HEADER LIGASE 15-JUN-15 5C1O
TITLE CRYSTAL STRUCTURE OF AMP-PNP COMPLEXED D-ALANINE-D-ALANINE LIGASE(DDL)
TITLE 2 FROM YERSINIA PESTIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: D-ALA-D-ALA LIGASE,D-ALANYLALANINE SYNTHETASE;
COMPND 5 EC: 6.3.2.4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: YERSINIA PESTIS;
SOURCE 3 ORGANISM_TAXID: 632;
SOURCE 4 GENE: DDL, DDLB, YPO0557, Y3624, YP_3627;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS D-ALANINE-D-ALANINE LIGASE, DDL, DRUG TARGET, BACTERIAL CELL WALL
KEYWDS 2 SYNTHESIS, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.T.TRAN,L.W.KANG,M.K.HONG
REVDAT 2 20-MAR-24 5C1O 1 REMARK LINK
REVDAT 1 02-MAR-16 5C1O 0
JRNL AUTH H.T.TRAN,M.K.HONG,H.P.NGO,K.H.HUYNH,Y.J.AHN,Z.WANG,L.W.KANG
JRNL TITL STRUCTURE OF D-ALANINE-D-ALANINE LIGASE FROM YERSINIA
JRNL TITL 2 PESTIS: NUCLEOTIDE PHOSPHATE RECOGNITION BY THE SERINE LOOP.
JRNL REF ACTA CRYSTALLOGR D STRUCT V. 72 12 2016
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 26894530
JRNL DOI 10.1107/S2059798315021671
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 47927
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2567
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3352
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.67
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE SET COUNT : 187
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9041
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 133
REMARK 3 SOLVENT ATOMS : 36
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -0.01000
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): 0.436
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.271
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.189
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.322
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9389 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8940 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12704 ; 1.731 ; 1.998
REMARK 3 BOND ANGLES OTHERS (DEGREES): 20613 ; 0.833 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1178 ; 6.682 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 377 ;37.961 ;25.013
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1559 ;17.279 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;21.085 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1452 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10471 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1985 ; 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): 4742 ; 4.152 ; 5.189
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4741 ; 4.149 ; 5.189
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5910 ; 6.151 ; 7.765
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5911 ; 6.151 ; 7.766
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4647 ; 5.049 ; 5.919
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4648 ; 5.049 ; 5.919
