HEADER PROTEIN BINDING 22-JUN-10 3NMN
TITLE CRYSTAL STRUCTURE OF PYRABACTIN-BOUND ABSCISIC ACID RECEPTOR PYL1 IN
TITLE 2 COMPLEX WITH TYPE 2C PROTEIN PHOSPHATASE ABI1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ABSCISIC ACID RECEPTOR PYL1;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: PYR1-LIKE PROTEIN 1, ABI1-BINDING PROTEIN 6, REGULATORY
COMPND 5 COMPONENTS OF ABA RECEPTOR 9;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROTEIN PHOSPHATASE 2C 56;
COMPND 9 CHAIN: B, D;
COMPND 10 SYNONYM: ATPP2C56, PROTEIN PHOSPHATASE 2C ABI1, PP2C ABI1, PROTEIN
COMPND 11 ABSCISIC ACID-INSENSITIVE 1;
COMPND 12 EC: 3.1.3.16;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: PYL1, RCAR12, AT5G46790, MZA15.21;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 13 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;
SOURCE 14 ORGANISM_TAXID: 3702;
SOURCE 15 GENE: ABI1, AT4G26080, F20B18.190;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET24A
KEYWDS PYL1, PYRABACTIN, PLANT HORMONE RECEPTOR, ABSCISIC ACID SIGNALING,
KEYWDS 2 PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR X.E.ZHOU,K.MELCHER,L.-M.NG,F.-F.SOON,Y.XU,K.M.SUINO-POWELL,A.KOVACH,
AUTHOR 2 J.LI,E.-L.YONG,H.E.XU
REVDAT 3 06-SEP-23 3NMN 1 REMARK SEQADV LINK
REVDAT 2 15-SEP-10 3NMN 1 JRNL
REVDAT 1 25-AUG-10 3NMN 0
JRNL AUTH K.MELCHER,Y.XU,L.M.NG,X.E.ZHOU,F.F.SOON,V.CHINNUSAMY,
JRNL AUTH 2 K.M.SUINO-POWELL,A.KOVACH,F.S.THAM,S.R.CUTLER,J.LI,E.L.YONG,
JRNL AUTH 3 J.K.ZHU,H.E.XU
JRNL TITL IDENTIFICATION AND MECHANISM OF ABA RECEPTOR ANTAGONISM.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 17 1102 2010
JRNL REFN ISSN 1545-9993
JRNL PMID 20729862
JRNL DOI 10.1038/NSMB.1887
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 46283
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.200
REMARK 3 FREE R VALUE TEST SET COUNT : 3617
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3118
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.35
REMARK 3 BIN R VALUE (WORKING SET) : 0.3110
REMARK 3 BIN FREE R VALUE SET COUNT : 280
REMARK 3 BIN FREE R VALUE : 0.3470
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6956
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 180
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.28000
REMARK 3 B22 (A**2) : 0.11000
REMARK 3 B33 (A**2) : -0.57000
REMARK 3 B12 (A**2) : -1.47000
REMARK 3 B13 (A**2) : -2.38000
REMARK 3 B23 (A**2) : 1.22000
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): 0.217
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.171
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.115
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7134 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4926 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9649 ; 1.552 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11921 ; 0.909 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 875 ; 4.677 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 332 ;37.280 ;23.253
