HEADER CONTRACTILE PROTEIN 29-SEP-11 3U1A
TITLE N-TERMINAL 81-AA FRAGMENT OF SMOOTH MUSCLE TROPOMYOSIN ALPHA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SMOOTH MUSCLE TROPOMYOSIN ALPHA;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 1-81;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: BANTAM,CHICKENS;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTYB12
KEYWDS MUSCLE CONTRACTION, ACTIN, CONTRACTILE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR N.JAMPANI,R.DOMINGUEZ
REVDAT 3 28-FEB-24 3U1A 1 SEQADV
REVDAT 2 04-SEP-13 3U1A 1 JRNL
REVDAT 1 23-NOV-11 3U1A 0
JRNL AUTH J.N.RAO,R.RIVERA-SANTIAGO,X.E.LI,W.LEHMAN,R.DOMINGUEZ
JRNL TITL STRUCTURAL ANALYSIS OF SMOOTH MUSCLE TROPOMYOSIN ALPHA AND
JRNL TITL 2 BETA ISOFORMS.
JRNL REF J.BIOL.CHEM. V. 287 3165 2012
JRNL REFN ISSN 0021-9258
JRNL PMID 22119916
JRNL DOI 10.1074/JBC.M111.307330
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.52
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 24909
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 1253
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.5263 - 4.1588 0.99 2895 154 0.2174 0.2548
REMARK 3 2 4.1588 - 3.3015 0.99 2782 147 0.1977 0.2414
REMARK 3 3 3.3015 - 2.8843 0.98 2708 144 0.2243 0.2598
REMARK 3 4 2.8843 - 2.6206 0.97 2664 141 0.2350 0.2620
REMARK 3 5 2.6206 - 2.4328 0.96 2626 139 0.2388 0.3029
REMARK 3 6 2.4328 - 2.2894 0.95 2599 138 0.2346 0.2671
REMARK 3 7 2.2894 - 2.1748 0.93 2516 134 0.2226 0.3229
REMARK 3 8 2.1748 - 2.0801 0.90 2446 131 0.2512 0.2739
REMARK 3 9 2.0801 - 2.0000 0.89 2420 125 0.2647 0.3328
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.31
REMARK 3 B_SOL : 41.19
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.930
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.04700
REMARK 3 B22 (A**2) : 0.87710
REMARK 3 B33 (A**2) : -7.92410
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 2668
REMARK 3 ANGLE : 0.935 3557
REMARK 3 CHIRALITY : 0.073 396
REMARK 3 PLANARITY : 0.003 483
REMARK 3 DIHEDRAL : 19.956 1098
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 20.6208 7.2301 9.4895
REMARK 3 T TENSOR
REMARK 3 T11: 0.3572 T22: 0.1265
REMARK 3 T33: 0.0768 T12: -0.0071
REMARK 3 T13: 0.0175 T23: -0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 0.5054 L22: 0.2741
REMARK 3 L33: 0.4462 L12: -0.0130
REMARK 3 L13: -0.4230 L23: -0.1551
REMARK 3 S TENSOR
REMARK 3 S11: 0.1329 S12: -0.1263 S13: 0.0621
REMARK 3 S21: -0.0563 S22: -0.0529 S23: -0.0351
REMARK 3 S31: -0.2759 S32: -0.0765 S33: 0.0161
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 21.3412 5.7147 12.5096
REMARK 3 T TENSOR
REMARK 3 T11: 0.3554 T22: 0.1153
REMARK 3 T33: 0.0692 T12: -0.0408
REMARK 3 T13: 0.0008 T23: -0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 0.3589 L22: 0.2513
REMARK 3 L33: 0.2926 L12: -0.0838
REMARK 3 L13: -0.1470 L23: 0.1360
REMARK 3 S TENSOR
REMARK 3 S11: -0.0669 S12: -0.1629 S13: -0.0278
REMARK 3 S21: -0.0493 S22: -0.0412 S23: 0.0028
REMARK 3 S31: -0.0221 S32: 0.2866 S33: 0.0149
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): 2.7816 24.0430 -6.9616
REMARK 3 T TENSOR
REMARK 3 T11: 0.3760 T22: 0.1085
REMARK 3 T33: 0.0846 T12: 0.0142
REMARK 3 T13: 0.0159 T23: 0.0274
REMARK 3 L TENSOR
REMARK 3 L11: 0.1899 L22: 0.3474
REMARK 3 L33: 0.2013 L12: 0.0405
REMARK 3 L13: -0.1529 L23: 0.0410
REMARK 3 S TENSOR
REMARK 3 S11: 0.0462 S12: 0.0691 S13: 0.0632
REMARK 3 S21: -0.0515 S22: -0.0046 S23: 0.0282