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6795 ; 7.548 ; 8.625
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 10030 ; 9.784 ;41.733
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 10031 ; 9.783 ;41.734
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5C1O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1000210606.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-MAR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 5C (4A)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.997
REMARK 200 MONOCHROMATOR : DCM SI (111) CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50546
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 35.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM ACETATE, BIS-TRIS PH7.0,
REMARK 280 PEG 8000 29%, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 287K
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 31.51450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 106.00600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.39750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 106.00600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.51450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.39750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLU A 148
REMARK 465 GLY A 149
REMARK 465 SER A 150
REMARK 465 SER A 151
REMARK 465 ASP A 213
REMARK 465 ALA A 214
REMARK 465 LYS A 215
REMARK 465 TYR A 216
REMARK 465 LEU A 217
REMARK 465 GLY B 149
REMARK 465 SER B 150
REMARK 465 GLY B 207
REMARK 465 VAL B 208
REMARK 465 PHE B 209
REMARK 465 TYR B 210
REMARK 465 ASP B 211
REMARK 465 TYR B 212
REMARK 465 ASP B 213
REMARK 465 ALA B 214
REMARK 465 LYS B 215
REMARK 465 TYR B 216
REMARK 465 LEU B 217
REMARK 465 SER B 218
REMARK 465 ASP B 219
REMARK 465 LYS B 220
REMARK 465 GLY D 149
REMARK 465 SER D 150
REMARK 465 TYR D 210
REMARK 465 ASP D 211
REMARK 465 TYR D 212
REMARK 465 ASP D 213
REMARK 465 ALA D 214
REMARK 465 LYS D 215
REMARK 465 TYR D 216
REMARK 465 LEU D 217
REMARK 465 SER D 218
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLU C 196 OH TYR C 290 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 300 NE - CZ - NH2 ANGL. DEV. = -3.8 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 GLN A 120 -98.53 -58.61
REMARK 500 GLN A 121 -30.56 -25.02
REMARK 500 LEU A 163 -70.69 -56.70
REMARK 500 HIS A 173 31.99 -149.83
REMARK 500 ASP A 219 -12.09 -10.04
REMARK 500 THR A 221 130.73 -31.31
REMARK 500 VAL B 47 -30.70 129.18
REMARK 500 ASP B 249 35.66 71.56
REMARK 500 ARG C 16 -57.62 -22.71
REMARK 500 GLU C 148 104.00 -56.90
REMARK 500 SER C 151 19.65 3.75
REMARK 500 ASP C 174 164.87 175.86
REMARK 500 LEU D 304 22.69 -75.48
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 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 68 O
REMARK 620 2 SER A 91 O 81.2
REMARK 620 3 THR A 94 OG1 155.6 76.1
REMARK 620 4 THR A 273 OG1 93.2 117.7 89.7
REMARK 620 5 HOH A 504 O 117.7 157.0 86.5 76.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 270 OE1
