HEADER PROTEIN BINDING 27-JUN-14 4TVQ
TITLE CCM3 IN COMPLEX WITH CCM2 LD-LIKE MOTIF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CEREBRAL CAVERNOUS MALFORMATIONS 3 PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: PROGRAMMED CELL DEATH PROTEIN 10 TF-1 CELL APOPTOSIS-RELATED
COMPND 5 PROTEIN 15;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CEREBRAL CAVERNOUS MALFORMATIONS 2 PROTEIN;
COMPND 9 CHAIN: E;
COMPND 10 FRAGMENT: INTERDOMAIN LINKER LD-LIKE MOTIF RESIDUES 224-239;
COMPND 11 SYNONYM: MALCAVERNIN;
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: PDCD10, CCM3, TFAR15;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET32;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606
KEYWDS FAT-HOMOLOGY DOMAIN, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR X.LI,R.ZHANG,O.S.FISHER,T.J.BOGGON
REVDAT 5 27-SEP-23 4TVQ 1 REMARK
REVDAT 4 18-DEC-19 4TVQ 1 REMARK
REVDAT 3 20-SEP-17 4TVQ 1 REMARK
REVDAT 2 21-OCT-15 4TVQ 1 JRNL REMARK
REVDAT 1 25-MAR-15 4TVQ 0
JRNL AUTH K.M.DRAHEIM,X.LI,R.ZHANG,O.S.FISHER,G.VILLARI,T.J.BOGGON,
JRNL AUTH 2 D.A.CALDERWOOD
JRNL TITL CCM2-CCM3 INTERACTION STABILIZES THEIR PROTEIN EXPRESSION
JRNL TITL 2 AND PERMITS ENDOTHELIAL NETWORK FORMATION.
JRNL REF J.CELL BIOL. V. 208 987 2015
JRNL REFN ESSN 1540-8140
JRNL PMID 25825518
JRNL DOI 10.1083/JCB.201407129
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 21136
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.241
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 1076
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 49.4952 - 5.6011 1.00 2695 143 0.2465 0.2587
REMARK 3 2 5.6011 - 4.4467 1.00 2560 152 0.2351 0.2877
REMARK 3 3 4.4467 - 3.8848 1.00 2556 121 0.2226 0.2464
REMARK 3 4 3.8848 - 3.5297 1.00 2530 127 0.2319 0.2818
REMARK 3 5 3.5297 - 3.2768 0.99 2489 131 0.2445 0.2953
REMARK 3 6 3.2768 - 3.0836 0.98 2437 133 0.2444 0.3120
REMARK 3 7 3.0836 - 2.9292 0.98 2441 142 0.2663 0.3287
REMARK 3 8 2.9292 - 2.8000 0.95 2352 127 0.2556 0.3015
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.830
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 78.96
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 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 : 0.002 6050
REMARK 3 ANGLE : 0.583 8124
REMARK 3 CHIRALITY : 0.041 945
REMARK 3 PLANARITY : 0.003 1026
REMARK 3 DIHEDRAL : 10.927 2336
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 17 THROUGH 69 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.0787 -4.9489 -35.9601
REMARK 3 T TENSOR
REMARK 3 T11: 0.3304 T22: 0.4495
REMARK 3 T33: 0.5854 T12: 0.0142
REMARK 3 T13: 0.0922 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 4.1557 L22: 4.0061
REMARK 3 L33: 2.5442 L12: 0.2455
REMARK 3 L13: -0.3519 L23: -1.4653
REMARK 3 S TENSOR
REMARK 3 S11: 0.0357 S12: 0.1174 S13: 0.8639
REMARK 3 S21: 0.5111 S22: 0.2770 S23: 0.4385
REMARK 3 S31: -0.0179 S32: -0.1683 S33: -0.3130
