN
SEQRES 20 A 575 ARG GLY TYR VAL THR GLY LEU GLY ILE PRO LYS GLY ILE
SEQRES 21 A 575 THR LEU ILE VAL GLY GLY GLY PHE HIS GLY LYS SER THR
SEQRES 22 A 575 LEU LEU ASN ALA ILE GLU ARG SER ILE TYR ASN HIS ILE
SEQRES 23 A 575 PRO GLY ASP GLY ARG GLU TYR ILE VAL THR ASP GLY SER
SEQRES 24 A 575 ALA MSE LYS ILE ARG ALA GLU GLU GLY ARG CYS VAL HIS
SEQRES 25 A 575 HIS LEU ASN LEU SER ASN TYR ILE ASN HIS LEU PRO MSE
SEQRES 26 A 575 GLY LYS ASP THR ALA ASP PHE THR THR GLN ASP ALA SER
SEQRES 27 A 575 GLY SER THR SER GLN ALA ALA TRP LEU GLN GLU SER VAL
SEQRES 28 A 575 GLU ALA GLY ALA SER THR LEU LEU ILE ASP GLU ASP THR
SEQRES 29 A 575 SER ALA THR ASN PHE MSE ILE ARG ASP GLU ARG MSE GLN
SEQRES 30 A 575 ALA LEU VAL ALA LYS GLY ASP GLU PRO ILE THR PRO LEU
SEQRES 31 A 575 VAL ASP ARG ILE GLY GLN LEU ARG ASP GLU LEU GLU ILE
SEQRES 32 A 575 SER THR ILE ILE VAL MSE GLY GLY SER GLY ASP TYR LEU
SEQRES 33 A 575 ASP VAL ALA ASP ASN VAL ILE GLN MSE HIS ASP TYR GLN
SEQRES 34 A 575 ALA LEU ASP VAL THR GLU LYS ALA LYS GLU VAL ILE GLN
SEQRES 35 A 575 LEU HIS PRO THR GLN ARG HIS ASN GLU SER GLU ALA PRO
SEQRES 36 A 575 LEU VAL THR PHE PRO PRO ARG ALA LEU HIS CYS SER ALA
SEQRES 37 A 575 LEU MSE ASN ILE LEU THR ASP GLY LYS PHE ARG VAL SER
SEQRES 38 A 575 ALA LYS GLY LYS ASP SER LEU ARG PHE GLY LYS GLU PHE
SEQRES 39 A 575 THR ASP LEU SER ALA LEU GLU GLN LEU GLU SER SER ASP
SEQRES 40 A 575 GLU VAL ASN ALA ILE GLY TRP VAL TRP TYR GLN LEU ALA
SEQRES 41 A 575 GLN HIS ALA GLY TRP ASN SER ASN PRO ALA LYS GLN ILE
SEQRES 42 A 575 SER GLU LEU LEU GLY ASP ALA TRP PHE GLN ASN MSE PRO
SEQRES 43 A 575 GLN HIS GLY ASP LEU ALA LYS PRO ARG PRO ILE ASP VAL
SEQRES 44 A 575 MSE ALA ALA LEU ASN ARG MSE ARG LYS SER GLN PHE ARG
SEQRES 45 A 575 ASN ASN HIS
MODRES 5D6A MSE A 1 MET MODIFIED RESIDUE
MODRES 5D6A MSE A 203 MET MODIFIED RESIDUE
MODRES 5D6A MSE A 277 MET MODIFIED RESIDUE
MODRES 5D6A MSE A 301 MET MODIFIED RESIDUE
MODRES 5D6A MSE A 346 MET MODIFIED RESIDUE
MODRES 5D6A MSE A 352 MET MODIFIED RESIDUE
MODRES 5D6A MSE A 385 MET MODIFIED RESIDUE
MODRES 5D6A MSE A 401 MET MODIFIED RESIDUE
MODRES 5D6A MSE A 446 MET MODIFIED RESIDUE
MODRES 5D6A MSE A 521 MET MODIFIED RESIDUE
MODRES 5D6A MSE A 536 MET MODIFIED RESIDUE
MODRES 5D6A MSE A 542 MET MODIFIED RESIDUE
HET MSE A 1 16
HET MSE A 203 8
HET MSE A 277 8
HET MSE A 301 8
HET MSE A 346 16
HET MSE A 352 8
HET MSE A 385 8
HET MSE A 401 8
HET MSE A 446 8
HET MSE A 521 8
HET MSE A 536 8