REMARK 620 2 ANP A 401 O1G 150.7
REMARK 620 3 ANP A 401 O2G 143.2 65.6
REMARK 620 4 ANP A 401 O1B 95.8 107.4 62.0
REMARK 620 5 ANP A 401 O1A 76.8 89.3 123.0 80.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 68 O
REMARK 620 2 SER B 91 O 81.6
REMARK 620 3 THR B 94 OG1 158.6 78.7
REMARK 620 4 THR B 273 OG1 86.1 118.9 96.0
REMARK 620 5 HOH B 505 O 111.0 160.9 90.2 77.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 148 OE1
REMARK 620 2 GLU B 148 OE2 58.1
REMARK 620 3 GLU B 270 OE1 73.8 88.6
REMARK 620 4 GLU B 270 OE2 132.1 110.5 58.9
REMARK 620 5 ANP B 401 O2G 136.1 106.1 150.1 91.3
REMARK 620 6 ANP B 401 O2B 65.6 99.4 124.8 150.1 79.2
REMARK 620 7 ANP B 401 O2A 111.8 169.5 91.1 78.2 79.0 72.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 68 O
REMARK 620 2 SER C 91 O 80.8
REMARK 620 3 THR C 94 OG1 160.0 79.8
REMARK 620 4 THR C 273 OG1 88.5 124.3 98.3
REMARK 620 5 HOH C 507 O 106.1 162.4 93.9 72.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 148 OE2
REMARK 620 2 GLU C 270 OE1 69.9
REMARK 620 3 GLU C 270 OE2 100.1 59.1
REMARK 620 4 ANP C 401 O2G 113.3 175.5 122.2
REMARK 620 5 ANP C 401 O2B 92.3 104.0 152.8 73.0
REMARK 620 6 ANP C 401 O2A 149.9 92.9 90.9 82.9 67.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 68 O
REMARK 620 2 SER D 91 O 78.3
REMARK 620 3 THR D 94 OG1 149.9 72.2
REMARK 620 4 THR D 273 OG1 87.1 117.0 101.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 148 OE1
REMARK 620 2 GLU D 270 OE1 112.3
REMARK 620 3 GLU D 270 OE2 104.6 60.8
REMARK 620 4 ANP D 401 O1G 108.9 105.9 146.4
REMARK 620 5 ANP D 401 O1B 86.7 158.3 105.5 75.7
REMARK 620 6 ANP D 401 O1A 155.7 90.5 78.8 70.2 69.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5C1P RELATED DB: PDB
DBREF 5C1O A 1 306 UNP Q8ZIE7 DDL_YERPE 1 306
DBREF 5C1O B 1 306 UNP Q8ZIE7 DDL_YERPE 1 306
DBREF 5C1O C 1 306 UNP Q8ZIE7 DDL_YERPE 1 306
DBREF 5C1O D 1 306 UNP Q8ZIE7 DDL_YERPE 1 306
SEQRES 1 A 306 MET ALA GLU LYS VAL ALA VAL LEU LEU GLY GLY THR SER
SEQRES 2 A 306 ALA GLU ARG GLU VAL SER LEU LEU SER GLY GLN ALA VAL
SEQRES 3 A 306 LEU ALA GLY LEU LYS GLU ALA GLY ILE ASP ALA TYR GLY
SEQRES 4 A 306 VAL ASP THR LYS ASP PHE PRO VAL THR GLN LEU LYS GLU
SEQRES 5 A 306 GLN GLY PHE ASP LYS VAL PHE ILE ALA LEU HIS GLY ARG
SEQRES 6 A 306 GLY GLY GLU ASP GLY THR LEU GLN GLY VAL LEU GLU PHE
SEQRES 7 A 306 LEU GLN LEU PRO TYR THR GLY SER GLY VAL MET ALA SER
SEQRES 8 A 306 ALA LEU THR MET ASP LYS LEU ARG THR LYS LEU VAL TRP
SEQRES 9 A 306 GLN ALA LEU GLY LEU PRO ILE SER PRO TYR VAL ALA LEU
SEQRES 10 A 306 ASN ARG GLN GLN PHE GLU THR LEU SER PRO GLU GLU LEU
SEQRES 11 A 306 VAL ALA CYS VAL ALA LYS LEU GLY LEU PRO LEU ILE VAL
SEQRES 12 A 306 LYS PRO SER HIS GLU GLY SER SER VAL GLY MET SER LYS
SEQRES 13 A 306 VAL ASP HIS ALA SER GLU LEU GLN LYS ALA LEU VAL GLU
SEQRES 14 A 306 ALA PHE GLN HIS ASP SER ASP VAL LEU ILE GLU LYS TRP
SEQRES 15 A 306 LEU SER GLY PRO GLU PHE THR VAL ALA ILE LEU GLY ASP