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1228 ;15.062 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 68 ;20.253 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1076 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7905 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1487 ; 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): 4405 ; 1.869 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1782 ; 0.771 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7114 ; 3.306 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2729 ; 3.638 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2535 ; 5.425 ; 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): 12060 ; 2.702 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 184 ;14.877 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 11926 ; 5.583 ; 5.000
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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3NMN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000060018.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
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-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46283
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : 13.40
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 49.1000
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3KDJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULPHATE, 0.1M BISTRIS,
REMARK 280 22% PEG 3350, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: 1880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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: 1810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 GLY A 34
REMARK 465 LYS A 158
REMARK 465 GLU A 159
REMARK 465 GLU A 160
REMARK 465 GLU A 161
REMARK 465 GLU A 162
REMARK 465 GLU A 163
REMARK 465 ARG A 164
REMARK 465 ARG A 210
REMARK 465 ASN A 211
REMARK 465 GLY B 116
REMARK 465 SER B 117
REMARK 465 ARG B 118
REMARK 465 SER B 119
REMARK 465 LEU B 120
REMARK 465 PHE B 121
REMARK 465 GLU B 122
REMARK 465 PHE B 123
REMARK 465 LYS B 124
REMARK 465 SER B 125
REMARK 465 SER B 155
REMARK 465 SER B 156
REMARK 465 GLY B 157
REMARK 465 SER B 158
REMARK 465 MET B 159
REMARK 465 LEU B 160
REMARK 465 ASP B 161
REMARK 465 GLY B 162
REMARK 465 ARG B 163
REMARK 465 PHE B 164
REMARK 465 CYS B 208
REMARK 465 LYS B 372
REMARK 465 ASN B 373
REMARK 465 ALA B 374
REMARK 465 VAL B 375
REMARK 465 ALA B 376
REMARK 465 GLY B 377
REMARK 465 ASP B 378
REMARK 465 ALA B 379
REMARK 465 SER B 380
REMARK 465 LEU B 381
REMARK 465 LEU B 382
REMARK 465 ALA B 383
REMARK 465 ASP B 384
REMARK 465 GLU B 385
REMARK 465 ARG B 386
REMARK 465 ARG B 387
REMARK 465 LYS B 388
