HEADER STRUCTURAL PROTEIN 28-JUL-04 1U5P
TITLE CRYSTAL STRUCTURE OF REPEATS 15 AND 16 OF CHICKEN BRAIN ALPHA SPECTRIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SPECTRIN ALPHA CHAIN, BRAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: REPEATS 15 AND 16 (RESIDUES 1662 TO 1876);
COMPND 5 SYNONYM: ALPHA SPECTRIN, SPECTRIN, NON-ERYTHROID ALPHA CHAIN, FODRIN
COMPND 6 ALPHA CHAIN;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 TISSUE: BRAIN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3D
KEYWDS ALPHA SPECTRIN, TWO REPEATS OF SPECTRIN, ALPHA-HELICAL LINKER REGION,
KEYWDS 2 3-HELIX COILED COIL, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.KUSUNOKI,G.MINASOV,R.I.MACDONALD,A.MONDRAGON
REVDAT 4 13-MAR-24 1U5P 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1U5P 1 VERSN
REVDAT 2 30-NOV-04 1U5P 1 JRNL
REVDAT 1 19-OCT-04 1U5P 0
JRNL AUTH H.KUSUNOKI,G.MINASOV,R.I.MACDONALD,A.MONDRAGON
JRNL TITL INDEPENDENT MOVEMENT, DIMERIZATION AND STABILITY OF TANDEM
JRNL TITL 2 REPEATS OF CHICKEN BRAIN ALPHA-SPECTRIN
JRNL REF J.MOL.BIOL. V. 344 495 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15522301
JRNL DOI 10.1016/J.JMB.2004.09.019
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 36092
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1897
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2596
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2070
REMARK 3 BIN FREE R VALUE SET COUNT : 130
REMARK 3 BIN FREE R VALUE : 0.2120
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1706
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 374
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : UNVERIFIED
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.113
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.117
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.074
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.634
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1972 ; 0.021 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1807 ; 0.013 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2648 ; 1.911 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4266 ; 1.627 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 227 ; 4.902 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 293 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2146 ; 0.016 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 383 ; 0.017 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 406 ; 0.186 ; 0.100
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1972 ; 0.179 ; 0.100
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1223 ; 0.072 ; 0.100
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 654 ; 0.199 ; 0.100
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): 7 ; 0.097 ; 0.100
REMARK 3 SYMMETRY VDW OTHERS (A): 59 ; 0.174 ; 0.100
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 79 ; 0.237 ; 0.100
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): 1138 ; 2.060 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1860 ; 2.686 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 834 ; 4.299 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 788 ; 6.240 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 33
REMARK 3 ORIGIN FOR THE GROUP (A): -53.8772 46.2474 10.1920
REMARK 3 T TENSOR
REMARK 3 T11: 0.1092 T22: 0.0606
REMARK 3 T33: 0.0472 T12: -0.0139
REMARK 3 T13: -0.0259 T23: -0.0459
REMARK 3 L TENSOR
REMARK 3 L11: 4.9318 L22: 5.6551
REMARK 3 L33: 11.5829 L12: -3.6668
REMARK 3 L13: 6.0113 L23: -6.5541
REMARK 3 S TENSOR
REMARK 3 S11: -0.0659 S12: -0.1346 S13: 0.0369
REMARK 3 S21: -0.0367 S22: 0.1064 S23: -0.0617
REMARK 3 S31: -0.0721 S32: -0.0662 S33: -0.0405
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 34 A 55
REMARK 3 ORIGIN FOR THE GROUP (A): -46.9082 30.2274 14.2666
REMARK 3 T TENSOR
REMARK 3 T11: 0.0754 T22: 0.0762
REMARK 3 T33: 0.3042 T12: -0.0287
REMARK 3 T13: -0.1217 T23: 0.0406
REMARK 3 L TENSOR
REMARK 3 L11: 10.5409 L22: 10.5419
REMARK 3 L33: 16.1194 L12: -8.9342
REMARK 3 L13: 8.1747 L23: -11.2323
REMARK 3 S TENSOR
REMARK 3 S11: 0.1817 S12: -0.5946 S13: -1.1711
REMARK 3 S21: -0.2803 S22: 0.3280 S23: 0.5613
REMARK 3 S31: 0.4359 S32: -0.3673 S33: -0.5097
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 56 A 74
REMARK 3 ORIGIN FOR THE GROUP (A): -55.1024 51.2446 -4.4819
REMARK 3 T TENSOR
REMARK 3 T11: 0.1863 T22: 0.1029
REMARK 3 T33: 0.0397 T12: -0.0290
REMARK 3 T13: -0.0609 T23: -0.0280
REMARK 3 L TENSOR
REMARK 3 L11: 3.6109 L22: 18.9559
REMARK 3 L33: 5.7607 L12: -4.6865
REMARK 3 L13: 2.3141 L23: -10.5163
REMARK 3 S TENSOR
REMARK 3 S11: -0.1748 S12: 0.2208 S13: 0.1368
REMARK 3 S21: -0.3260 S22: -0.0267 S23: -0.4551
REMARK 3 S31: 0.1677 S32: 0.1932 S33: 0.2016
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 75 A 140
REMARK 3 ORIGIN FOR THE GROUP (A): -36.5127 29.1352 20.0200
REMARK 3 T TENSOR
REMARK 3 T11: 0.0949 T22: 0.1140
REMARK 3 T33: 0.1673 T12: -0.0199
REMARK 3 T13: -0.0522 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 4.9965 L22: 10.6878
REMARK 3 L33: 6.4214 L12: -6.9927
REMARK 3 L13: 5.4036 L23: -8.0751
REMARK 3 S TENSOR
REMARK 3 S11: 0.0656 S12: -0.1147 S13: -0.3770
REMARK 3 S21: 0.0922 S22: 0.1841 S23: 0.3968
REMARK 3 S31: -0.0325 S32: -0.0141 S33: -0.2497
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 141 A 161
REMARK 3 ORIGIN FOR THE GROUP (A): -15.5309 -3.1007 37.4867
REMARK 3 T TENSOR
REMARK 3 T11: 0.6798 T22: 0.1798
REMARK 3 T33: 0.2844 T12: 0.0908
REMARK 3 T13: -0.0583 T23: 0.0501
REMARK 3 L TENSOR
REMARK 3 L11: 1.6629 L22: 26.0269
REMARK 3 L33: 49.1530 L12: -4.5876
REMARK 3 L13: 4.7290 L23: -33.1126
REMARK 3 S TENSOR
REMARK 3 S11: 0.5492 S12: -0.0825 S13: -0.5029
REMARK 3 S21: -2.1015 S22: -0.6904 S23: 0.0983
REMARK 3 S31: 3.8088 S32: 0.8574 S33: 0.1412
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 162 A 180
REMARK 3 ORIGIN FOR THE GROUP (A): -21.6286 21.9361 22.0358
REMARK 3 T TENSOR
REMARK 3 T11: 0.0971 T22: 0.1500
REMARK 3 T33: 0.1193 T12: 0.0464