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 70 THROUGH 207 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.6286 -10.5976 -15.9201
REMARK 3 T TENSOR
REMARK 3 T11: 0.5363 T22: 0.6428
REMARK 3 T33: 0.3185 T12: -0.1469
REMARK 3 T13: 0.0509 T23: 0.1070
REMARK 3 L TENSOR
REMARK 3 L11: 2.2165 L22: 1.6950
REMARK 3 L33: 2.5484 L12: -0.2158
REMARK 3 L13: 0.1688 L23: -0.0140
REMARK 3 S TENSOR
REMARK 3 S11: 0.3748 S12: -0.9300 S13: -0.3675
REMARK 3 S21: 0.2987 S22: -0.1807 S23: -0.0472
REMARK 3 S31: -0.6261 S32: -0.1518 S33: -0.1462
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 12 THROUGH 69 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.1542 -1.0011 -37.1491
REMARK 3 T TENSOR
REMARK 3 T11: 0.2854 T22: 0.4385
REMARK 3 T33: 0.4972 T12: 0.0990
REMARK 3 T13: 0.0949 T23: 0.0549
REMARK 3 L TENSOR
REMARK 3 L11: 3.3564 L22: 4.4947
REMARK 3 L33: 3.4557 L12: 0.6656
REMARK 3 L13: -0.4366 L23: -0.6635
REMARK 3 S TENSOR
REMARK 3 S11: 0.1650 S12: 0.4131 S13: 0.4901
REMARK 3 S21: -0.4252 S22: 0.2737 S23: 0.4493
REMARK 3 S31: -0.3523 S32: -0.4042 S33: -0.1789
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 70 THROUGH 209 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4132 -30.5244 -47.8668
REMARK 3 T TENSOR
REMARK 3 T11: 0.6243 T22: 0.3782
REMARK 3 T33: 0.7037 T12: -0.0867
REMARK 3 T13: 0.0228 T23: -0.1832
REMARK 3 L TENSOR
REMARK 3 L11: 0.8376 L22: 3.1947
REMARK 3 L33: 3.8551 L12: -0.1013
REMARK 3 L13: -1.0740 L23: 3.2738
REMARK 3 S TENSOR
REMARK 3 S11: -0.0777 S12: 0.0320 S13: -0.4007
REMARK 3 S21: -0.5134 S22: 0.6005 S23: -0.5811
REMARK 3 S31: -0.2369 S32: 0.5455 S33: -0.1577
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 69 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.4248 -7.0251 -25.5012
REMARK 3 T TENSOR
REMARK 3 T11: 0.2635 T22: 0.3909
REMARK 3 T33: 0.4591 T12: -0.0774
REMARK 3 T13: -0.0085 T23: -0.0374
REMARK 3 L TENSOR
REMARK 3 L11: 3.3093 L22: 2.9172
REMARK 3 L33: 1.9469 L12: -1.0008
REMARK 3 L13: -0.6507 L23: 0.8885
REMARK 3 S TENSOR
REMARK 3 S11: 0.2249 S12: -0.1134 S13: 0.7330
REMARK 3 S21: 0.3476 S22: -0.0775 S23: -0.5709
REMARK 3 S31: 0.0328 S32: 0.3363 S33: 0.0031
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 70 THROUGH 210 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.0137 5.8678 -52.0921
REMARK 3 T TENSOR
REMARK 3 T11: 0.3893 T22: 0.4022
REMARK 3 T33: 0.0974 T12: -0.0325
REMARK 3 T13: 0.0329 T23: -0.0563
REMARK 3 L TENSOR
REMARK 3 L11: 0.8846 L22: 3.4564
REMARK 3 L33: 3.8986 L12: 0.9046
REMARK 3 L13: -0.1845 L23: -1.8473
REMARK 3 S TENSOR
REMARK 3 S11: -0.0730 S12: 0.2013 S13: -0.1664
REMARK 3 S21: -0.1187 S22: 0.2209 S23: 0.3831
REMARK 3 S31: -0.5630 S32: 0.2245 S33: 0.0068
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 15 THROUGH 69 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.4006 -4.9048 -24.9562
REMARK 3 T TENSOR
REMARK 3 T11: 0.2895 T22: 0.3476
REMARK 3 T33: 0.3195 T12: -0.1009
REMARK 3 T13: 0.0143 T23: 0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 2.4756 L22: 3.4067
REMARK 3 L33: 2.8032 L12: -1.2736