REMARK 465 ARG B 425
REMARK 465 ARG B 426
REMARK 465 LYS B 427
REMARK 465 LEU B 428
REMARK 465 LYS B 429
REMARK 465 SER B 430
REMARK 465 LYS B 431
REMARK 465 PRO B 432
REMARK 465 LEU B 433
REMARK 465 ASN B 434
REMARK 465 GLY C 34
REMARK 465 LYS C 158
REMARK 465 GLU C 159
REMARK 465 GLU C 160
REMARK 465 GLU C 161
REMARK 465 GLU C 162
REMARK 465 GLU C 163
REMARK 465 GLY D 116
REMARK 465 SER D 117
REMARK 465 ARG D 118
REMARK 465 SER D 119
REMARK 465 LEU D 120
REMARK 465 PHE D 121
REMARK 465 GLU D 122
REMARK 465 PHE D 123
REMARK 465 LYS D 124
REMARK 465 SER D 155
REMARK 465 SER D 156
REMARK 465 GLY D 157
REMARK 465 SER D 158
REMARK 465 MET D 159
REMARK 465 LEU D 160
REMARK 465 ASP D 161
REMARK 465 GLY D 162
REMARK 465 ARG D 163
REMARK 465 PHE D 164
REMARK 465 VAL D 375
REMARK 465 ALA D 376
REMARK 465 GLY D 377
REMARK 465 ASP D 378
REMARK 465 ALA D 379
REMARK 465 SER D 380
REMARK 465 LEU D 381
REMARK 465 LEU D 382
REMARK 465 ALA D 383
REMARK 465 ASP D 384
REMARK 465 GLU D 385
REMARK 465 ARG D 386
REMARK 465 ARG D 387
REMARK 465 LYS D 388
REMARK 465 ARG D 425
REMARK 465 ARG D 426
REMARK 465 LYS D 427
REMARK 465 LEU D 428
REMARK 465 LYS D 429
REMARK 465 SER D 430
REMARK 465 LYS D 431
REMARK 465 PRO D 432
REMARK 465 LEU D 433
REMARK 465 ASN D 434
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 ND2 ASN C 54 O GLU D 389 1455 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 104 CB CYS A 104 SG -0.149
REMARK 500 CYS B 259 CB CYS B 259 SG -0.157
REMARK 500 CYS D 259 CB CYS D 259 SG -0.136
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 ASN A 54 -165.07 53.70
REMARK 500 MET A 100 74.56 -117.67
REMARK 500 HIS A 142 -176.52 -177.76
REMARK 500 LEU A 144 68.08 -115.28
REMARK 500 ARG B 137 42.51 -98.57
REMARK 500 ARG B 150 50.80 33.15
REMARK 500 GLN B 153 -72.52 -28.74
REMARK 500 PRO B 166 17.59 -62.50
REMARK 500 GLN B 167 -30.18 -145.35
REMARK 500 LYS B 204 79.23 48.52
REMARK 500 ARG B 268 75.47 -105.10
REMARK 500 TRP B 300 77.31 -152.33
REMARK 500 LEU C 52 -82.26 -89.96
REMARK 500 ASN C 54 -147.87 -125.12
REMARK 500 PHE C 88 -1.47 72.08
REMARK 500 ASP C 97 33.22 -95.68
REMARK 500 LEU C 126 97.11 -160.66
REMARK 500 ASN C 209 48.29 -79.72
REMARK 500 LEU D 152 42.37 -88.63
REMARK 500 ARG D 191 -33.08 -131.86
REMARK 500 LYS D 204 65.42 61.35
REMARK 500 TRP D 300 81.61 -159.62
REMARK 500 VAL D 308 -63.78 -91.96
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 MG B 998 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 55 O
REMARK 620 2 ASP B 177 OD2 133.4
REMARK 620 3 ASP B 347 OD1 89.4 75.3
REMARK 620 4 ASP B 413 OD1 91.9 134.2 118.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 999 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 177 OD2
REMARK 620 2 ASP B 261 OD1 113.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 998 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 177 OD2