SEQRES 16 A 306 GLU VAL LEU PRO SER ILE ARG ILE GLN PRO PRO GLY VAL
SEQRES 17 A 306 PHE TYR ASP TYR ASP ALA LYS TYR LEU SER ASP LYS THR
SEQRES 18 A 306 GLN TYR PHE CYS PRO SER GLY LEU SER ASP GLU SER GLU
SEQRES 19 A 306 GLN GLN LEU ALA ALA LEU ALA LEU GLN ALA TYR HIS ALA
SEQRES 20 A 306 LEU ASP CYS SER GLY TRP GLY ARG VAL ASP VAL MET GLN
SEQRES 21 A 306 ASP ARG ASP GLY HIS PHE TYR LEU LEU GLU VAL ASN THR
SEQRES 22 A 306 SER PRO GLY MET THR SER HIS SER LEU VAL PRO MET ALA
SEQRES 23 A 306 ALA ARG GLN TYR GLY LEU SER PHE SER GLN LEU VAL ALA
SEQRES 24 A 306 ARG ILE LEU MET LEU ALA ASP
SEQRES 1 B 306 MET ALA GLU LYS VAL ALA VAL LEU LEU GLY GLY THR SER
SEQRES 2 B 306 ALA GLU ARG GLU VAL SER LEU LEU SER GLY GLN ALA VAL
SEQRES 3 B 306 LEU ALA GLY LEU LYS GLU ALA GLY ILE ASP ALA TYR GLY
SEQRES 4 B 306 VAL ASP THR LYS ASP PHE PRO VAL THR GLN LEU LYS GLU
SEQRES 5 B 306 GLN GLY PHE ASP LYS VAL PHE ILE ALA LEU HIS GLY ARG
SEQRES 6 B 306 GLY GLY GLU ASP GLY THR LEU GLN GLY VAL LEU GLU PHE
SEQRES 7 B 306 LEU GLN LEU PRO TYR THR GLY SER GLY VAL MET ALA SER
SEQRES 8 B 306 ALA LEU THR MET ASP LYS LEU ARG THR LYS LEU VAL TRP
SEQRES 9 B 306 GLN ALA LEU GLY LEU PRO ILE SER PRO TYR VAL ALA LEU
SEQRES 10 B 306 ASN ARG GLN GLN PHE GLU THR LEU SER PRO GLU GLU LEU
SEQRES 11 B 306 VAL ALA CYS VAL ALA LYS LEU GLY LEU PRO LEU ILE VAL
SEQRES 12 B 306 LYS PRO SER HIS GLU GLY SER SER VAL GLY MET SER LYS
SEQRES 13 B 306 VAL ASP HIS ALA SER GLU LEU GLN LYS ALA LEU VAL GLU
SEQRES 14 B 306 ALA PHE GLN HIS ASP SER ASP VAL LEU ILE GLU LYS TRP
SEQRES 15 B 306 LEU SER GLY PRO GLU PHE THR VAL ALA ILE LEU GLY ASP
SEQRES 16 B 306 GLU VAL LEU PRO SER ILE ARG ILE GLN PRO PRO GLY VAL
SEQRES 17 B 306 PHE TYR ASP TYR ASP ALA LYS TYR LEU SER ASP LYS THR
SEQRES 18 B 306 GLN TYR PHE CYS PRO SER GLY LEU SER ASP GLU SER GLU
SEQRES 19 B 306 GLN GLN LEU ALA ALA LEU ALA LEU GLN ALA TYR HIS ALA
SEQRES 20 B 306 LEU ASP CYS SER GLY TRP GLY ARG VAL ASP VAL MET GLN
SEQRES 21 B 306 ASP ARG ASP GLY HIS PHE TYR LEU LEU GLU VAL ASN THR
SEQRES 22 B 306 SER PRO GLY MET THR SER HIS SER LEU VAL PRO MET ALA
SEQRES 23 B 306 ALA ARG GLN TYR GLY LEU SER PHE SER GLN LEU VAL ALA
SEQRES 24 B 306 ARG ILE LEU MET LEU ALA ASP
SEQRES 1 C 306 MET ALA GLU LYS VAL ALA VAL LEU LEU GLY GLY THR SER
SEQRES 2 C 306 ALA GLU ARG GLU VAL SER LEU LEU SER GLY GLN ALA VAL
SEQRES 3 C 306 LEU ALA GLY LEU LYS GLU ALA GLY ILE ASP ALA TYR GLY
SEQRES 4 C 306 VAL ASP THR LYS ASP PHE PRO VAL THR GLN LEU LYS GLU
SEQRES 5 C 306 GLN GLY PHE ASP LYS VAL PHE ILE ALA LEU HIS GLY ARG
SEQRES 6 C 306 GLY GLY GLU ASP GLY THR LEU GLN GLY VAL LEU GLU PHE
SEQRES 7 C 306 LEU GLN LEU PRO TYR THR GLY SER GLY VAL MET ALA SER
SEQRES 8 C 306 ALA LEU THR MET ASP LYS LEU ARG THR LYS LEU VAL TRP
SEQRES 9 C 306 GLN ALA LEU GLY LEU PRO ILE SER PRO TYR VAL ALA LEU
SEQRES 10 C 306 ASN ARG GLN GLN PHE GLU THR LEU SER PRO GLU GLU LEU
SEQRES 11 C 306 VAL ALA CYS VAL ALA LYS LEU GLY LEU PRO LEU ILE VAL
SEQRES 12 C 306 LYS PRO SER HIS GLU GLY SER SER VAL GLY MET SER LYS