REMARK 3 L13: 1.2224 L23: 1.8785
REMARK 3 S TENSOR
REMARK 3 S11: 0.0591 S12: 0.0546 S13: 0.0058
REMARK 3 S21: 0.4028 S22: -0.2542 S23: -0.0751
REMARK 3 S31: 0.1836 S32: 0.1339 S33: 0.2223
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 70 THROUGH 210 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.6128 -33.6724 -24.4606
REMARK 3 T TENSOR
REMARK 3 T11: 0.3685 T22: 0.1642
REMARK 3 T33: 0.5120 T12: -0.0216
REMARK 3 T13: -0.1657 T23: -0.0364
REMARK 3 L TENSOR
REMARK 3 L11: 3.7852 L22: 5.2082
REMARK 3 L33: 5.2356 L12: -0.3434
REMARK 3 L13: -1.9244 L23: 1.5746
REMARK 3 S TENSOR
REMARK 3 S11: 0.0251 S12: -0.1810 S13: -0.0890
REMARK 3 S21: 0.3624 S22: 0.2953 S23: -0.1960
REMARK 3 S31: 0.8330 S32: -0.0527 S33: -0.1510
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 224 THROUGH 239 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.9361 1.5475 -65.2750
REMARK 3 T TENSOR
REMARK 3 T11: 0.6634 T22: 0.6592
REMARK 3 T33: 0.4068 T12: 0.0925
REMARK 3 T13: 0.2011 T23: -0.0270
REMARK 3 L TENSOR
REMARK 3 L11: 5.1286 L22: 2.5718
REMARK 3 L33: 0.9692 L12: -0.4481
REMARK 3 L13: 2.1273 L23: 0.2644
REMARK 3 S TENSOR
REMARK 3 S11: 0.4277 S12: 0.0470 S13: -0.5513
REMARK 3 S21: -0.7598 S22: 0.0320 S23: -0.1879
REMARK 3 S31: -1.0382 S32: -0.5842 S33: 0.1760
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 4TVQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000202320.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 100
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 : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1000
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR +
REMARK 200 SAGITTALLY-FOCUSING SECOND
REMARK 200 CRYSTAL + MIRROR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 2000.0.98.705A
REMARK 200 DATA SCALING SOFTWARE : HKL-2000 2000.0.98.705A
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 130452
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : 0.10700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : 0.93700
REMARK 200 R SYM FOR SHELL (I) : 0.93700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.654
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER CCP4-6.4.0
REMARK 200 STARTING MODEL: PDB ENTRY 3L8I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-20% PEG3350, 0.1-0.2M POTASSIUM
REMARK 280 FLUORIDE, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 30.92750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.01700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.77600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.01700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.92750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.77600
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: 3950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ARG A 2
REMARK 465 MET A 3
REMARK 465 THR A 4
REMARK 465 MET A 5
REMARK 465 GLU A 6
REMARK 465 GLU A 7
REMARK 465 MET A 8
REMARK 465 LYS A 9
REMARK 465 ASN A 10
REMARK 465 GLU A 11