REMARK 3 T13: -0.0746 T23: -0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 8.8613 L22: 22.0804
REMARK 3 L33: 5.5296 L12: -10.9572
REMARK 3 L13: 3.8711 L23: -7.4366
REMARK 3 S TENSOR
REMARK 3 S11: 0.1436 S12: 0.3168 S13: 0.3132
REMARK 3 S21: -0.4935 S22: -0.2233 S23: -0.1476
REMARK 3 S31: 0.2860 S32: 0.2379 S33: 0.0796
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 181 A 212
REMARK 3 ORIGIN FOR THE GROUP (A): -20.6892 16.5908 35.6460
REMARK 3 T TENSOR
REMARK 3 T11: 0.0637 T22: 0.1633
REMARK 3 T33: 0.0989 T12: 0.0328
REMARK 3 T13: 0.0143 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 6.8119 L22: 19.6955
REMARK 3 L33: 9.2669 L12: -9.8376
REMARK 3 L13: 7.4134 L23: -12.3664
REMARK 3 S TENSOR
REMARK 3 S11: -0.1968 S12: -0.3235 S13: 0.0098
REMARK 3 S21: 0.4148 S22: 0.1084 S23: -0.0440
REMARK 3 S31: -0.1955 S32: -0.2661 S33: 0.0884
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 1U5P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1000023277.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-APR-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 5ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794, 1.0721, 1.0494
REMARK 200 MONOCHROMATOR : SILICON MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS, SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38078
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 28.513
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.00
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : 0.07200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.50
REMARK 200 R MERGE FOR SHELL (I) : 0.31400
REMARK 200 R SYM FOR SHELL (I) : 0.29800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SOLVE, SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 77.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M NAH2PO4, 1M K2HPO4, 0.2M AMMONIUM
REMARK 280 ACETATE, 0.1M TRIS-HCL, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 287K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 3 2
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 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 Y+1/4,X+3/4,-Z+3/4
REMARK 290 14555 -Y+1/4,-X+1/4,-Z+1/4
REMARK 290 15555 Y+3/4,-X+3/4,Z+1/4
REMARK 290 16555 -Y+3/4,X+1/4,Z+3/4
REMARK 290 17555 X+1/4,Z+3/4,-Y+3/4
REMARK 290 18555 -X+3/4,Z+1/4,Y+3/4
REMARK 290 19555 -X+1/4,-Z+1/4,-Y+1/4
REMARK 290 20555 X+3/4,-Z+3/4,Y+1/4
REMARK 290 21555 Z+1/4,Y+3/4,-X+3/4
REMARK 290 22555 Z+3/4,-Y+3/4,X+1/4
REMARK 290 23555 -Z+3/4,Y+1/4,X+3/4
REMARK 290 24555 -Z+1/4,-Y+1/4,-X+1/4
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 74.10000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.10000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 74.10000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.10000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 74.10000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 74.10000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 74.10000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 74.10000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 74.10000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 74.10000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 74.10000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 74.10000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 74.10000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 74.10000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 74.10000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 74.10000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 74.10000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 74.10000
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 37.05000
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 111.15000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 111.15000
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 37.05000
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 37.05000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 37.05000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 111.15000
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 111.15000
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 37.05000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 111.15000
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 37.05000
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 111.15000
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 37.05000
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 111.15000
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 111.15000
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 111.15000
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 37.05000
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 111.15000
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 37.05000
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 37.05000
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 37.05000
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 111.15000
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 111.15000
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 37.05000
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 37.05000
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 111.15000
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 111.15000
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 111.15000
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 111.15000
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 37.05000
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 111.15000
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 37.05000
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 111.15000
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 37.05000
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 37.05000
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 37.05000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 P PO4 A 2 LIES ON A SPECIAL POSITION.