SEQRES 13 C 306 VAL ASP HIS ALA SER GLU LEU GLN LYS ALA LEU VAL GLU
SEQRES 14 C 306 ALA PHE GLN HIS ASP SER ASP VAL LEU ILE GLU LYS TRP
SEQRES 15 C 306 LEU SER GLY PRO GLU PHE THR VAL ALA ILE LEU GLY ASP
SEQRES 16 C 306 GLU VAL LEU PRO SER ILE ARG ILE GLN PRO PRO GLY VAL
SEQRES 17 C 306 PHE TYR ASP TYR ASP ALA LYS TYR LEU SER ASP LYS THR
SEQRES 18 C 306 GLN TYR PHE CYS PRO SER GLY LEU SER ASP GLU SER GLU
SEQRES 19 C 306 GLN GLN LEU ALA ALA LEU ALA LEU GLN ALA TYR HIS ALA
SEQRES 20 C 306 LEU ASP CYS SER GLY TRP GLY ARG VAL ASP VAL MET GLN
SEQRES 21 C 306 ASP ARG ASP GLY HIS PHE TYR LEU LEU GLU VAL ASN THR
SEQRES 22 C 306 SER PRO GLY MET THR SER HIS SER LEU VAL PRO MET ALA
SEQRES 23 C 306 ALA ARG GLN TYR GLY LEU SER PHE SER GLN LEU VAL ALA
SEQRES 24 C 306 ARG ILE LEU MET LEU ALA ASP
SEQRES 1 D 306 MET ALA GLU LYS VAL ALA VAL LEU LEU GLY GLY THR SER
SEQRES 2 D 306 ALA GLU ARG GLU VAL SER LEU LEU SER GLY GLN ALA VAL
SEQRES 3 D 306 LEU ALA GLY LEU LYS GLU ALA GLY ILE ASP ALA TYR GLY
SEQRES 4 D 306 VAL ASP THR LYS ASP PHE PRO VAL THR GLN LEU LYS GLU
SEQRES 5 D 306 GLN GLY PHE ASP LYS VAL PHE ILE ALA LEU HIS GLY ARG
SEQRES 6 D 306 GLY GLY GLU ASP GLY THR LEU GLN GLY VAL LEU GLU PHE
SEQRES 7 D 306 LEU GLN LEU PRO TYR THR GLY SER GLY VAL MET ALA SER
SEQRES 8 D 306 ALA LEU THR MET ASP LYS LEU ARG THR LYS LEU VAL TRP
SEQRES 9 D 306 GLN ALA LEU GLY LEU PRO ILE SER PRO TYR VAL ALA LEU
SEQRES 10 D 306 ASN ARG GLN GLN PHE GLU THR LEU SER PRO GLU GLU LEU
SEQRES 11 D 306 VAL ALA CYS VAL ALA LYS LEU GLY LEU PRO LEU ILE VAL
SEQRES 12 D 306 LYS PRO SER HIS GLU GLY SER SER VAL GLY MET SER LYS
SEQRES 13 D 306 VAL ASP HIS ALA SER GLU LEU GLN LYS ALA LEU VAL GLU
SEQRES 14 D 306 ALA PHE GLN HIS ASP SER ASP VAL LEU ILE GLU LYS TRP
SEQRES 15 D 306 LEU SER GLY PRO GLU PHE THR VAL ALA ILE LEU GLY ASP
SEQRES 16 D 306 GLU VAL LEU PRO SER ILE ARG ILE GLN PRO PRO GLY VAL
SEQRES 17 D 306 PHE TYR ASP TYR ASP ALA LYS TYR LEU SER ASP LYS THR
SEQRES 18 D 306 GLN TYR PHE CYS PRO SER GLY LEU SER ASP GLU SER GLU
SEQRES 19 D 306 GLN GLN LEU ALA ALA LEU ALA LEU GLN ALA TYR HIS ALA
SEQRES 20 D 306 LEU ASP CYS SER GLY TRP GLY ARG VAL ASP VAL MET GLN
SEQRES 21 D 306 ASP ARG ASP GLY HIS PHE TYR LEU LEU GLU VAL ASN THR
SEQRES 22 D 306 SER PRO GLY MET THR SER HIS SER LEU VAL PRO MET ALA
SEQRES 23 D 306 ALA ARG GLN TYR GLY LEU SER PHE SER GLN LEU VAL ALA
SEQRES 24 D 306 ARG ILE LEU MET LEU ALA ASP
HET ANP A 401 31
HET NA A 402 1
HET MG A 403 1
HET ANP B 401 31
HET NA B 402 1
HET MG B 403 1
HET NA B 404 1
HET ANP C 401 31
HET NA C 402 1
HET MG C 403 1
HET ANP D 401 31
HET NA D 402 1
HET MG D 403 1
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM NA SODIUM ION
HETNAM MG MAGNESIUM ION
FORMUL 5 ANP 4(C10 H17 N6 O12 P3)
FORMUL 6 NA 5(NA 1+)
FORMUL 7 MG 4(MG 2+)
FORMUL 18 HOH *36(H2 O)
HELIX 1 AA1 GLU A 15 ALA A 33 1 19
HELIX 2 AA2 PRO A 46 LEU A 50 5 5
HELIX 3 AA3 GLY A 70 GLN A 80 1 11
HELIX 4 AA4 GLY A 87 THR A 94 1 8