REMARK 620 2 ASP D 261 OD1 114.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 999 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 177 OD2
REMARK 620 2 ASP D 347 OD2 107.3
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYV A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYV C 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 999
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KAY RELATED DB: PDB
REMARK 900 APO PYL1 CRYSTAL STRUCTURE
REMARK 900 RELATED ID: 3NMH RELATED DB: PDB
REMARK 900 PYRABACTIN BOUND PYL2
REMARK 900 RELATED ID: 3NMP RELATED DB: PDB
REMARK 900 RELATED ID: 3NMT RELATED DB: PDB
REMARK 900 RELATED ID: 3NMV RELATED DB: PDB
DBREF 3NMN A 36 211 UNP Q8VZS8 PYL1_ARATH 36 211
DBREF 3NMN B 117 434 UNP P49597 P2C56_ARATH 117 434
DBREF 3NMN C 36 211 UNP Q8VZS8 PYL1_ARATH 36 211
DBREF 3NMN D 117 434 UNP P49597 P2C56_ARATH 117 434
SEQADV 3NMN GLY A 34 UNP Q8VZS8 EXPRESSION TAG
SEQADV 3NMN SER A 35 UNP Q8VZS8 EXPRESSION TAG
SEQADV 3NMN GLY B 116 UNP P49597 EXPRESSION TAG
SEQADV 3NMN GLY C 34 UNP Q8VZS8 EXPRESSION TAG
SEQADV 3NMN SER C 35 UNP Q8VZS8 EXPRESSION TAG
SEQADV 3NMN GLY D 116 UNP P49597 EXPRESSION TAG
SEQRES 1 A 178 GLY SER GLU PHE THR GLN LEU SER GLN SER ILE ALA GLU
SEQRES 2 A 178 PHE HIS THR TYR GLN LEU GLY ASN GLY ARG CYS SER SER
SEQRES 3 A 178 LEU LEU ALA GLN ARG ILE HIS ALA PRO PRO GLU THR VAL
SEQRES 4 A 178 TRP SER VAL VAL ARG ARG PHE ASP ARG PRO GLN ILE TYR
SEQRES 5 A 178 LYS HIS PHE ILE LYS SER CYS ASN VAL SER GLU ASP PHE
SEQRES 6 A 178 GLU MET ARG VAL GLY CYS THR ARG ASP VAL ASN VAL ILE
SEQRES 7 A 178 SER GLY LEU PRO ALA ASN THR SER ARG GLU ARG LEU ASP
SEQRES 8 A 178 LEU LEU ASP ASP ASP ARG ARG VAL THR GLY PHE SER ILE
SEQRES 9 A 178 THR GLY GLY GLU HIS ARG LEU ARG ASN TYR LYS SER VAL
SEQRES 10 A 178 THR THR VAL HIS ARG PHE GLU LYS GLU GLU GLU GLU GLU
SEQRES 11 A 178 ARG ILE TRP THR VAL VAL LEU GLU SER TYR VAL VAL ASP
SEQRES 12 A 178 VAL PRO GLU GLY ASN SER GLU GLU ASP THR ARG LEU PHE
SEQRES 13 A 178 ALA ASP THR VAL ILE ARG LEU ASN LEU GLN LYS LEU ALA
SEQRES 14 A 178 SER ILE THR GLU ALA MET ASN ARG ASN
SEQRES 1 B 319 GLY SER ARG SER LEU PHE GLU PHE LYS SER VAL PRO LEU
SEQRES 2 B 319 TYR GLY PHE THR SER ILE CYS GLY ARG ARG PRO GLU MET
SEQRES 3 B 319 GLU ASP ALA VAL SER THR ILE PRO ARG PHE LEU GLN SER
SEQRES 4 B 319 SER SER GLY SER MET LEU ASP GLY ARG PHE ASP PRO GLN
SEQRES 5 B 319 SER ALA ALA HIS PHE PHE GLY VAL TYR ASP GLY HIS GLY
SEQRES 6 B 319 GLY SER GLN VAL ALA ASN TYR CYS ARG GLU ARG MET HIS
SEQRES 7 B 319 LEU ALA LEU ALA GLU GLU ILE ALA LYS GLU LYS PRO MET
SEQRES 8 B 319 LEU CYS ASP GLY ASP THR TRP LEU GLU LYS TRP LYS LYS
SEQRES 9 B 319 ALA LEU PHE ASN SER PHE LEU ARG VAL ASP SER GLU ILE
SEQRES 10 B 319 GLU SER VAL ALA PRO GLU THR VAL GLY SER THR SER VAL
SEQRES 11 B 319 VAL ALA VAL VAL PHE PRO SER HIS ILE PHE VAL ALA ASN
