HEADER HYDROLASE/HYDROLASE INHIBITOR 18-AUG-08 3E7A
TITLE CRYSTAL STRUCTURE OF PROTEIN PHOSPHATASE-1 BOUND TO THE NATURAL TOXIN
TITLE 2 NODULARIN-R
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-ALPHA CATALYTIC
COMPND 3 SUBUNIT;
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: RESIDUES 7-300;
COMPND 6 SYNONYM: PP-1A;
COMPND 7 EC: 3.1.3.16;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: NODULARIN R;
COMPND 11 CHAIN: C, D;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PPP1CA, PPP1A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: IN HOUSE DERIVED;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: NODULARIA SPUMIGENA;
SOURCE 14 ORGANISM_TAXID: 70799
KEYWDS CARBOHYDRATE METABOLISM, CELL CYCLE, CELL DIVISION, GLYCOGEN
KEYWDS 2 METABOLISM, HYDROLASE, IRON, MANGANESE, METAL-BINDING,
KEYWDS 3 PHOSPHOPROTEIN, PROTEIN PHOSPHATASE, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 4 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.S.KELKER,R.PAGE,W.PETI
REVDAT 5 25-OCT-17 3E7A 1 REMARK
REVDAT 4 10-APR-13 3E7A 1 REMARK
REVDAT 3 13-JUL-11 3E7A 1 VERSN
REVDAT 2 13-JAN-09 3E7A 1 JRNL VERSN
REVDAT 1 04-NOV-08 3E7A 0
JRNL AUTH M.S.KELKER,R.PAGE,W.PETI
JRNL TITL CRYSTAL STRUCTURES OF PROTEIN PHOSPHATASE-1 BOUND TO
JRNL TITL 2 NODULARIN-R AND TAUTOMYCIN: A NOVEL SCAFFOLD FOR
JRNL TITL 3 STRUCTURE-BASED DRUG DESIGN OF SERINE/THREONINE PHOSPHATASE
JRNL TITL 4 INHIBITORS
JRNL REF J.MOL.BIOL. V. 385 11 2009
JRNL REFN ISSN 0022-2836
JRNL PMID 18992256
JRNL DOI 10.1016/J.JMB.2008.10.053
REMARK 2
REMARK 2 RESOLUTION. 1.63 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 79699
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) : 0.144
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.169
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4185
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) : 1.63
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5611
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.74
REMARK 3 BIN R VALUE (WORKING SET) : 0.2120
REMARK 3 BIN FREE R VALUE SET COUNT : 286
REMARK 3 BIN FREE R VALUE : 0.2590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4753
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 682
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.38000
REMARK 3 B22 (A**2) : 0.15000
REMARK 3 B33 (A**2) : 0.23000
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): 0.075
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.075
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.046
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.373
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5080 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3486 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6926 ; 1.374 ; 1.997
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8498 ; 0.930 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 647 ; 6.607 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 240 ;32.809 ;23.833
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 850 ;10.805 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;16.732 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 757 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5756 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1105 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1067 ; 0.219 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3896 ; 0.203 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2526 ; 0.181 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2603 ; 0.083 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 494 ; 0.163 ; 0.200