REMARK 375 O4 PO4 A 2 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 165 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 187 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 363 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1661
REMARK 465 GLU A 1873
REMARK 465 SER A 1874
REMARK 465 LEU A 1875
REMARK 465 GLU A 1876
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 ASP A1694 CB - CG - OD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ASP A1717 CB - CA - C ANGL. DEV. = 16.0 DEGREES
REMARK 500 ARG A1718 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A1718 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A1753 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A1753 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A1770 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A1770 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A1770 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A1770 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP A1796 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A1800 CB - CG - OD2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 ARG A1808 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A1870 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CUN RELATED DB: PDB
REMARK 900 CHICKEN BRAIN ALPHA SPECTRIN REPEATS 16 AND 17
REMARK 900 RELATED ID: 1U4Q RELATED DB: PDB
REMARK 900 CHICKEN BRAIN ALPHA SPECTRIN REPEATS 15, 16 AND 17
REMARK 900 RELATED ID: 1S35 RELATED DB: PDB
REMARK 900 HUMAN ERYTHROID BETA SPECTRIN REPEATS 8 AND 9
DBREF 1U5P A 1662 1876 UNP P07751 SPTA2_CHICK 1662 1876
SEQADV 1U5P MET A 1661 UNP P07751 INITIATING METHIONINE
SEQRES 1 A 216 MET ALA ASN LYS GLN GLN ASN PHE ASN THR GLY ILE LYS
SEQRES 2 A 216 ASP PHE ASP PHE TRP LEU SER GLU VAL GLU ALA LEU LEU
SEQRES 3 A 216 ALA SER GLU ASP TYR GLY LYS ASP LEU ALA SER VAL ASN
SEQRES 4 A 216 ASN LEU LEU LYS LYS HIS GLN LEU LEU GLU ALA ASP ILE
SEQRES 5 A 216 SER ALA HIS GLU ASP ARG LEU LYS ASP LEU ASN SER GLN
SEQRES 6 A 216 ALA ASP SER LEU MET THR SER SER ALA PHE ASP THR SER
SEQRES 7 A 216 GLN VAL LYS ASP LYS ARG GLU THR ILE ASN GLY ARG PHE
SEQRES 8 A 216 GLN ARG ILE LYS SER MET ALA ALA ALA ARG ARG ALA LYS
SEQRES 9 A 216 LEU ASN GLU SER HIS ARG LEU HIS GLN PHE PHE ARG ASP
SEQRES 10 A 216 MET ASP ASP GLU GLU SER TRP ILE LYS GLU LYS LYS LEU
SEQRES 11 A 216 LEU VAL SER SER GLU ASP TYR GLY ARG ASP LEU THR GLY
SEQRES 12 A 216 VAL GLN ASN LEU ARG LYS LYS HIS LYS ARG LEU GLU ALA
SEQRES 13 A 216 GLU LEU ALA ALA HIS GLU PRO ALA ILE GLN GLY VAL LEU
SEQRES 14 A 216 ASP THR GLY LYS LYS LEU SER ASP ASP ASN THR ILE GLY
SEQRES 15 A 216 LYS GLU GLU ILE GLN GLN ARG LEU ALA GLN PHE VAL ASP
SEQRES 16 A 216 HIS TRP LYS GLU LEU LYS GLN LEU ALA ALA ALA ARG GLY
SEQRES 17 A 216 GLN ARG LEU GLU GLU SER LEU GLU
HET K A 1 1
HET PO4 A 2 5
HETNAM K POTASSIUM ION
HETNAM PO4 PHOSPHATE ION
FORMUL 2 K K 1+
FORMUL 3 PO4 O4 P 3-
FORMUL 4 HOH *374(H2 O)
HELIX 1 1 ASN A 1663 ALA A 1687 1 25
HELIX 2 2 ASP A 1694 THR A 1731 1 38
HELIX 3 3 THR A 1737 SER A 1793 1 57
HELIX 4 4 ASP A 1800 ASP A 1838 1 39
HELIX 5 5 LYS A 1843 LEU A 1871 1 29
SITE 1 AC1 3 HOH A 375 SER A1732 SER A1733
CRYST1 148.200 148.200 148.200 90.00 90.00 90.00 P 43 3 2 24
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 0.006748 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006748 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006748 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