HELIX 5 AA5 ASP A 96 LEU A 107 1 12
HELIX 6 AA6 ARG A 119 THR A 124 1 6
HELIX 7 AA7 SER A 126 LYS A 136 1 11
HELIX 8 AA8 HIS A 159 PHE A 171 1 13
HELIX 9 AA9 SER A 230 LEU A 248 1 19
HELIX 10 AB1 SER A 281 TYR A 290 1 10
HELIX 11 AB2 SER A 293 LEU A 304 1 12
HELIX 12 AB3 GLU B 15 ALA B 33 1 19
HELIX 13 AB4 GLY B 70 GLN B 80 1 11
HELIX 14 AB5 GLY B 87 THR B 94 1 8
HELIX 15 AB6 ASP B 96 LEU B 107 1 12
HELIX 16 AB7 ARG B 119 LEU B 125 1 7
HELIX 17 AB8 SER B 126 VAL B 134 1 9
HELIX 18 AB9 ALA B 135 GLY B 138 5 4
HELIX 19 AC1 HIS B 159 SER B 161 5 3
HELIX 20 AC2 GLU B 162 GLN B 172 1 11
HELIX 21 AC3 SER B 230 LEU B 248 1 19
HELIX 22 AC4 SER B 281 GLY B 291 1 11
HELIX 23 AC5 SER B 293 LEU B 304 1 12
HELIX 24 AC6 GLU C 15 ALA C 33 1 19
HELIX 25 AC7 PRO C 46 LEU C 50 5 5
HELIX 26 AC8 GLY C 70 GLN C 80 1 11
HELIX 27 AC9 GLY C 87 THR C 94 1 8
HELIX 28 AD1 ASP C 96 GLY C 108 1 13
HELIX 29 AD2 ARG C 119 LEU C 125 1 7
HELIX 30 AD3 SER C 126 ALA C 135 1 10
HELIX 31 AD4 LYS C 136 GLY C 138 5 3
HELIX 32 AD5 HIS C 159 SER C 161 5 3
HELIX 33 AD6 GLU C 162 HIS C 173 1 12
HELIX 34 AD7 ASP C 211 LEU C 217 1 7
HELIX 35 AD8 SER C 230 LEU C 248 1 19
HELIX 36 AD9 SER C 281 GLY C 291 1 11
HELIX 37 AE1 SER C 293 LEU C 304 1 12
HELIX 38 AE2 GLU D 15 ALA D 33 1 19
HELIX 39 AE3 PRO D 46 LEU D 50 5 5
HELIX 40 AE4 GLY D 70 GLN D 80 1 11
HELIX 41 AE5 GLY D 87 THR D 94 1 8
HELIX 42 AE6 ASP D 96 LEU D 107 1 12
HELIX 43 AE7 ARG D 119 LEU D 125 1 7
HELIX 44 AE8 SER D 126 VAL D 134 1 9
HELIX 45 AE9 ALA D 135 GLY D 138 5 4
HELIX 46 AF1 HIS D 159 SER D 161 5 3
HELIX 47 AF2 GLU D 162 PHE D 171 1 10
HELIX 48 AF3 SER D 230 LEU D 248 1 19
HELIX 49 AF4 SER D 281 GLY D 291 1 11
HELIX 50 AF5 SER D 293 LEU D 304 1 12
SHEET 1 AA1 3 ASP A 36 ASP A 41 0
SHEET 2 AA1 3 LYS A 4 LEU A 9 1 N VAL A 7 O TYR A 38
SHEET 3 AA1 3 LYS A 57 ILE A 60 1 O PHE A 59 N ALA A 6
SHEET 1 AA2 4 TYR A 114 ASN A 118 0
SHEET 2 AA2 4 ASP A 176 LYS A 181 -1 O VAL A 177 N LEU A 117
SHEET 3 AA2 4 LEU A 141 PRO A 145 -1 N LYS A 144 O LEU A 178
SHEET 4 AA2 4 SER A 155 VAL A 157 -1 O VAL A 157 N LEU A 141
SHEET 1 AA3 4 GLU A 196 VAL A 197 0
SHEET 2 AA3 4 GLU A 187 LEU A 193 -1 N LEU A 193 O GLU A 196
SHEET 3 AA3 4 ILE A 201 GLN A 204 -1 O ILE A 203 N GLU A 187
SHEET 4 AA3 4 GLN A 222 PHE A 224 -1 O GLN A 222 N GLN A 204
SHEET 1 AA4 4 GLU A 196 VAL A 197 0
SHEET 2 AA4 4 GLU A 187 LEU A 193 -1 N LEU A 193 O GLU A 196
SHEET 3 AA4 4 TRP A 253 GLN A 260 -1 O VAL A 258 N PHE A 188
SHEET 4 AA4 4 PHE A 266 ASN A 272 -1 O ASN A 272 N ARG A 255
SHEET 1 AA5 3 ASP B 36 ASP B 41 0
SHEET 2 AA5 3 LYS B 4 LEU B 9 1 N VAL B 5 O TYR B 38
SHEET 3 AA5 3 LYS B 57 ILE B 60 1 O PHE B 59 N ALA B 6
SHEET 1 AA6 4 TYR B 114 ASN B 118 0
SHEET 2 AA6 4 ASP B 176 LYS B 181 -1 O ILE B 179 N VAL B 115
SHEET 3 AA6 4 LEU B 141 PRO B 145 -1 N ILE B 142 O GLU B 180
SHEET 4 AA6 4 SER B 155 VAL B 157 -1 O SER B 155 N VAL B 143
SHEET 1 AA7 4 GLU B 196 VAL B 197 0
SHEET 2 AA7 4 GLU B 187 LEU B 193 -1 N LEU B 193 O GLU B 196