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): 13 ; 0.183 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 41 ; 0.228 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 45 ; 0.195 ; 0.200
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): 3033 ; 1.230 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1221 ; 0.318 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4883 ; 1.954 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2229 ; 3.066 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2010 ; 4.418 ;11.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
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 7 A 21
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7446 -25.5462 -6.6025
REMARK 3 T TENSOR
REMARK 3 T11: -0.0698 T22: 0.0167
REMARK 3 T33: 0.0016 T12: 0.0009
REMARK 3 T13: -0.0051 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 1.1623 L22: 3.7081
REMARK 3 L33: 1.4901 L12: -0.3390
REMARK 3 L13: 1.1157 L23: -0.4632
REMARK 3 S TENSOR
REMARK 3 S11: -0.0070 S12: 0.0562 S13: -0.0241
REMARK 3 S21: -0.0529 S22: -0.0047 S23: 0.0667
REMARK 3 S31: 0.0296 S32: -0.2119 S33: 0.0116
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 22 A 40
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7655 -25.7022 -7.5893
REMARK 3 T TENSOR
REMARK 3 T11: -0.0537 T22: -0.0032
REMARK 3 T33: -0.0089 T12: 0.0035
REMARK 3 T13: -0.0146 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 0.2778 L22: 0.1159
REMARK 3 L33: 1.0877 L12: -0.1707
REMARK 3 L13: -0.3737 L23: 0.3099
REMARK 3 S TENSOR
REMARK 3 S11: -0.0218 S12: 0.0929 S13: -0.0556
REMARK 3 S21: -0.0969 S22: 0.0030 S23: 0.0310
REMARK 3 S31: -0.0198 S32: -0.0272 S33: 0.0188
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 41 A 186
REMARK 3 ORIGIN FOR THE GROUP (A): -2.4146 -24.0622 8.0421
REMARK 3 T TENSOR
REMARK 3 T11: -0.0552 T22: -0.0167
REMARK 3 T33: -0.0254 T12: -0.0033
REMARK 3 T13: -0.0065 T23: 0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 0.4826 L22: 0.6520
REMARK 3 L33: 0.6332 L12: -0.0319
REMARK 3 L13: -0.2837 L23: -0.0158
REMARK 3 S TENSOR
REMARK 3 S11: 0.0117 S12: -0.0494 S13: -0.0183
REMARK 3 S21: 0.0816 S22: -0.0123 S23: -0.0082
REMARK 3 S31: -0.0119 S32: 0.0346 S33: 0.0006
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 187 A 200
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9798 -14.4878 16.5892
REMARK 3 T TENSOR
REMARK 3 T11: 0.0054 T22: 0.0368
REMARK 3 T33: 0.0131 T12: -0.0451
REMARK 3 T13: -0.0468 T23: -0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 0.3786 L22: 2.9493
REMARK 3 L33: 1.5031 L12: -0.6727
REMARK 3 L13: -0.0511 L23: -0.4850
REMARK 3 S TENSOR
REMARK 3 S11: 0.0079 S12: -0.0702 S13: 0.2171
REMARK 3 S21: 0.3724 S22: -0.0544 S23: -0.3200
REMARK 3 S31: -0.2034 S32: 0.2191 S33: 0.0465
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 201 A 299
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3289 -32.8039 22.3471
REMARK 3 T TENSOR
REMARK 3 T11: 0.0444 T22: 0.0330
REMARK 3 T33: -0.0192 T12: 0.0106
REMARK 3 T13: -0.0079 T23: 0.0426
