HEADER STRUCTURAL PROTEIN 06-FEB-10 3LPW
TITLE CRYSTAL STRUCTURE OF THE FNIII-TANDEM A77-A78 FROM THE A-BAND OF TITIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: A77-A78 DOMAIN FROM TITIN;
COMPND 3 CHAIN: A, B;
COMPND 4 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: TTN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DL3)ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETM-11
KEYWDS INTRACELLULAR FNIII-TANDEM, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.M.BUCHER,O.MAYANS
REVDAT 2 01-NOV-23 3LPW 1 REMARK SEQADV
REVDAT 1 08-SEP-10 3LPW 0
JRNL AUTH R.M.BUCHER,D.I.SVERGUN,C.MUHLE-GOLL,O.MAYANS
JRNL TITL THE STRUCTURE OF THE FNIII TANDEM A77-A78 POINTS TO A
JRNL TITL 2 PERIODICALLY CONSERVED ARCHITECTURE IN THE MYOSIN-BINDING
JRNL TITL 3 REGION OF TITIN
JRNL REF J.MOL.BIOL. V. 401 843 2010
JRNL REFN ISSN 0022-2836
JRNL PMID 20542041
JRNL DOI 10.1016/J.JMB.2010.06.011
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 74213
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.320
REMARK 3 FREE R VALUE TEST SET COUNT : 978
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 19.8060 - 3.1530 0.99 10714 173 0.1540 0.1920
REMARK 3 2 3.1530 - 2.5040 1.00 10530 117 0.1690 0.2070
REMARK 3 3 2.5040 - 2.1880 1.00 10469 140 0.1640 0.2050
REMARK 3 4 2.1880 - 1.9880 1.00 10409 159 0.1620 0.1820
REMARK 3 5 1.9880 - 1.8460 1.00 10426 120 0.1910 0.2110
REMARK 3 6 1.8460 - 1.7370 1.00 10411 151 0.2470 0.2490
REMARK 3 7 1.7370 - 1.6500 0.99 10276 118 0.3090 0.3270
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 : 0.35
REMARK 3 B_SOL : 60.26
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.740
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.47
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.60600
REMARK 3 B22 (A**2) : 2.06900
REMARK 3 B33 (A**2) : -0.46400
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 : 0.006 3159
REMARK 3 ANGLE : 1.019 4306
REMARK 3 CHIRALITY : 0.069 493
REMARK 3 PLANARITY : 0.005 549
REMARK 3 DIHEDRAL : 16.615 1192
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESID 1:100
REMARK 3 ORIGIN FOR THE GROUP (A): 46.4818 54.3337 29.7654
REMARK 3 T TENSOR
REMARK 3 T11: 0.1196 T22: 0.0977
REMARK 3 T33: 0.1156 T12: -0.0578
REMARK 3 T13: -0.0142 T23: 0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 0.9739 L22: 1.6671
REMARK 3 L33: 0.9176 L12: 0.4305
REMARK 3 L13: -0.6272 L23: -1.0088
REMARK 3 S TENSOR
REMARK 3 S11: 0.0238 S12: -0.0832 S13: 0.0168
REMARK 3 S21: 0.0809 S22: -0.0742 S23: -0.0723
REMARK 3 S31: -0.0794 S32: 0.0565 S33: 0.0305
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESID 101:197
REMARK 3 ORIGIN FOR THE GROUP (A): 49.4476 91.2442 10.3047
REMARK 3 T TENSOR
REMARK 3 T11: 0.1500 T22: 0.0361
REMARK 3 T33: 0.0869 T12: -0.0048
REMARK 3 T13: -0.0130 T23: 0.0255
REMARK 3 L TENSOR
REMARK 3 L11: 1.6591 L22: 0.3879
REMARK 3 L33: 0.9940 L12: 0.3208
REMARK 3 L13: 0.3257 L23: -0.1240
REMARK 3 S TENSOR
REMARK 3 S11: -0.1464 S12: 0.0869 S13: 0.2206
REMARK 3 S21: -0.0790 S22: 0.0518 S23: 0.0628