SHEET 3 AA7 4 ILE B 201 GLN B 204 -1 O ILE B 203 N GLU B 187
SHEET 4 AA7 4 GLN B 222 PHE B 224 -1 O PHE B 224 N ARG B 202
SHEET 1 AA8 4 GLU B 196 VAL B 197 0
SHEET 2 AA8 4 GLU B 187 LEU B 193 -1 N LEU B 193 O GLU B 196
SHEET 3 AA8 4 TRP B 253 GLN B 260 -1 O VAL B 258 N PHE B 188
SHEET 4 AA8 4 PHE B 266 ASN B 272 -1 O LEU B 269 N ASP B 257
SHEET 1 AA9 3 ALA C 37 ASP C 41 0
SHEET 2 AA9 3 VAL C 5 LEU C 9 1 N VAL C 7 O TYR C 38
SHEET 3 AA9 3 LYS C 57 ILE C 60 1 O PHE C 59 N ALA C 6
SHEET 1 AB1 4 TYR C 114 ASN C 118 0
SHEET 2 AB1 4 ASP C 176 LYS C 181 -1 O VAL C 177 N LEU C 117
SHEET 3 AB1 4 LEU C 141 PRO C 145 -1 N ILE C 142 O GLU C 180
SHEET 4 AB1 4 SER C 155 VAL C 157 -1 O VAL C 157 N LEU C 141
SHEET 1 AB2 4 GLU C 196 VAL C 197 0
SHEET 2 AB2 4 GLU C 187 LEU C 193 -1 N LEU C 193 O GLU C 196
SHEET 3 AB2 4 ILE C 201 GLN C 204 -1 O ILE C 201 N THR C 189
SHEET 4 AB2 4 GLN C 222 PHE C 224 -1 O PHE C 224 N ARG C 202
SHEET 1 AB3 4 GLU C 196 VAL C 197 0
SHEET 2 AB3 4 GLU C 187 LEU C 193 -1 N LEU C 193 O GLU C 196
SHEET 3 AB3 4 TRP C 253 GLN C 260 -1 O VAL C 256 N VAL C 190
SHEET 4 AB3 4 PHE C 266 ASN C 272 -1 O GLU C 270 N ASP C 257
SHEET 1 AB4 3 ALA D 37 ASP D 41 0
SHEET 2 AB4 3 VAL D 5 LEU D 9 1 N VAL D 7 O VAL D 40
SHEET 3 AB4 3 LYS D 57 ILE D 60 1 O PHE D 59 N ALA D 6
SHEET 1 AB5 4 TYR D 114 ASN D 118 0
SHEET 2 AB5 4 ASP D 176 LYS D 181 -1 O ILE D 179 N VAL D 115
SHEET 3 AB5 4 LEU D 141 PRO D 145 -1 N LYS D 144 O LEU D 178
SHEET 4 AB5 4 SER D 155 VAL D 157 -1 O VAL D 157 N LEU D 141
SHEET 1 AB6 4 GLU D 196 VAL D 197 0
SHEET 2 AB6 4 GLU D 187 LEU D 193 -1 N LEU D 193 O GLU D 196
SHEET 3 AB6 4 ILE D 201 GLN D 204 -1 O ILE D 203 N GLU D 187
SHEET 4 AB6 4 GLN D 222 PHE D 224 -1 O GLN D 222 N GLN D 204
SHEET 1 AB7 4 GLU D 196 VAL D 197 0
SHEET 2 AB7 4 GLU D 187 LEU D 193 -1 N LEU D 193 O GLU D 196
SHEET 3 AB7 4 TRP D 253 GLN D 260 -1 O VAL D 258 N PHE D 188
SHEET 4 AB7 4 PHE D 266 ASN D 272 -1 O ASN D 272 N ARG D 255
LINK O GLU A 68 NA NA A 402 1555 1555 2.25
LINK O SER A 91 NA NA A 402 1555 1555 2.27
LINK OG1 THR A 94 NA NA A 402 1555 1555 2.30
LINK OE1 GLU A 270 MG MG A 403 1555 1555 2.25
LINK OG1 THR A 273 NA NA A 402 1555 1555 2.24
LINK O1G ANP A 401 MG MG A 403 1555 1555 2.22
LINK O2G ANP A 401 MG MG A 403 1555 1555 2.21
LINK O1B ANP A 401 MG MG A 403 1555 1555 2.19
LINK O1A ANP A 401 MG MG A 403 1555 1555 2.19
LINK NA NA A 402 O HOH A 504 1555 1555 2.28
LINK O GLU B 68 NA NA B 402 1555 1555 2.28
LINK O SER B 91 NA NA B 402 1555 1555 2.32
LINK OG1 THR B 94 NA NA B 402 1555 1555 2.27
LINK OE1 GLU B 148 MG MG B 403 1555 1555 2.21
LINK OE2 GLU B 148 MG MG B 403 1555 1555 2.21
LINK OE1 GLU B 270 MG MG B 403 1555 1555 2.19
LINK OE2 GLU B 270 MG MG B 403 1555 1555 2.22
LINK OG1 THR B 273 NA NA B 402 1555 1555 2.24
LINK O2G ANP B 401 MG MG B 403 1555 1555 2.19
LINK O2B ANP B 401 MG MG B 403 1555 1555 2.20
LINK O2A ANP B 401 MG MG B 403 1555 1555 2.22
LINK NA NA B 402 O HOH B 505 1555 1555 2.29
LINK O GLU C 68 NA NA C 402 1555 1555 2.26