REMARK 3 L TENSOR
REMARK 3 L11: 0.6965 L22: 0.9075
REMARK 3 L33: 0.5948 L12: 0.0802
REMARK 3 L13: -0.3130 L23: 0.0638
REMARK 3 S TENSOR
REMARK 3 S11: -0.0581 S12: -0.1894 S13: -0.1170
REMARK 3 S21: 0.2623 S22: -0.0060 S23: -0.0142
REMARK 3 S31: 0.0602 S32: 0.1147 S33: 0.0641
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 : B 7 B 21
REMARK 3 ORIGIN FOR THE GROUP (A): -29.0072 -38.9372 46.0518
REMARK 3 T TENSOR
REMARK 3 T11: -0.0270 T22: -0.0427
REMARK 3 T33: -0.0081 T12: -0.0090
REMARK 3 T13: -0.0005 T23: -0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 3.0008 L22: 2.1452
REMARK 3 L33: 2.8855 L12: 0.2865
REMARK 3 L13: 1.7380 L23: 0.1441
REMARK 3 S TENSOR
REMARK 3 S11: -0.0447 S12: -0.0709 S13: 0.0776
REMARK 3 S21: 0.0700 S22: 0.0138 S23: -0.0734
REMARK 3 S31: -0.2190 S32: 0.1166 S33: 0.0309
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 22 B 49
REMARK 3 ORIGIN FOR THE GROUP (A): -36.3817 -46.0101 41.9984
REMARK 3 T TENSOR
REMARK 3 T11: -0.0492 T22: -0.0418
REMARK 3 T33: -0.0060 T12: -0.0015
REMARK 3 T13: 0.0010 T23: 0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 0.6595 L22: 0.7948
REMARK 3 L33: 1.3836 L12: -0.0310
REMARK 3 L13: 0.3089 L23: -0.0949
REMARK 3 S TENSOR
REMARK 3 S11: -0.0099 S12: -0.0708 S13: 0.0449
REMARK 3 S21: 0.0307 S22: -0.0024 S23: 0.0716
REMARK 3 S31: -0.0334 S32: -0.0613 S33: 0.0122
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 50 B 181
REMARK 3 ORIGIN FOR THE GROUP (A): -32.0100 -47.7932 31.3207
REMARK 3 T TENSOR
REMARK 3 T11: -0.0357 T22: -0.0504
REMARK 3 T33: -0.0210 T12: -0.0056
REMARK 3 T13: -0.0050 T23: 0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 0.5058 L22: 0.6830
REMARK 3 L33: 0.6491 L12: 0.1183
REMARK 3 L13: -0.0683 L23: 0.0287
REMARK 3 S TENSOR
REMARK 3 S11: -0.0247 S12: 0.0257 S13: 0.0124
REMARK 3 S21: -0.0905 S22: 0.0209 S23: 0.0347
REMARK 3 S31: -0.0078 S32: -0.0126 S33: 0.0038
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 182 B 198
REMARK 3 ORIGIN FOR THE GROUP (A): -45.7654 -52.0833 20.0553
REMARK 3 T TENSOR
REMARK 3 T11: 0.0027 T22: 0.0410
REMARK 3 T33: 0.0369 T12: -0.0297
REMARK 3 T13: -0.0643 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.4438 L22: 1.0190
REMARK 3 L33: 1.9216 L12: -0.5127
REMARK 3 L13: -0.5708 L23: -0.0523
REMARK 3 S TENSOR
REMARK 3 S11: -0.0564 S12: 0.1929 S13: -0.0774
REMARK 3 S21: -0.2131 S22: -0.0094 S23: 0.2202
REMARK 3 S31: 0.0234 S32: -0.3722 S33: 0.0657
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 199 B 299
REMARK 3 ORIGIN FOR THE GROUP (A): -25.7101 -50.6155 16.1721
REMARK 3 T TENSOR
REMARK 3 T11: 0.0466 T22: 0.0041
REMARK 3 T33: -0.0230 T12: -0.0231
REMARK 3 T13: 0.0199 T23: 0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 0.7956 L22: 0.7897
REMARK 3 L33: 0.5866 L12: 0.1230
REMARK 3 L13: -0.1001 L23: -0.0226
REMARK 3 S TENSOR
REMARK 3 S11: -0.0811 S12: 0.1721 S13: -0.0427
REMARK 3 S21: -0.2599 S22: 0.0468 S23: -0.0641
REMARK 3 S31: 0.0221 S32: 0.0264 S33: 0.0343
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 3E7A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-AUG-08.
REMARK 100 THE DEPOSITION ID IS D_1000048964.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : MONOCHROMATOR: SI(111) CHANNEL
REMARK 200 CUT MONOCHROMATOR.
REMARK 200 OPTICS : OXFORD DANFYSIK TOROIDAL
REMARK 200 FOCUSING MIRROR.