SEQRES 12 B 319 CYS GLY ASP SER ARG ALA VAL LEU CYS ARG GLY LYS THR
SEQRES 13 B 319 ALA LEU PRO LEU SER VAL ASP HIS LYS PRO ASP ARG GLU
SEQRES 14 B 319 ASP GLU ALA ALA ARG ILE GLU ALA ALA GLY GLY LYS VAL
SEQRES 15 B 319 ILE GLN TRP ASN GLY ALA ARG VAL PHE GLY VAL LEU ALA
SEQRES 16 B 319 MET SER ARG SER ILE GLY ASP ARG TYR LEU LYS PRO SER
SEQRES 17 B 319 ILE ILE PRO ASP PRO GLU VAL THR ALA VAL LYS ARG VAL
SEQRES 18 B 319 LYS GLU ASP ASP CYS LEU ILE LEU ALA SER ASP GLY VAL
SEQRES 19 B 319 TRP ASP VAL MET THR ASP GLU GLU ALA CYS GLU MET ALA
SEQRES 20 B 319 ARG LYS ARG ILE LEU LEU TRP HIS LYS LYS ASN ALA VAL
SEQRES 21 B 319 ALA GLY ASP ALA SER LEU LEU ALA ASP GLU ARG ARG LYS
SEQRES 22 B 319 GLU GLY LYS ASP PRO ALA ALA MET SER ALA ALA GLU TYR
SEQRES 23 B 319 LEU SER LYS LEU ALA ILE GLN ARG GLY SER LYS ASP ASN
SEQRES 24 B 319 ILE SER VAL VAL VAL VAL ASP LEU LYS PRO ARG ARG LYS
SEQRES 25 B 319 LEU LYS SER LYS PRO LEU ASN
SEQRES 1 C 178 GLY SER GLU PHE THR GLN LEU SER GLN SER ILE ALA GLU
SEQRES 2 C 178 PHE HIS THR TYR GLN LEU GLY ASN GLY ARG CYS SER SER
SEQRES 3 C 178 LEU LEU ALA GLN ARG ILE HIS ALA PRO PRO GLU THR VAL
SEQRES 4 C 178 TRP SER VAL VAL ARG ARG PHE ASP ARG PRO GLN ILE TYR
SEQRES 5 C 178 LYS HIS PHE ILE LYS SER CYS ASN VAL SER GLU ASP PHE
SEQRES 6 C 178 GLU MET ARG VAL GLY CYS THR ARG ASP VAL ASN VAL ILE
SEQRES 7 C 178 SER GLY LEU PRO ALA ASN THR SER ARG GLU ARG LEU ASP
SEQRES 8 C 178 LEU LEU ASP ASP ASP ARG ARG VAL THR GLY PHE SER ILE
SEQRES 9 C 178 THR GLY GLY GLU HIS ARG LEU ARG ASN TYR LYS SER VAL
SEQRES 10 C 178 THR THR VAL HIS ARG PHE GLU LYS GLU GLU GLU GLU GLU
SEQRES 11 C 178 ARG ILE TRP THR VAL VAL LEU GLU SER TYR VAL VAL ASP
SEQRES 12 C 178 VAL PRO GLU GLY ASN SER GLU GLU ASP THR ARG LEU PHE
SEQRES 13 C 178 ALA ASP THR VAL ILE ARG LEU ASN LEU GLN LYS LEU ALA
SEQRES 14 C 178 SER ILE THR GLU ALA MET ASN ARG ASN
SEQRES 1 D 319 GLY SER ARG SER LEU PHE GLU PHE LYS SER VAL PRO LEU
SEQRES 2 D 319 TYR GLY PHE THR SER ILE CYS GLY ARG ARG PRO GLU MET
SEQRES 3 D 319 GLU ASP ALA VAL SER THR ILE PRO ARG PHE LEU GLN SER
SEQRES 4 D 319 SER SER GLY SER MET LEU ASP GLY ARG PHE ASP PRO GLN
SEQRES 5 D 319 SER ALA ALA HIS PHE PHE GLY VAL TYR ASP GLY HIS GLY
SEQRES 6 D 319 GLY SER GLN VAL ALA ASN TYR CYS ARG GLU ARG MET HIS
SEQRES 7 D 319 LEU ALA LEU ALA GLU GLU ILE ALA LYS GLU LYS PRO MET
SEQRES 8 D 319 LEU CYS ASP GLY ASP THR TRP LEU GLU LYS TRP LYS LYS
SEQRES 9 D 319 ALA LEU PHE ASN SER PHE LEU ARG VAL ASP SER GLU ILE
SEQRES 10 D 319 GLU SER VAL ALA PRO GLU THR VAL GLY SER THR SER VAL
SEQRES 11 D 319 VAL ALA VAL VAL PHE PRO SER HIS ILE PHE VAL ALA ASN
SEQRES 12 D 319 CYS GLY ASP SER ARG ALA VAL LEU CYS ARG GLY LYS THR
SEQRES 13 D 319 ALA LEU PRO LEU SER VAL ASP HIS LYS PRO ASP ARG GLU
SEQRES 14 D 319 ASP GLU ALA ALA ARG ILE GLU ALA ALA GLY GLY LYS VAL
SEQRES 15 D 319 ILE GLN TRP ASN GLY ALA ARG VAL PHE GLY VAL LEU ALA