REMARK 465 ALA A 12
REMARK 465 GLU A 13
REMARK 465 THR A 14
REMARK 465 THR A 15
REMARK 465 SER A 16
REMARK 465 ASP A 87
REMARK 465 VAL A 88
REMARK 465 GLU A 89
REMARK 465 GLU A 90
REMARK 465 TYR A 91
REMARK 465 MET A 92
REMARK 465 ILE A 93
REMARK 465 GLU A 94
REMARK 465 ARG A 95
REMARK 465 PRO A 96
REMARK 465 GLU A 97
REMARK 465 PRO A 98
REMARK 465 GLU A 99
REMARK 465 PHE A 100
REMARK 465 GLN A 101
REMARK 465 ASP A 102
REMARK 465 LEU A 103
REMARK 465 ASN A 104
REMARK 465 GLU A 105
REMARK 465 LYS A 106
REMARK 465 ALA A 107
REMARK 465 ILE A 134
REMARK 465 ALA A 135
REMARK 465 SER A 136
REMARK 465 ALA A 137
REMARK 465 ILE A 138
REMARK 465 LYS A 139
REMARK 465 GLU A 140
REMARK 465 LEU A 141
REMARK 465 LEU A 142
REMARK 465 ASP A 143
REMARK 465 THR A 144
REMARK 465 VAL A 145
REMARK 465 ASN A 146
REMARK 465 ASN A 147
REMARK 465 VAL A 148
REMARK 465 PHE A 149
REMARK 465 LYS A 150
REMARK 465 LYS A 151
REMARK 465 TYR A 152
REMARK 465 GLN A 153
REMARK 465 TYR A 154
REMARK 465 GLN A 155
REMARK 465 ASN A 156
REMARK 465 ARG A 157
REMARK 465 ARG A 158
REMARK 465 ALA A 159
REMARK 465 LEU A 160
REMARK 465 GLU A 161
REMARK 465 HIS A 162
REMARK 465 GLN A 163
REMARK 465 LYS A 164
REMARK 465 LYS A 165
REMARK 465 PHE A 208
REMARK 465 LYS A 209
REMARK 465 THR A 210
REMARK 465 VAL A 211
REMARK 465 ALA A 212
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 MET B 3
REMARK 465 THR B 4
REMARK 465 MET B 5
REMARK 465 GLU B 6
REMARK 465 GLU B 7
REMARK 465 MET B 8
REMARK 465 LYS B 9
REMARK 465 ASN B 10
REMARK 465 GLU B 11
REMARK 465 GLU B 94
REMARK 465 ARG B 95
REMARK 465 LYS B 150
REMARK 465 LYS B 151
REMARK 465 TYR B 152
REMARK 465 GLN B 153
REMARK 465 TYR B 154
REMARK 465 GLN B 155
REMARK 465 ASN B 156
REMARK 465 ARG B 157
REMARK 465 ARG B 158
REMARK 465 ALA B 159
REMARK 465 LEU B 160
REMARK 465 THR B 210
REMARK 465 VAL B 211
REMARK 465 ALA B 212
REMARK 465 GLY C -1
REMARK 465 HIS C 0
REMARK 465 ASP C 87
REMARK 465 VAL C 88
REMARK 465 GLU C 89
REMARK 465 TYR C 154
REMARK 465 GLN C 155
REMARK 465 VAL C 211
REMARK 465 ALA C 212
REMARK 465 GLY D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 ARG D 2
REMARK 465 MET D 3
REMARK 465 THR D 4
REMARK 465 MET D 5
REMARK 465 GLU D 6
REMARK 465 GLU D 7
REMARK 465 MET D 8
REMARK 465 LYS D 9
REMARK 465 ASN D 10
REMARK 465 GLU D 11
REMARK 465 ALA D 12
REMARK 465 GLU D 13
REMARK 465 THR D 14
REMARK 465 VAL D 88
REMARK 465 GLU D 89
REMARK 465 GLU D 90
REMARK 465 GLN D 155
REMARK 465 ASN D 156
REMARK 465 VAL D 211
REMARK 465 ALA D 212
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 LYS A 69 33.02 -89.03
REMARK 500 VAL B 25 -51.15 -121.86
REMARK 500 ASP B 184 -78.53 -67.92
REMARK 500 LYS C 69 41.48 -95.01
REMARK 500 ALA C 84 4.87 -63.85
REMARK 500 PRO C 96 58.31 -90.76
REMARK 500 TYR C 152 -86.67 -146.90
REMARK 500 VAL D 36 -58.98 -121.50
REMARK 500 TYR D 152 -27.23 -140.03
REMARK 500 GLN D 153 82.34 53.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3L8I RELATED DB: PDB
REMARK 900 CCM3