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83444
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.630
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.51000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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 1FJM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350 AND 0.2 M NAI, PH 7.0,
REMARK 280 UNDER PARAFIN OIL, TEMPERATURE 298K, MICROBATCH
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 32.67700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.22200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.63700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.22200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.67700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.63700
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: 3190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: 2930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE NODULARIN-R IS OLIGOPEPTIDE, A MEMBER OF TOXIN CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: NODULARIN-R
REMARK 400 CHAIN: C, D
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 2
REMARK 465 HIS A 3
REMARK 465 MET A 4
REMARK 465 GLY A 5
REMARK 465 SER A 6
REMARK 465 ASP A 300
REMARK 465 GLY B 2
REMARK 465 HIS B 3
REMARK 465 MET B 4
REMARK 465 GLY B 5
REMARK 465 SER B 6
REMARK 465 ASP B 300
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 23 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 26 NZ
REMARK 470 LYS A 41 CD CE NZ
REMARK 470 LYS A 98 NZ
REMARK 470 LYS A 211 CG CD CE NZ
REMARK 470 GLN A 214 CG CD OE1 NE2
REMARK 470 GLU A 218 CG CD OE1 OE2
REMARK 470 GLU A 230 CG CD OE1 OE2
REMARK 470 LYS A 234 CG CD CE NZ
REMARK 470 LYS A 260 CD CE NZ
REMARK 470 GLU A 275 OE1 OE2
REMARK 470 ARG B 23 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 26 NZ
REMARK 470 GLU B 77 CD OE1 OE2
REMARK 470 LYS B 211 CE NZ
REMARK 470 GLN B 214 CG CD OE1 NE2
REMARK 470 GLU B 218 CG CD OE1 OE2
REMARK 470 GLU B 230 CD OE1 OE2
REMARK 470 LYS B 234 CG CD CE NZ
REMARK 470 LYS B 260 CD CE NZ
REMARK 470 GLU B 275 OE1 OE2
REMARK 470 GLU B 287 CG CD OE1 OE2
REMARK 470 ARG D 2 CD NE CZ NH1 NH2
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 O GLN A 214 O HOH A 652 1.90
REMARK 500 O HOH A 689 O HOH A 690 1.96
REMARK 500 O HOH B 464 O HOH B 555 2.03
REMARK 500 ND2 ASN B 271 O PHE B 276 2.15
REMARK 500 OE2 GLU B 32 O HOH B 447 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 O HOH A 473 O HOH B 690 2444 2.06
REMARK 500 OG SER A 129 O HOH A 499 4545 2.17
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 A 43 CB - CA - C ANGL. DEV. = 13.2 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 ARG A 23 60.49 69.39
REMARK 500 ASP A 95 153.18 77.32
REMARK 500 ARG A 96 -49.75 76.58
REMARK 500 TYR A 144 -114.56 -136.61
REMARK 500 GLN A 214 -71.68 -77.38
REMARK 500 SER A 224 -152.30 59.72
REMARK 500 ALA A 247 -132.18 -132.25
REMARK 500 HIS A 248 -27.11 82.94
REMARK 500 ARG B 23 62.91 67.70
REMARK 500 ASP B 95 151.72 79.16
REMARK 500 ARG B 96 -48.70 77.26
REMARK 500 TYR B 144 -111.89 -137.21
REMARK 500 SER B 224 -153.86 65.74
REMARK 500 ALA B 247 -126.32 -133.69
REMARK 500 HIS B 248 -25.19 78.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 22 ARG A 23 41.80