HET MSE A 542 8
HET NA A 601 1
HET ANP A 602 31
HETNAM MSE SELENOMETHIONINE
HETNAM NA SODIUM ION
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 2 NA NA 1+
FORMUL 3 ANP C10 H17 N6 O12 P3
FORMUL 4 HOH *84(H2 O)
HELIX 1 AA1 SER A -2 LYS A 10 1 13
HELIX 2 AA2 ASN A 15 LYS A 23 5 9
HELIX 3 AA3 SER A 56 THR A 58 5 3
HELIX 4 AA4 LEU A 60 GLU A 66 5 7
HELIX 5 AA5 SER A 67 ALA A 86 1 20
HELIX 6 AA6 LEU A 130 PHE A 140 1 11
HELIX 7 AA7 PHE A 140 SER A 149 1 10
HELIX 8 AA8 THR A 150 LEU A 155 5 6
HELIX 9 AA9 ASP A 156 GLN A 176 1 21
HELIX 10 AB1 PRO A 212 SER A 214 5 3
HELIX 11 AB2 GLY A 246 SER A 257 1 12
HELIX 12 AB3 SER A 314 ALA A 329 1 16
HELIX 13 AB4 ASP A 339 SER A 341 5 3
HELIX 14 AB5 ALA A 342 ILE A 347 1 6
HELIX 15 AB6 ASP A 349 VAL A 356 1 8
HELIX 16 AB7 PRO A 365 GLU A 378 1 14
HELIX 17 AB8 GLY A 389 ASP A 393 5 5
HELIX 18 AB9 VAL A 409 HIS A 420 1 12
HELIX 19 AC1 SER A 443 GLY A 452 1 10
HELIX 20 AC2 SER A 481 ALA A 496 1 16
HELIX 21 AC3 ASN A 504 LEU A 513 1 10
HELIX 22 AC4 ARG A 531 ARG A 541 1 11
SHEET 1 AA1 5 GLY A 24 ASN A 27 0
SHEET 2 AA1 5 ASP A 32 HIS A 37 -1 O LEU A 33 N TYR A 26
SHEET 3 AA1 5 SER A 47 ALA A 54 -1 O ARG A 50 N PHE A 34
SHEET 4 AA1 5 GLY A 113 VAL A 120 -1 O PHE A 118 N PHE A 49
SHEET 5 AA1 5 ILE A 92 ALA A 93 -1 N ALA A 93 O ARG A 119
SHEET 1 AA2 5 GLY A 24 ASN A 27 0
SHEET 2 AA2 5 ASP A 32 HIS A 37 -1 O LEU A 33 N TYR A 26
SHEET 3 AA2 5 SER A 47 ALA A 54 -1 O ARG A 50 N PHE A 34
SHEET 4 AA2 5 GLY A 113 VAL A 120 -1 O PHE A 118 N PHE A 49
SHEET 5 AA2 5 VAL A 107 PHE A 109 -1 N LEU A 108 O GLU A 115
SHEET 1 AA3 2 THR A 100 VAL A 101 0
SHEET 2 AA3 2 ASN A 260 HIS A 261 -1 O ASN A 260 N VAL A 101
SHEET 1 AA4 2 ALA A 124 GLU A 125 0
SHEET 2 AA4 2 ASP A 128 ILE A 129 -1 O ASP A 128 N GLU A 125
SHEET 1 AA5 4 GLN A 216 ALA A 221 0
SHEET 2 AA5 4 GLY A 225 PRO A 233 -1 O GLY A 225 N ALA A 221
SHEET 3 AA5 4 LEU A 182 ALA A 187 -1 N VAL A 186 O LEU A 230
SHEET 4 AA5 4 ILE A 270 THR A 272 -1 O VAL A 271 N PHE A 185
SHEET 1 AA6 2 ARG A 194 ALA A 196 0
SHEET 2 AA6 2 CYS A 199 PRO A 202 -1 O LEU A 201 N VAL A 195
SHEET 1 AA7 6 MSE A 277 LYS A 278 0
SHEET 2 AA7 6 THR A 333 ASP A 337 1 O THR A 333 N MSE A 277
SHEET 3 AA7 6 SER A 380 VAL A 384 1 O ILE A 382 N ILE A 336
SHEET 4 AA7 6 ILE A 236 VAL A 240 1 N THR A 237 O THR A 381
SHEET 5 AA7 6 ASN A 397 MSE A 401 1 O ILE A 399 N LEU A 238
SHEET 6 AA7 6 ALA A 406 ASP A 408 -1 O LEU A 407 N GLN A 400