REMARK 3 S31: -0.0771 S32: 0.1637 S33: -0.0967
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN D
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9941 22.5574 -9.0760
REMARK 3 T TENSOR
REMARK 3 T11: 0.4431 T22: 0.1859
REMARK 3 T33: 0.1151 T12: 0.0522
REMARK 3 T13: -0.0088 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 0.0474 L22: 0.3014
REMARK 3 L33: 0.3543 L12: 0.0630
REMARK 3 L13: 0.1427 L23: -0.3619
REMARK 3 S TENSOR
REMARK 3 S11: 0.0908 S12: 0.0846 S13: 0.0440
REMARK 3 S21: -0.0864 S22: 0.0829 S23: 0.0463
REMARK 3 S31: 0.2006 S32: 0.0182 S33: -0.1232
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3U1A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1000068179.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25949
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 12.05
REMARK 200 R MERGE (I) : 0.10580
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.5900
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) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 10.40
REMARK 200 R MERGE FOR SHELL (I) : 0.41980
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.520
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX AUTOSOL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, PH 4.4, 20 MM
REMARK 280 CALCIUM CHLORIDE, 30-33 % 2-METHYL-2,4-PENTANEDIOL , VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 29.38400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.64950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.59050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.64950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.38400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.59050
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, 3
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: 3550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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: 3440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 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 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 29.38400
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 31.59050
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -101.29900
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 ALA A -2
REMARK 465 GLY A -1
REMARK 465 ALA D -2
REMARK 465 GLY D -1
REMARK 465 LYS D 80
REMARK 465 ALA D 81
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 HIS A 0 CG ND1 CD2 CE1 NE2
REMARK 470 HIS D 0 CG ND1 CD2 CE1 NE2
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 HOH C 104 O HOH C 152 1.81
REMARK 500 O HOH A 203 O HOH B 216 1.82
REMARK 500 O HOH C 121 O HOH C 159 1.83
REMARK 500 O HOH A 85 O HOH A 148 1.85
REMARK 500 OD2 ASP A 69 O HOH A 89 1.85
REMARK 500 O HOH A 179 O HOH A 183 1.89
REMARK 500 O ALA A 18 O HOH A 178 1.89
REMARK 500 OE1 GLU B 62 O HOH B 200 1.89
REMARK 500 O HOH A 98 O HOH A 164 1.93
REMARK 500 NH1 ARG C 51 O HOH C 154 1.93
REMARK 500 O HOH C 89 O HOH C 173 1.96
REMARK 500 NE ARG A 21 O HOH A 196 2.00
REMARK 500 NH2 ARG D 35 O HOH D 188 2.01
REMARK 500 O HOH C 186 O HOH C 193 2.04
REMARK 500 O HOH A 182 O HOH C 174 2.05
REMARK 500 OE1 GLU B 26 O HOH B 83 2.06
REMARK 500 OD1 ASP D 42 O HOH D 184 2.07
REMARK 500 CZ ARG A 21 O HOH A 196 2.07
REMARK 500 NZ LYS D 29 O HOH D 105 2.08
REMARK 500 O HOH D 197 O HOH D 213 2.10
REMARK 500 O HOH A 162 O HOH C 214 2.11
REMARK 500 O HOH B 189 O HOH B 210 2.12