REMARK 500 SER B 22 ARG B 23 35.62
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 MN B 403 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 698 O
REMARK 620 2 ASN B 124 OD1 128.2
REMARK 620 3 HIS B 173 NE2 134.9 95.8
REMARK 620 4 ASP B 92 OD2 79.6 95.6 87.7
REMARK 620 5 HIS B 248 ND1 91.7 97.4 91.7 167.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 403 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 669 O
REMARK 620 2 ASN A 124 OD1 126.3
REMARK 620 3 HIS A 173 NE2 136.0 95.8
REMARK 620 4 HIS A 248 ND1 90.7 100.9 93.3
REMARK 620 5 ASP A 92 OD2 79.2 93.6 86.9 165.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 402 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 64 OD2
REMARK 620 2 HOH A 669 O 105.5
REMARK 620 3 HIS A 66 NE2 106.3 147.4
REMARK 620 4 HOH C 769 O 103.0 93.9 85.8
REMARK 620 5 ASP A 92 OD2 93.5 77.9 93.3 163.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 402 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 64 OD2
REMARK 620 2 HOH B 698 O 102.4
REMARK 620 3 HOH D 724 O 101.6 94.4
REMARK 620 4 HIS B 66 NE2 105.8 151.1 85.8
REMARK 620 5 ASP B 92 OD2 93.8 76.8 163.8 95.4
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF nodularin R
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF nodularin R
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JK7 RELATED DB: PDB
REMARK 900 PP1:OKADAIC ACID CO-CRYSTAL STRUCTURE
REMARK 900 RELATED ID: 1IT6 RELATED DB: PDB
REMARK 900 PP1:CALYCULIN A CO-CRYSTAL STRUCTURE
REMARK 900 RELATED ID: 1FJM RELATED DB: PDB
REMARK 900 PP1 COMPLEXED WITH MICROCYSTIN-LR
REMARK 900 RELATED ID: 2BCD RELATED DB: PDB
REMARK 900 PP1 COMPLEXED WITH NODULARIN-V (MOTUPORIN)
REMARK 900 RELATED ID: 3E7B RELATED DB: PDB
DBREF 3E7A A 7 300 UNP P62136 PP1A_HUMAN 7 300
DBREF 3E7A B 7 300 UNP P62136 PP1A_HUMAN 7 300
DBREF 3E7A C 1 5 NOR NOR00279 NOR00279 1 5
DBREF 3E7A D 1 5 NOR NOR00279 NOR00279 1 5
SEQADV 3E7A GLY A 2 UNP P62136 EXPRESSION TAG
SEQADV 3E7A HIS A 3 UNP P62136 EXPRESSION TAG
SEQADV 3E7A MET A 4 UNP P62136 EXPRESSION TAG
SEQADV 3E7A GLY A 5 UNP P62136 EXPRESSION TAG
SEQADV 3E7A SER A 6 UNP P62136 EXPRESSION TAG
SEQADV 3E7A GLY B 2 UNP P62136 EXPRESSION TAG
SEQADV 3E7A HIS B 3 UNP P62136 EXPRESSION TAG
SEQADV 3E7A MET B 4 UNP P62136 EXPRESSION TAG
SEQADV 3E7A GLY B 5 UNP P62136 EXPRESSION TAG
SEQADV 3E7A SER B 6 UNP P62136 EXPRESSION TAG
SEQRES 1 A 299 GLY HIS MET GLY SER LEU ASN LEU ASP SER ILE ILE GLY
SEQRES 2 A 299 ARG LEU LEU GLU VAL GLN GLY SER ARG PRO GLY LYS ASN
SEQRES 3 A 299 VAL GLN LEU THR GLU ASN GLU ILE ARG GLY LEU CYS LEU
SEQRES 4 A 299 LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU
SEQRES 5 A 299 GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS
SEQRES 6 A 299 GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY
SEQRES 7 A 299 GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP
SEQRES 8 A 299 TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS
SEQRES 9 A 299 LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE
SEQRES 10 A 299 PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN
SEQRES 11 A 299 ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR
SEQRES 12 A 299 ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN
SEQRES 13 A 299 CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE
SEQRES 14 A 299 CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET
SEQRES 15 A 299 GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO
SEQRES 16 A 299 ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO
SEQRES 17 A 299 ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN ASP ARG GLY
SEQRES 18 A 299 VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE
SEQRES 19 A 299 LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS
SEQRES 20 A 299 GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG
SEQRES 21 A 299 GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY
SEQRES 22 A 299 GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU
SEQRES 23 A 299 THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA ASP
SEQRES 1 B 299 GLY HIS MET GLY SER LEU ASN LEU ASP SER ILE ILE GLY
SEQRES 2 B 299 ARG LEU LEU GLU VAL GLN GLY SER ARG PRO GLY LYS ASN
SEQRES 3 B 299 VAL GLN LEU THR GLU ASN GLU ILE ARG GLY LEU CYS LEU
SEQRES 4 B 299 LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU
SEQRES 5 B 299 GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS
SEQRES 6 B 299 GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY
SEQRES 7 B 299 GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP
SEQRES 8 B 299 TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS
SEQRES 9 B 299 LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE
SEQRES 10 B 299 PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN
SEQRES 11 B 299 ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR
SEQRES 12 B 299 ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN
SEQRES 13 B 299 CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE
SEQRES 14 B 299 CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET
SEQRES 15 B 299 GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO
SEQRES 16 B 299 ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO
SEQRES 17 B 299 ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN ASP ARG GLY
SEQRES 18 B 299 VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE
SEQRES 19 B 299 LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS
SEQRES 20 B 299 GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG
SEQRES 21 B 299 GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY
SEQRES 22 B 299 GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU
SEQRES 23 B 299 THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA ASP
SEQRES 1 C 5 ACB ARG 1ZN FGA MDH
SEQRES 1 D 5 ACB ARG 1ZN FGA MDH
HET ACB C 1 9
HET 1ZN C 3 23
HET FGA C 4 9
HET MDH C 5 7
HET ACB D 1 9
HET 1ZN D 3 23
HET FGA D 4 9
HET MDH D 5 7
HET MN A 402 1
HET MN A 403 1
HET IOD A 301 2
HET IOD A 302 2
HET IOD A 303 1
HET IOD A 404 2
HET IOD A 405 2
HET IOD A 406 2
HET IOD A 407 2
HET CL A 408 1
HET CL A 304 1
HET CL A 305 1
HET GOL A 409 6
HET MN B 402 1
HET MN B 403 1
HET IOD B 301 2
HET IOD B 302 2
HET IOD B 404 1
HET IOD B 405 1
HET IOD B 407 2
HET IOD B 406 2
HET IOD B 408 2
HET CL B 409 1
HET AZI B 303 3
HET AZI B 410 3
HET GOL B 411 6
HETNAM ACB 3-METHYL-BETA-D-ASPARTIC ACID
HETNAM 1ZN (2S,3S,4E,6E,8S,9S)-3-AMINO-9-METHOXY-2,6,8-TRIMETHYL-
HETNAM 2 1ZN 10-PHENYLDECA-4,6-DIENOIC ACID
HETNAM FGA GAMMA-D-GLUTAMIC ACID