REMARK 3 S31: -0.1952 S32: -0.0898 S33: 0.0959
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN B AND RESID 198:295
REMARK 3 ORIGIN FOR THE GROUP (A): 30.7488 31.2185 -14.2395
REMARK 3 T TENSOR
REMARK 3 T11: 0.0891 T22: 0.1520
REMARK 3 T33: 0.0806 T12: -0.0587
REMARK 3 T13: -0.0064 T23: 0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 1.9420 L22: 1.2358
REMARK 3 L33: 0.8828 L12: 0.1645
REMARK 3 L13: -1.1633 L23: -0.3787
REMARK 3 S TENSOR
REMARK 3 S11: 0.0153 S12: 0.0155 S13: -0.0072
REMARK 3 S21: -0.0783 S22: -0.0357 S23: -0.0071
REMARK 3 S31: 0.0972 S32: -0.0166 S33: 0.0105
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN B AND RESID 296:392
REMARK 3 ORIGIN FOR THE GROUP (A): 66.8647 33.2356 5.9789
REMARK 3 T TENSOR
REMARK 3 T11: 0.0500 T22: 0.1221
REMARK 3 T33: 0.0536 T12: -0.0031
REMARK 3 T13: -0.0019 T23: -0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 1.2243 L22: 1.2835
REMARK 3 L33: 2.0939 L12: 0.0754
REMARK 3 L13: -0.8345 L23: 0.1061
REMARK 3 S TENSOR
REMARK 3 S11: -0.0424 S12: -0.1965 S13: -0.0271
REMARK 3 S21: 0.0306 S22: -0.0007 S23: -0.0905
REMARK 3 S31: 0.1281 S32: 0.0731 S33: 0.0460
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 3LPW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-FEB-10.
REMARK 100 THE DEPOSITION ID IS D_1000057581.
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 : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ELLIOTT GX-20
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : CU-KA
REMARK 200 OPTICS : OSMIC CONFOCAL SYSTEM
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74213
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 19.805
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.36800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
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: A170 EXTRACTED FROM PDB ENTRY 2NZI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 32.60000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 32.60000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 57.95000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 81.60000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 57.95000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 81.60000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 32.60000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 57.95000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 81.60000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 32.60000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 57.95000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 81.60000
REMARK 290 SMTRY3 8 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 HOH A 201 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 247 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 486 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 660 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 419 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 GLY B 1