SHEET 1 AA8 2 VAL A 287 LEU A 290 0
SHEET 2 AA8 2 PHE A 308 THR A 310 -1 O PHE A 308 N LEU A 290
SHEET 1 AA9 3 TRP A 501 ASN A 502 0
SHEET 2 AA9 3 ALA A 439 HIS A 441 -1 N LEU A 440 O ASN A 502
SHEET 3 AA9 3 PHE A 547 ARG A 548 -1 O ARG A 548 N ALA A 439
SHEET 1 AB1 3 VAL A 456 LYS A 459 0
SHEET 2 AB1 3 SER A 463 PHE A 466 -1 O ARG A 465 N SER A 457
SHEET 3 AB1 3 GLU A 469 ASP A 472 -1 O GLU A 469 N PHE A 466
LINK C ALA A 0 N AMSE A 1 1555 1555 1.33
LINK C ALA A 0 N BMSE A 1 1555 1555 1.33
LINK C AMSE A 1 N ASP A 2 1555 1555 1.33
LINK C BMSE A 1 N ASP A 2 1555 1555 1.33
LINK C PRO A 202 N MSE A 203 1555 1555 1.33
LINK C MSE A 203 N LYS A 204 1555 1555 1.33
LINK C ALA A 276 N MSE A 277 1555 1555 1.33
LINK C MSE A 277 N LYS A 278 1555 1555 1.33
LINK C PRO A 300 N MSE A 301 1555 1555 1.33
LINK C MSE A 301 N GLY A 302 1555 1555 1.33
LINK C PHE A 345 N AMSE A 346 1555 1555 1.33
LINK C PHE A 345 N BMSE A 346 1555 1555 1.33
LINK C AMSE A 346 N ILE A 347 1555 1555 1.33
LINK C BMSE A 346 N ILE A 347 1555 1555 1.33
LINK C ARG A 351 N MSE A 352 1555 1555 1.33
LINK C MSE A 352 N GLN A 353 1555 1555 1.33
LINK C VAL A 384 N MSE A 385 1555 1555 1.33
LINK C MSE A 385 N GLY A 386 1555 1555 1.33
LINK C GLN A 400 N MSE A 401 1555 1555 1.33
LINK C MSE A 401 N HIS A 402 1555 1555 1.33
LINK C LEU A 445 N MSE A 446 1555 1555 1.33
LINK C MSE A 446 N ASN A 447 1555 1555 1.33
LINK C ASN A 520 N MSE A 521 1555 1555 1.33
LINK C MSE A 521 N PRO A 522 1555 1555 1.35
LINK C VAL A 535 N MSE A 536 1555 1555 1.33
LINK C MSE A 536 N ALA A 537 1555 1555 1.33
LINK C ARG A 541 N MSE A 542 1555 1555 1.33
LINK C MSE A 542 N ARG A 543 1555 1555 1.33
LINK NA NA A 601 O3G ANP A 602 1555 1555 2.44
LINK NA NA A 601 O2B ANP A 602 1555 1555 2.46
LINK OG SER A 314 NA NA A 601 1555 6555 2.43
LINK OG SER A 316 NA NA A 601 1555 6555 3.00
SITE 1 AC1 4 SER A 314 SER A 316 ASP A 339 ANP A 602
SITE 1 AC2 20 PRO A 193 MSE A 203 ALA A 206 VAL A 207
SITE 2 AC2 20 GLY A 243 PHE A 244 HIS A 245 GLY A 246
SITE 3 AC2 20 LYS A 247 SER A 248 THR A 249 ASP A 312
SITE 4 AC2 20 SER A 314 GLY A 315 ASP A 337 ASP A 339
SITE 5 AC2 20 VAL A 384 TYR A 404 NA A 601 HOH A 709
CRYST1 104.957 104.957 85.354 90.00 90.00 120.00 P 31 2 1 6
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 0.009528 0.005501 0.000000 0.00000
SCALE2 0.000000 0.011002 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011716 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