HETNAM MDH N-METHYLDEHYDROBUTYRINE
HETNAM MN MANGANESE (II) ION
HETNAM IOD IODIDE ION
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETNAM AZI AZIDE ION
HETSYN ACB (3S)-3-METHYL-D-ASPARTIC ACID; D-METHYL ASPARTIC ACID
HETSYN FGA D-GLUTAMIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ACB 2(C5 H9 N O4)
FORMUL 3 1ZN 2(C20 H29 N O3)
FORMUL 3 FGA 2(C5 H9 N O4)
FORMUL 3 MDH 2(C5 H9 N O2)
FORMUL 5 MN 4(MN 2+)
FORMUL 7 IOD 14(I 1-)
FORMUL 14 CL 4(CL 1-)
FORMUL 17 GOL 2(C3 H8 O3)
FORMUL 28 AZI 2(N3 1-)
FORMUL 31 HOH *682(H2 O)
HELIX 1 1 ASN A 8 GLU A 18 1 11
HELIX 2 2 THR A 31 GLN A 49 1 19
HELIX 3 3 GLN A 68 GLY A 80 1 13
HELIX 4 4 GLN A 99 TYR A 114 1 16
HELIX 5 5 CYS A 127 GLY A 135 1 9
HELIX 6 6 GLY A 135 TYR A 144 1 10
HELIX 7 7 ASN A 145 ASN A 157 1 13
HELIX 8 8 MET A 183 ARG A 188 1 6
HELIX 9 9 GLY A 199 SER A 207 1 9
HELIX 10 10 GLY A 228 ASP A 240 1 13
HELIX 11 11 ASN A 271 GLU A 275 5 5
HELIX 12 12 ASN B 8 GLU B 18 1 11
HELIX 13 13 THR B 31 GLN B 49 1 19
HELIX 14 14 GLN B 68 GLY B 80 1 13
HELIX 15 15 GLN B 99 TYR B 114 1 16
HELIX 16 16 CYS B 127 GLY B 135 1 9
HELIX 17 17 GLY B 135 TYR B 144 1 10
HELIX 18 18 ASN B 145 ASN B 157 1 13
HELIX 19 19 MET B 183 ARG B 188 1 6
HELIX 20 20 GLY B 199 SER B 207 1 9
HELIX 21 21 GLY B 228 ASP B 240 1 13
HELIX 22 22 ASN B 271 GLU B 275 5 5
SHEET 1 A 6 LEU A 52 LEU A 55 0
SHEET 2 A 6 ALA A 162 VAL A 165 1 O ALA A 162 N LEU A 53
SHEET 3 A 6 ILE A 169 CYS A 172 -1 O CYS A 171 N ALA A 163
SHEET 4 A 6 LEU A 243 ARG A 246 1 O CYS A 245 N PHE A 170
SHEET 5 A 6 LEU A 263 LEU A 266 1 O LEU A 266 N ARG A 246
SHEET 6 A 6 TYR A 255 PHE A 258 -1 N GLU A 256 O THR A 265
SHEET 1 B 5 PHE A 118 LEU A 120 0
SHEET 2 B 5 TYR A 87 PHE A 89 1 N PHE A 89 O PHE A 119
SHEET 3 B 5 LEU A 59 CYS A 62 1 N CYS A 62 O LEU A 88
SHEET 4 B 5 GLY A 280 VAL A 285 -1 O MET A 283 N ILE A 61
SHEET 5 B 5 CYS A 291 LEU A 296 -1 O LEU A 296 N GLY A 280
SHEET 1 C 3 ASP A 208 PRO A 209 0
SHEET 2 C 3 PHE A 225 PHE A 227 1 O PHE A 227 N ASP A 208
SHEET 3 C 3 TRP A 216 GLU A 218 -1 N GLY A 217 O THR A 226
SHEET 1 D 6 LEU B 52 LEU B 55 0
SHEET 2 D 6 ALA B 162 VAL B 165 1 O ILE B 164 N LEU B 53
SHEET 3 D 6 ILE B 169 CYS B 172 -1 O CYS B 171 N ALA B 163
SHEET 4 D 6 LEU B 243 ARG B 246 1 O CYS B 245 N PHE B 170
SHEET 5 D 6 LEU B 263 LEU B 266 1 O VAL B 264 N ARG B 246
SHEET 6 D 6 TYR B 255 PHE B 258 -1 N PHE B 258 O LEU B 263
SHEET 1 E 5 PHE B 118 LEU B 120 0
SHEET 2 E 5 TYR B 87 PHE B 89 1 N PHE B 89 O PHE B 119
SHEET 3 E 5 LEU B 59 CYS B 62 1 N LYS B 60 O LEU B 88
SHEET 4 E 5 GLY B 280 VAL B 285 -1 O VAL B 285 N LEU B 59
SHEET 5 E 5 CYS B 291 LEU B 296 -1 O LEU B 296 N GLY B 280
SHEET 1 F 3 ASP B 208 PRO B 209 0
SHEET 2 F 3 PHE B 225 PHE B 227 1 O PHE B 227 N ASP B 208
SHEET 3 F 3 TRP B 216 GLU B 218 -1 N GLY B 217 O THR B 226
LINK CG ACB C 1 N ARG C 2 1555 1555 1.33
LINK C ARG C 2 N1 1ZN C 3 1555 1555 1.34
LINK C20 1ZN C 3 N FGA C 4 1555 1555 1.33
LINK CG ACB D 1 N ARG D 2 1555 1555 1.33
LINK C ARG D 2 N1 1ZN D 3 1555 1555 1.35
LINK C20 1ZN D 3 N FGA D 4 1555 1555 1.34
LINK MN MN B 403 O HOH B 698 1555 1555 1.99
LINK MN MN A 403 O HOH A 669 1555 1555 2.00
LINK OD1 ASN B 124 MN MN B 403 1555 1555 2.06
LINK OD2 ASP A 64 MN MN A 402 1555 1555 2.06
LINK MN MN A 402 O HOH A 669 1555 1555 2.07