REMARK 465 ALA B 2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLU A 16 O HOH A 311 2.14
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 THR A 62 43.91 -91.85
REMARK 500 ASP A 67 -167.48 -115.30
REMARK 500 ASN A 83 -167.94 -122.76
REMARK 500 THR A 158 44.89 -98.67
REMARK 500 THR B 62 45.41 -84.15
REMARK 500 ASP B 67 -169.29 -115.71
REMARK 500 THR B 158 41.07 -89.47
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 MPD A 394
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD A 395
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 393
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2A38 RELATED DB: PDB
REMARK 900 RELATED ID: 2NZI RELATED DB: PDB
REMARK 900 RELATED ID: 3B43 RELATED DB: PDB
REMARK 900 RELATED ID: 2RIK RELATED DB: PDB
REMARK 900 RELATED ID: 2RJM RELATED DB: PDB
DBREF 3LPW A 4 197 UNP Q8WZ42 TITIN_HUMAN 22877 23070
DBREF 3LPW B 4 197 UNP Q8WZ42 TITIN_HUMAN 22877 23070
SEQADV 3LPW GLY A 1 UNP Q8WZ42 EXPRESSION TAG
SEQADV 3LPW ALA A 2 UNP Q8WZ42 EXPRESSION TAG
SEQADV 3LPW MET A 3 UNP Q8WZ42 EXPRESSION TAG
SEQADV 3LPW GLY B 1 UNP Q8WZ42 EXPRESSION TAG
SEQADV 3LPW ALA B 2 UNP Q8WZ42 EXPRESSION TAG
SEQADV 3LPW MET B 3 UNP Q8WZ42 EXPRESSION TAG
SEQRES 1 A 197 GLY ALA MET ASP THR PRO GLY PRO PRO GLN ASP LEU LYS
SEQRES 2 A 197 VAL LYS GLU VAL THR LYS THR SER VAL THR LEU THR TRP
SEQRES 3 A 197 ASP PRO PRO LEU LEU ASP GLY GLY SER LYS ILE LYS ASN
SEQRES 4 A 197 TYR ILE VAL GLU LYS ARG GLU SER THR ARG LYS ALA TYR
SEQRES 5 A 197 SER THR VAL ALA THR ASN CYS HIS LYS THR SER TRP LYS
SEQRES 6 A 197 VAL ASP GLN LEU GLN GLU GLY CYS SER TYR TYR PHE ARG
SEQRES 7 A 197 VAL LEU ALA GLU ASN GLU TYR GLY ILE GLY LEU PRO ALA
SEQRES 8 A 197 GLU THR ALA GLU SER VAL LYS ALA SER GLU ARG PRO LEU
SEQRES 9 A 197 PRO PRO GLY LYS ILE THR LEU MET ASP VAL THR ARG ASN
SEQRES 10 A 197 SER VAL SER LEU SER TRP GLU LYS PRO GLU HIS ASP GLY
SEQRES 11 A 197 GLY SER ARG ILE LEU GLY TYR ILE VAL GLU MET GLN THR
SEQRES 12 A 197 LYS GLY SER ASP LYS TRP ALA THR CYS ALA THR VAL LYS
SEQRES 13 A 197 VAL THR GLU ALA THR ILE THR GLY LEU ILE GLN GLY GLU
SEQRES 14 A 197 GLU TYR SER PHE ARG VAL SER ALA GLN ASN GLU LYS GLY
SEQRES 15 A 197 ILE SER ASP PRO ARG GLN LEU SER VAL PRO VAL ILE ALA
SEQRES 16 A 197 LYS ASP
SEQRES 1 B 197 GLY ALA MET ASP THR PRO GLY PRO PRO GLN ASP LEU LYS
SEQRES 2 B 197 VAL LYS GLU VAL THR LYS THR SER VAL THR LEU THR TRP
SEQRES 3 B 197 ASP PRO PRO LEU LEU ASP GLY GLY SER LYS ILE LYS ASN
SEQRES 4 B 197 TYR ILE VAL GLU LYS ARG GLU SER THR ARG LYS ALA TYR
SEQRES 5 B 197 SER THR VAL ALA THR ASN CYS HIS LYS THR SER TRP LYS
SEQRES 6 B 197 VAL ASP GLN LEU GLN GLU GLY CYS SER TYR TYR PHE ARG
SEQRES 7 B 197 VAL LEU ALA GLU ASN GLU TYR GLY ILE GLY LEU PRO ALA
SEQRES 8 B 197 GLU THR ALA GLU SER VAL LYS ALA SER GLU ARG PRO LEU
SEQRES 9 B 197 PRO PRO GLY LYS ILE THR LEU MET ASP VAL THR ARG ASN
SEQRES 10 B 197 SER VAL SER LEU SER TRP GLU LYS PRO GLU HIS ASP GLY
SEQRES 11 B 197 GLY SER ARG ILE LEU GLY TYR ILE VAL GLU MET GLN THR
SEQRES 12 B 197 LYS GLY SER ASP LYS TRP ALA THR CYS ALA THR VAL LYS