REMARK 500 O ALA A 3 O HOH A 99 2.13
REMARK 500 NE2 HIS B 65 O HOH B 176 2.14
REMARK 500 CB ARG A 21 O HOH A 178 2.14
REMARK 500 O HOH C 98 O HOH C 163 2.14
REMARK 500 O ASP C 20 OE1 GLU C 23 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 B 200 O HOH C 89 4555 1.96
REMARK 500 OE1 GLN A 45 O HOH D 85 4555 1.98
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 HIS B 0 -162.11 141.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3U1C RELATED DB: PDB
REMARK 900 RELATED ID: 3U59 RELATED DB: PDB
DBREF 3U1A A 1 81 UNP P04268 P04268 1 81
DBREF 3U1A B 1 81 UNP P04268 P04268 1 81
DBREF 3U1A C 1 81 UNP P04268 P04268 1 81
DBREF 3U1A D 1 81 UNP P04268 P04268 1 81
SEQADV 3U1A ALA A -2 UNP P04268 EXPRESSION TAG
SEQADV 3U1A GLY A -1 UNP P04268 EXPRESSION TAG
SEQADV 3U1A HIS A 0 UNP P04268 EXPRESSION TAG
SEQADV 3U1A ALA B -2 UNP P04268 EXPRESSION TAG
SEQADV 3U1A GLY B -1 UNP P04268 EXPRESSION TAG
SEQADV 3U1A HIS B 0 UNP P04268 EXPRESSION TAG
SEQADV 3U1A ALA C -2 UNP P04268 EXPRESSION TAG
SEQADV 3U1A GLY C -1 UNP P04268 EXPRESSION TAG
SEQADV 3U1A HIS C 0 UNP P04268 EXPRESSION TAG
SEQADV 3U1A ALA D -2 UNP P04268 EXPRESSION TAG
SEQADV 3U1A GLY D -1 UNP P04268 EXPRESSION TAG
SEQADV 3U1A HIS D 0 UNP P04268 EXPRESSION TAG
SEQRES 1 A 84 ALA GLY HIS MET ASP ALA ILE LYS LYS LYS MET GLN MET
SEQRES 2 A 84 LEU LYS LEU ASP LYS GLU ASN ALA LEU ASP ARG ALA GLU
SEQRES 3 A 84 GLN ALA GLU ALA ASP LYS LYS ALA ALA GLU GLU ARG SER
SEQRES 4 A 84 LYS GLN LEU GLU ASP ASP ILE VAL GLN LEU GLU LYS GLN
SEQRES 5 A 84 LEU ARG VAL THR GLU ASP SER ARG ASP GLN VAL LEU GLU
SEQRES 6 A 84 GLU LEU HIS LYS SER GLU ASP SER LEU LEU PHE ALA GLU
SEQRES 7 A 84 GLU ASN ALA ALA LYS ALA
SEQRES 1 B 84 ALA GLY HIS MET ASP ALA ILE LYS LYS LYS MET GLN MET
SEQRES 2 B 84 LEU LYS LEU ASP LYS GLU ASN ALA LEU ASP ARG ALA GLU
SEQRES 3 B 84 GLN ALA GLU ALA ASP LYS LYS ALA ALA GLU GLU ARG SER
SEQRES 4 B 84 LYS GLN LEU GLU ASP ASP ILE VAL GLN LEU GLU LYS GLN
SEQRES 5 B 84 LEU ARG VAL THR GLU ASP SER ARG ASP GLN VAL LEU GLU
SEQRES 6 B 84 GLU LEU HIS LYS SER GLU ASP SER LEU LEU PHE ALA GLU
SEQRES 7 B 84 GLU ASN ALA ALA LYS ALA
SEQRES 1 C 84 ALA GLY HIS MET ASP ALA ILE LYS LYS LYS MET GLN MET
SEQRES 2 C 84 LEU LYS LEU ASP LYS GLU ASN ALA LEU ASP ARG ALA GLU
SEQRES 3 C 84 GLN ALA GLU ALA ASP LYS LYS ALA ALA GLU GLU ARG SER
SEQRES 4 C 84 LYS GLN LEU GLU ASP ASP ILE VAL GLN LEU GLU LYS GLN
SEQRES 5 C 84 LEU ARG VAL THR GLU ASP SER ARG ASP GLN VAL LEU GLU
SEQRES 6 C 84 GLU LEU HIS LYS SER GLU ASP SER LEU LEU PHE ALA GLU
SEQRES 7 C 84 GLU ASN ALA ALA LYS ALA
SEQRES 1 D 84 ALA GLY HIS MET ASP ALA ILE LYS LYS LYS MET GLN MET
SEQRES 2 D 84 LEU LYS LEU ASP LYS GLU ASN ALA LEU ASP ARG ALA GLU
SEQRES 3 D 84 GLN ALA GLU ALA ASP LYS LYS ALA ALA GLU GLU ARG SER
SEQRES 4 D 84 LYS GLN LEU GLU ASP ASP ILE VAL GLN LEU GLU LYS GLN
SEQRES 5 D 84 LEU ARG VAL THR GLU ASP SER ARG ASP GLN VAL LEU GLU
SEQRES 6 D 84 GLU LEU HIS LYS SER GLU ASP SER LEU LEU PHE ALA GLU
SEQRES 7 D 84 GLU ASN ALA ALA LYS ALA
FORMUL 5 HOH *216(H2 O)
HELIX 1 1 HIS A 0 ALA A 81 1 82
HELIX 2 2 HIS B 0 ALA B 81 1 82
HELIX 3 3 ASP C 2 ALA C 81 1 80
HELIX 4 4 MET D 1 ALA D 79 1 79
CRYST1 58.768 63.181 101.299 90.00 90.00 90.00 P 21 21 21 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017016 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015828 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009872 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