SEQRES 16 D 319 MET SER ARG SER ILE GLY ASP ARG TYR LEU LYS PRO SER
SEQRES 17 D 319 ILE ILE PRO ASP PRO GLU VAL THR ALA VAL LYS ARG VAL
SEQRES 18 D 319 LYS GLU ASP ASP CYS LEU ILE LEU ALA SER ASP GLY VAL
SEQRES 19 D 319 TRP ASP VAL MET THR ASP GLU GLU ALA CYS GLU MET ALA
SEQRES 20 D 319 ARG LYS ARG ILE LEU LEU TRP HIS LYS LYS ASN ALA VAL
SEQRES 21 D 319 ALA GLY ASP ALA SER LEU LEU ALA ASP GLU ARG ARG LYS
SEQRES 22 D 319 GLU GLY LYS ASP PRO ALA ALA MET SER ALA ALA GLU TYR
SEQRES 23 D 319 LEU SER LYS LEU ALA ILE GLN ARG GLY SER LYS ASP ASN
SEQRES 24 D 319 ILE SER VAL VAL VAL VAL ASP LEU LYS PRO ARG ARG LYS
SEQRES 25 D 319 LEU LYS SER LYS PRO LEU ASN
HET PYV A 900 22
HET MG B 998 1
HET MG B 999 1
HET PYV C 900 22
HET MG D 998 1
HET MG D 999 1
HETNAM PYV 4-BROMO-N-(PYRIDIN-2-YLMETHYL)NAPHTHALENE-1-SULFONAMIDE
HETNAM MG MAGNESIUM ION
HETSYN PYV PYRABACTIN
FORMUL 5 PYV 2(C16 H13 BR N2 O2 S)
FORMUL 6 MG 4(MG 2+)
FORMUL 11 HOH *180(H2 O)
HELIX 1 1 SER A 35 HIS A 48 1 14
HELIX 2 2 PRO A 68 ARG A 77 1 10
HELIX 3 3 ARG A 81 TYR A 85 5 5
HELIX 4 4 SER A 182 ASN A 209 1 28
HELIX 5 5 SER B 182 LYS B 204 1 23
HELIX 6 6 GLY B 210 SER B 234 1 25
HELIX 7 7 ARG B 283 GLY B 294 1 12
HELIX 8 8 ARG B 318 LYS B 321 5 4
HELIX 9 9 SER B 346 ASP B 351 1 6
HELIX 10 10 THR B 354 HIS B 370 1 17
HELIX 11 11 ASP B 392 ARG B 409 1 18
HELIX 12 12 GLU C 36 PHE C 47 1 12
HELIX 13 13 PRO C 68 ARG C 77 1 10
HELIX 14 14 ARG C 81 TYR C 85 5 5
HELIX 15 15 SER C 182 ASN C 209 1 28
HELIX 16 16 ARG D 150 SER D 154 5 5
HELIX 17 17 SER D 182 LYS D 202 1 21
HELIX 18 18 MET D 206 ASP D 209 5 4
HELIX 19 19 GLY D 210 GLU D 233 1 24
HELIX 20 20 ARG D 283 GLY D 294 1 12
HELIX 21 21 ARG D 318 LYS D 321 5 4
HELIX 22 22 SER D 346 ASP D 351 1 6
HELIX 23 23 THR D 354 HIS D 370 1 17
HELIX 24 24 ASP D 392 ARG D 409 1 18
SHEET 1 A 7 ARG A 56 ILE A 65 0
SHEET 2 A 7 TRP A 166 ASP A 176 -1 O VAL A 175 N CYS A 57
SHEET 3 A 7 LYS A 148 PHE A 156 -1 N LYS A 148 O VAL A 174
SHEET 4 A 7 VAL A 132 GLY A 139 -1 N THR A 133 O THR A 151
SHEET 5 A 7 THR A 118 ASP A 127 -1 N ASP A 127 O VAL A 132
SHEET 6 A 7 THR A 105 VAL A 110 -1 N VAL A 108 O SER A 119
SHEET 7 A 7 ILE A 89 ASN A 93 -1 N ASN A 93 O ASP A 107
SHEET 1 B 5 LEU B 128 ILE B 134 0
SHEET 2 B 5 ILE B 415 ASP B 421 -1 O ASP B 421 N LEU B 128
SHEET 3 B 5 ASP B 339 ALA B 345 -1 N LEU B 342 O VAL B 420
SHEET 4 B 5 ARG B 263 ARG B 268 -1 N VAL B 265 O ILE B 343
SHEET 5 B 5 ALA B 272 PRO B 274 -1 O LEU B 273 N LEU B 266
SHEET 1 C 4 ASP B 143 ILE B 148 0
SHEET 2 C 4 HIS B 171 HIS B 179 -1 O PHE B 172 N ILE B 148
SHEET 3 C 4 GLY B 241 SER B 242 -1 O GLY B 241 N HIS B 179
SHEET 4 C 4 ILE B 315 GLY B 316 -1 O ILE B 315 N SER B 242
SHEET 1 D 5 ASP B 143 ILE B 148 0
SHEET 2 D 5 HIS B 171 HIS B 179 -1 O PHE B 172 N ILE B 148
SHEET 3 D 5 SER B 244 VAL B 249 -1 O ALA B 247 N PHE B 173