SEQRES 13 B 197 VAL THR GLU ALA THR ILE THR GLY LEU ILE GLN GLY GLU
SEQRES 14 B 197 GLU TYR SER PHE ARG VAL SER ALA GLN ASN GLU LYS GLY
SEQRES 15 B 197 ILE SER ASP PRO ARG GLN LEU SER VAL PRO VAL ILE ALA
SEQRES 16 B 197 LYS ASP
HET MPD A 394 8
HET MRD A 395 8
HET MPD B 393 8
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM MRD (4R)-2-METHYLPENTANE-2,4-DIOL
FORMUL 3 MPD 2(C6 H14 O2)
FORMUL 4 MRD C6 H14 O2
FORMUL 6 HOH *695(H2 O)
SHEET 1 A 3 GLN A 10 VAL A 17 0
SHEET 2 A 3 VAL A 22 ASP A 27 -1 O THR A 23 N LYS A 15
SHEET 3 A 3 SER A 63 VAL A 66 -1 O VAL A 66 N VAL A 22
SHEET 1 B 4 SER A 53 CYS A 59 0
SHEET 2 B 4 ASN A 39 GLU A 46 -1 N VAL A 42 O VAL A 55
SHEET 3 B 4 SER A 74 ASN A 83 -1 O ARG A 78 N GLU A 43
SHEET 4 B 4 ALA A 91 GLU A 92 -1 O ALA A 91 N VAL A 79
SHEET 1 C 3 GLY A 86 ILE A 87 0
SHEET 2 C 3 SER A 74 ASN A 83 -1 N ASN A 83 O GLY A 86
SHEET 3 C 3 VAL A 97 LYS A 98 -1 O VAL A 97 N TYR A 75
SHEET 1 D 3 ILE A 109 VAL A 114 0
SHEET 2 D 3 VAL A 119 TRP A 123 -1 O SER A 122 N THR A 110
SHEET 3 D 3 GLU A 159 ILE A 162 -1 O ALA A 160 N LEU A 121
SHEET 1 E 4 ALA A 150 VAL A 155 0
SHEET 2 E 4 GLY A 136 THR A 143 -1 N TYR A 137 O VAL A 155
SHEET 3 E 4 GLU A 170 ASN A 179 -1 O ARG A 174 N GLU A 140
SHEET 4 E 4 ARG A 187 GLN A 188 -1 O ARG A 187 N VAL A 175
SHEET 1 F 3 GLY A 182 ILE A 183 0
SHEET 2 F 3 GLU A 170 ASN A 179 -1 N ASN A 179 O GLY A 182
SHEET 3 F 3 VAL A 193 ILE A 194 -1 O VAL A 193 N TYR A 171
SHEET 1 G 3 GLN B 10 VAL B 17 0
SHEET 2 G 3 VAL B 22 ASP B 27 -1 O THR B 23 N LYS B 15
SHEET 3 G 3 SER B 63 VAL B 66 -1 O TRP B 64 N LEU B 24
SHEET 1 H 4 SER B 53 CYS B 59 0
SHEET 2 H 4 ASN B 39 GLU B 46 -1 N VAL B 42 O VAL B 55
SHEET 3 H 4 SER B 74 ASN B 83 -1 O LEU B 80 N ILE B 41
SHEET 4 H 4 ALA B 91 GLU B 92 -1 O ALA B 91 N VAL B 79
SHEET 1 I 3 GLY B 86 ILE B 87 0
SHEET 2 I 3 SER B 74 ASN B 83 -1 N ASN B 83 O GLY B 86
SHEET 3 I 3 VAL B 97 LYS B 98 -1 O VAL B 97 N TYR B 75
SHEET 1 J 3 THR B 110 THR B 115 0
SHEET 2 J 3 SER B 118 SER B 122 -1 O SER B 122 N THR B 110
SHEET 3 J 3 GLU B 159 ILE B 162 -1 O ILE B 162 N VAL B 119
SHEET 1 K 4 ALA B 150 VAL B 155 0
SHEET 2 K 4 GLY B 136 THR B 143 -1 N TYR B 137 O VAL B 155
SHEET 3 K 4 GLU B 170 ASN B 179 -1 O ARG B 174 N GLU B 140
SHEET 4 K 4 ARG B 187 GLN B 188 -1 O ARG B 187 N VAL B 175
SHEET 1 L 3 GLY B 182 ILE B 183 0
SHEET 2 L 3 GLU B 170 ASN B 179 -1 N ASN B 179 O GLY B 182
SHEET 3 L 3 VAL B 193 ILE B 194 -1 O VAL B 193 N TYR B 171
SITE 1 AC1 7 GLU A 92 THR A 93 ALA A 94 HOH A 321
SITE 2 AC1 7 HOH A 487 ARG B 45 LYS B 50
SITE 1 AC2 8 ILE A 37 LYS A 38 TYR A 40 HIS A 60
SITE 2 AC2 8 GLY A 145 HOH A 428 HOH A 495 HOH A 552
SITE 1 AC3 7 ILE B 37 LYS B 38 TYR B 40 HIS B 60
SITE 2 AC3 7 THR B 62 LYS B 144 GLY B 145
CRYST1 115.900 163.200 65.200 90.00 90.00 90.00 C 2 2 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 0.008628 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006127 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015337 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