LINK OD1 ASN A 124 MN MN A 403 1555 1555 2.08
LINK OD2 ASP B 64 MN MN B 402 1555 1555 2.08
LINK MN MN B 402 O HOH B 698 1555 1555 2.09
LINK MN MN B 402 O HOH D 724 1555 1555 2.14
LINK NE2 HIS B 173 MN MN B 403 1555 1555 2.17
LINK NE2 HIS A 173 MN MN A 403 1555 1555 2.19
LINK NE2 HIS A 66 MN MN A 402 1555 1555 2.20
LINK NE2 HIS B 66 MN MN B 402 1555 1555 2.20
LINK OD2 ASP B 92 MN MN B 403 1555 1555 2.20
LINK MN MN A 402 O HOH C 769 1555 1555 2.21
LINK ND1 HIS A 248 MN MN A 403 1555 1555 2.23
LINK ND1 HIS B 248 MN MN B 403 1555 1555 2.23
LINK OD2 ASP B 92 MN MN B 402 1555 1555 2.24
LINK OD2 ASP A 92 MN MN A 402 1555 1555 2.24
LINK OD2 ASP A 92 MN MN A 403 1555 1555 2.24
LINK N ACB D 1 C MDH D 5 1555 1555 1.33
LINK N ACB C 1 C MDH C 5 1555 1555 1.33
LINK CD FGA C 4 N MDH C 5 1555 1555 1.34
LINK CD FGA D 4 N MDH D 5 1555 1555 1.35
CISPEP 1 ALA A 57 PRO A 58 0 3.71
CISPEP 2 PRO A 82 PRO A 83 0 3.18
CISPEP 3 ARG A 191 PRO A 192 0 1.90
CISPEP 4 ALA B 57 PRO B 58 0 1.82
CISPEP 5 PRO B 82 PRO B 83 0 7.02
CISPEP 6 ARG B 191 PRO B 192 0 0.22
SITE 1 AC1 6 ASP A 64 HIS A 66 ASP A 92 MN A 403
SITE 2 AC1 6 HOH A 669 HOH C 769
SITE 1 AC2 6 ASP A 92 ASN A 124 HIS A 173 HIS A 248
SITE 2 AC2 6 MN A 402 HOH A 669
SITE 1 AC3 3 LYS A 260 GLN A 262 HOH A 681
SITE 1 AC4 3 LYS A 113 ARG A 132 HOH A 591
SITE 1 AC5 6 GLY A 97 SER A 100 GLY A 135 PHE A 136
SITE 2 AC5 6 GLU A 139 HOH A 483
SITE 1 AC6 3 ARG A 261 ILE B 295 HOH B 548
SITE 1 AC7 2 LYS A 260 ARG A 261
SITE 1 AC8 2 GLN A 99 CL A 304
SITE 1 AC9 1 HOH A 636
SITE 1 BC1 3 ARG A 142 HOH A 530 HOH A 720
SITE 1 BC2 3 LYS A 98 IOD A 406 HOH A 740
SITE 1 BC3 6 GLN A 198 GLY A 199 ASP A 203 PHE A 225
SITE 2 BC3 6 HOH A 449 HOH A 761
SITE 1 BC4 7 GLN A 49 PRO A 50 GLU A 54 PHE A 119
SITE 2 BC4 7 HOH A 533 HOH A 643 HOH A 655
SITE 1 BC5 6 ASP B 64 HIS B 66 ASP B 92 MN B 403
SITE 2 BC5 6 HOH B 698 HOH D 724
SITE 1 BC6 6 ASP B 92 ASN B 124 HIS B 173 HIS B 248
SITE 2 BC6 6 MN B 402 HOH B 698
SITE 1 BC7 2 ILE A 295 ARG B 261
SITE 1 BC8 2 LYS B 260 ARG B 261
SITE 1 BC9 6 GLY B 97 SER B 100 GLY B 135 PHE B 136
SITE 2 BC9 6 GLU B 139 HOH B 521
SITE 1 CC1 2 GLN B 262 HOH B 703
SITE 1 CC2 3 TYR B 69 TYR B 70 GLN B 99
SITE 1 CC3 3 GLY B 215 GLU B 230 VAL B 231
SITE 1 CC4 3 SER B 129 ARG B 132 HOH B 451
SITE 1 CC5 7 GLN B 49 PRO B 50 LEU B 53 GLU B 54
SITE 2 CC5 7 GLU B 116 PHE B 119 HOH B 667
SITE 1 CC6 22 ARG A 96 SER A 129 TYR A 134 VAL A 195
SITE 2 CC6 22 PRO A 196 TRP A 206 ASP A 220 ARG A 221
SITE 3 CC6 22 TYR A 272 GLU A 275 PHE A 276 GLU B 184
SITE 4 CC6 22 ARG B 187 HOH C 389 HOH C 766 HOH C 767
SITE 5 CC6 22 HOH C 768 HOH C 769 HOH C 770 HOH C 774
SITE 6 CC6 22 HOH C 775 HOH C 776
SITE 1 CC7 20 ARG B 96 SER B 129 TYR B 134 VAL B 195
SITE 2 CC7 20 PRO B 196 ASP B 197 TRP B 206 ARG B 221
SITE 3 CC7 20 VAL B 223 TYR B 272 GLU B 275 PHE B 276
SITE 4 CC7 20 HOH B 607 HOH B 710 HOH D 719 HOH D 720
SITE 5 CC7 20 HOH D 721 HOH D 722 HOH D 723 HOH D 724
CRYST1 65.354 77.274 132.444 90.00 90.00 90.00 P 21 21 21 8
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 0.015301 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012941 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007550 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