LINK O SER C 91 NA NA C 402 1555 1555 2.31
LINK OG1 THR C 94 NA NA C 402 1555 1555 2.26
LINK OE2 GLU C 148 MG MG C 403 1555 1555 2.16
LINK OE1 GLU C 270 MG MG C 403 1555 1555 2.21
LINK OE2 GLU C 270 MG MG C 403 1555 1555 2.21
LINK OG1 THR C 273 NA NA C 402 1555 1555 2.26
LINK O2G ANP C 401 MG MG C 403 1555 1555 1.81
LINK O2B ANP C 401 MG MG C 403 1555 1555 2.21
LINK O2A ANP C 401 MG MG C 403 1555 1555 2.17
LINK NA NA C 402 O HOH C 507 1555 1555 2.28
LINK O GLU D 68 NA NA D 402 1555 1555 2.24
LINK O SER D 91 NA NA D 402 1555 1555 2.32
LINK OG1 THR D 94 NA NA D 402 1555 1555 2.27
LINK OE1 GLU D 148 MG MG D 403 1555 1555 2.20
LINK OE1 GLU D 270 MG MG D 403 1555 1555 2.19
LINK OE2 GLU D 270 MG MG D 403 1555 1555 2.15
LINK OG1 THR D 273 NA NA D 402 1555 1555 2.28
LINK O1G ANP D 401 MG MG D 403 1555 1555 2.16
LINK O1B ANP D 401 MG MG D 403 1555 1555 2.17
LINK O1A ANP D 401 MG MG D 403 1555 1555 2.20
CISPEP 1 LEU A 139 PRO A 140 0 -7.01
CISPEP 2 GLY A 185 PRO A 186 0 1.39
CISPEP 3 CYS A 225 PRO A 226 0 -2.50
CISPEP 4 LEU B 139 PRO B 140 0 -8.26
CISPEP 5 GLY B 185 PRO B 186 0 -6.95
CISPEP 6 CYS B 225 PRO B 226 0 3.76
CISPEP 7 LEU C 139 PRO C 140 0 2.40
CISPEP 8 GLY C 185 PRO C 186 0 7.54
CISPEP 9 CYS C 225 PRO C 226 0 7.80
CISPEP 10 LEU D 139 PRO D 140 0 -7.59
CISPEP 11 GLY D 185 PRO D 186 0 1.60
CISPEP 12 CYS D 225 PRO D 226 0 5.69
SITE 1 AC1 15 LYS A 97 ILE A 142 LYS A 144 MET A 154
SITE 2 AC1 15 GLU A 180 LYS A 181 TRP A 182 LEU A 183
SITE 3 AC1 15 GLU A 187 TYR A 210 TYR A 212 MET A 259
SITE 4 AC1 15 LEU A 269 GLU A 270 MG A 403
SITE 1 AC2 6 GLU A 68 SER A 91 THR A 94 MET A 95
SITE 2 AC2 6 THR A 273 HOH A 504
SITE 1 AC3 2 GLU A 270 ANP A 401
SITE 1 AC4 12 LYS B 97 LYS B 144 GLU B 148 SER B 151
SITE 2 AC4 12 MET B 154 GLU B 180 LYS B 181 LEU B 183
SITE 3 AC4 12 GLU B 187 MET B 259 GLU B 270 MG B 403
SITE 1 AC5 6 GLU B 68 SER B 91 THR B 94 MET B 95
SITE 2 AC5 6 THR B 273 HOH B 505
SITE 1 AC6 4 LYS B 97 GLU B 148 GLU B 270 ANP B 401
SITE 1 AC7 2 HIS B 265 HIS C 280
SITE 1 AC8 17 LYS C 97 ILE C 142 LYS C 144 GLU C 148
SITE 2 AC8 17 SER C 151 MET C 154 GLU C 180 LYS C 181
SITE 3 AC8 17 TRP C 182 LEU C 183 GLU C 187 PHE C 209
SITE 4 AC8 17 TYR C 210 LYS C 215 MET C 259 GLU C 270
SITE 5 AC8 17 MG C 403
SITE 1 AC9 6 GLU C 68 SER C 91 THR C 94 MET C 95
SITE 2 AC9 6 THR C 273 HOH C 507
SITE 1 AD1 3 GLU C 148 GLU C 270 ANP C 401
SITE 1 AD2 15 LYS D 97 ILE D 142 LYS D 144 GLU D 148
SITE 2 AD2 15 SER D 151 MET D 154 GLU D 180 LYS D 181
SITE 3 AD2 15 TRP D 182 LEU D 183 GLU D 187 PHE D 209
SITE 4 AD2 15 MET D 259 GLU D 270 MG D 403
SITE 1 AD3 5 GLU D 68 SER D 91 THR D 94 MET D 95
SITE 2 AD3 5 THR D 273
SITE 1 AD4 3 GLU D 148 GLU D 270 ANP D 401
CRYST1 63.029 106.795 212.012 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 0.015866 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009364 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004717 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