SHEET 4 D 5 HIS B 253 CYS B 259 -1 O PHE B 255 N VAL B 248
SHEET 5 D 5 GLU B 329 LYS B 334 -1 O VAL B 333 N ILE B 254
SHEET 1 E 2 VAL B 297 GLN B 299 0
SHEET 2 E 2 ALA B 303 VAL B 305 -1 O ARG B 304 N ILE B 298
SHEET 1 F 7 ARG C 56 ILE C 65 0
SHEET 2 F 7 TRP C 166 ASP C 176 -1 O GLU C 171 N LEU C 61
SHEET 3 F 7 LYS C 148 PHE C 156 -1 N LYS C 148 O VAL C 174
SHEET 4 F 7 VAL C 132 GLY C 139 -1 N THR C 133 O THR C 151
SHEET 5 F 7 THR C 118 ASP C 127 -1 N ARG C 120 O THR C 138
SHEET 6 F 7 THR C 105 VAL C 110 -1 N VAL C 108 O SER C 119
SHEET 7 F 7 ILE C 89 ASN C 93 -1 N ASN C 93 O ASP C 107
SHEET 1 G 5 TYR D 129 ILE D 134 0
SHEET 2 G 5 ILE D 415 ASP D 421 -1 O VAL D 417 N THR D 132
SHEET 3 G 5 ASP D 339 ALA D 345 -1 N LEU D 344 O VAL D 418
SHEET 4 G 5 ARG D 263 ARG D 268 -1 N VAL D 265 O ILE D 343
SHEET 5 G 5 THR D 271 PRO D 274 -1 O LEU D 273 N LEU D 266
SHEET 1 H 4 ASP D 143 ILE D 148 0
SHEET 2 H 4 HIS D 171 HIS D 179 -1 O PHE D 172 N ILE D 148
SHEET 3 H 4 GLY D 241 VAL D 249 -1 O ALA D 247 N PHE D 173
SHEET 4 H 4 ILE D 315 GLY D 316 -1 O ILE D 315 N SER D 242
SHEET 1 I 5 ASP D 143 ILE D 148 0
SHEET 2 I 5 HIS D 171 HIS D 179 -1 O PHE D 172 N ILE D 148
SHEET 3 I 5 GLY D 241 VAL D 249 -1 O ALA D 247 N PHE D 173
SHEET 4 I 5 HIS D 253 CYS D 259 -1 O ALA D 257 N VAL D 246
SHEET 5 I 5 GLU D 329 LYS D 334 -1 O THR D 331 N VAL D 256
SHEET 1 J 2 VAL D 297 GLN D 299 0
SHEET 2 J 2 ALA D 303 VAL D 305 -1 O ARG D 304 N ILE D 298
SSBOND 1 CYS D 267 CYS D 359 1555 1555 2.11
LINK O HOH B 55 MG MG B 998 1555 1555 2.70
LINK OD2 ASP B 177 MG MG B 998 1555 1555 2.36
LINK OD2 ASP B 177 MG MG B 999 1555 1555 2.62
LINK OD1 ASP B 261 MG MG B 999 1555 1555 2.69
LINK OD1 ASP B 347 MG MG B 998 1555 1555 2.51
LINK OD1 ASP B 413 MG MG B 998 1555 1555 3.00
LINK OD2 ASP D 177 MG MG D 998 1555 1555 2.58
LINK OD2 ASP D 177 MG MG D 999 1555 1555 2.58
LINK OD1 ASP D 261 MG MG D 998 1555 1555 2.48
LINK OD2 ASP D 347 MG MG D 999 1555 1555 2.44
CISPEP 1 LYS B 321 PRO B 322 0 -2.93
CISPEP 2 LYS D 321 PRO D 322 0 -3.98
SITE 1 AC1 10 VAL A 108 ALA A 116 SER A 119 GLU A 121
SITE 2 AC1 10 HIS A 142 LEU A 144 TYR A 147 PHE A 189
SITE 3 AC1 10 VAL A 193 HOH A 219
SITE 1 AC2 4 HOH B 55 ASP B 177 ASP B 347 ASP B 413
SITE 1 AC3 4 ASP B 177 ASP B 261 SER B 262 ASP B 347
SITE 1 AC4 12 HOH C 7 ILE C 89 VAL C 108 LEU C 114
SITE 2 AC4 12 ALA C 116 SER C 119 GLU C 121 LEU C 144
SITE 3 AC4 12 TYR C 147 PHE C 189 VAL C 193 HOH C 214
SITE 1 AC5 6 HOH D 57 ASP D 177 ASP D 261 SER D 262
SITE 2 AC5 6 SER D 346 ASP D 347
SITE 1 AC6 5 ASP D 177 SER D 346 ASP D 347 GLY D 348
SITE 2 AC6 5 ASN D 414
CRYST1 59.978 66.710 72.598 115.78 95.43 105.60 P 1 2
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 0.016673 0.004655 0.004355 0.00000
SCALE2 0.000000 0.015564 0.008519 0.00000
SCALE3 0.000000 0.000000 0.015774 0.00000
(ATOM LINES ARE NOT SHOWN.)
END