REMARK 900 RELATED ID: 3L8J RELATED DB: PDB
REMARK 900 CCM3
REMARK 900 RELATED ID: 3RQE RELATED DB: PDB
REMARK 900 CCM3 WITH PAXILLIN LD1
REMARK 900 RELATED ID: 3RQF RELATED DB: PDB
REMARK 900 CCM3 WITH PAXILLIN LD2
REMARK 900 RELATED ID: 3RQG RELATED DB: PDB
REMARK 900 CCM3 WITH PAXILLIN LD4
DBREF 4TVQ A 1 212 UNP Q9BUL8 PDC10_HUMAN 1 212
DBREF 4TVQ B 1 212 UNP Q9BUL8 PDC10_HUMAN 1 212
DBREF 4TVQ C 1 212 UNP Q9BUL8 PDC10_HUMAN 1 212
DBREF 4TVQ D 1 212 UNP Q9BUL8 PDC10_HUMAN 1 212
DBREF 4TVQ E 224 239 UNP Q9BSQ5 CCM2_HUMAN 224 239
SEQADV 4TVQ GLY A -1 UNP Q9BUL8 EXPRESSION TAG
SEQADV 4TVQ HIS A 0 UNP Q9BUL8 EXPRESSION TAG
SEQADV 4TVQ GLY B -1 UNP Q9BUL8 EXPRESSION TAG
SEQADV 4TVQ HIS B 0 UNP Q9BUL8 EXPRESSION TAG
SEQADV 4TVQ GLY C -1 UNP Q9BUL8 EXPRESSION TAG
SEQADV 4TVQ HIS C 0 UNP Q9BUL8 EXPRESSION TAG
SEQADV 4TVQ GLY D -1 UNP Q9BUL8 EXPRESSION TAG
SEQADV 4TVQ HIS D 0 UNP Q9BUL8 EXPRESSION TAG
SEQRES 1 A 214 GLY HIS MET ARG MET THR MET GLU GLU MET LYS ASN GLU
SEQRES 2 A 214 ALA GLU THR THR SER MET VAL SER MET PRO LEU TYR ALA
SEQRES 3 A 214 VAL MET TYR PRO VAL PHE ASN GLU LEU GLU ARG VAL ASN
SEQRES 4 A 214 LEU SER ALA ALA GLN THR LEU ARG ALA ALA PHE ILE LYS
SEQRES 5 A 214 ALA GLU LYS GLU ASN PRO GLY LEU THR GLN ASP ILE ILE
SEQRES 6 A 214 MET LYS ILE LEU GLU LYS LYS SER VAL GLU VAL ASN PHE
SEQRES 7 A 214 THR GLU SER LEU LEU ARG MET ALA ALA ASP ASP VAL GLU
SEQRES 8 A 214 GLU TYR MET ILE GLU ARG PRO GLU PRO GLU PHE GLN ASP
SEQRES 9 A 214 LEU ASN GLU LYS ALA ARG ALA LEU LYS GLN ILE LEU SER
SEQRES 10 A 214 LYS ILE PRO ASP GLU ILE ASN ASP ARG VAL ARG PHE LEU
SEQRES 11 A 214 GLN THR ILE LYS ASP ILE ALA SER ALA ILE LYS GLU LEU
SEQRES 12 A 214 LEU ASP THR VAL ASN ASN VAL PHE LYS LYS TYR GLN TYR
SEQRES 13 A 214 GLN ASN ARG ARG ALA LEU GLU HIS GLN LYS LYS GLU PHE
SEQRES 14 A 214 VAL LYS TYR SER LYS SER PHE SER ASP THR LEU LYS THR
SEQRES 15 A 214 TYR PHE LYS ASP GLY LYS ALA ILE ASN VAL PHE VAL SER
SEQRES 16 A 214 ALA ASN ARG LEU ILE HIS GLN THR ASN LEU ILE LEU GLN
SEQRES 17 A 214 THR PHE LYS THR VAL ALA
SEQRES 1 B 214 GLY HIS MET ARG MET THR MET GLU GLU MET LYS ASN GLU
SEQRES 2 B 214 ALA GLU THR THR SER MET VAL SER MET PRO LEU TYR ALA
SEQRES 3 B 214 VAL MET TYR PRO VAL PHE ASN GLU LEU GLU ARG VAL ASN
SEQRES 4 B 214 LEU SER ALA ALA GLN THR LEU ARG ALA ALA PHE ILE LYS
SEQRES 5 B 214 ALA GLU LYS GLU ASN PRO GLY LEU THR GLN ASP ILE ILE
SEQRES 6 B 214 MET LYS ILE LEU GLU LYS LYS SER VAL GLU VAL ASN PHE
SEQRES 7 B 214 THR GLU SER LEU LEU ARG MET ALA ALA ASP ASP VAL GLU
SEQRES 8 B 214 GLU TYR MET ILE GLU ARG PRO GLU PRO GLU PHE GLN ASP
SEQRES 9 B 214 LEU ASN GLU LYS ALA ARG ALA LEU LYS GLN ILE LEU SER
SEQRES 10 B 214 LYS ILE PRO ASP GLU ILE ASN ASP ARG VAL ARG PHE LEU
SEQRES 11 B 214 GLN THR ILE LYS ASP ILE ALA SER ALA ILE LYS GLU LEU
SEQRES 12 B 214 LEU ASP THR VAL ASN ASN VAL PHE LYS LYS TYR GLN TYR
SEQRES 13 B 214 GLN ASN ARG ARG ALA LEU GLU HIS GLN LYS LYS GLU PHE
SEQRES 14 B 214 VAL LYS TYR SER LYS SER PHE SER ASP THR LEU LYS THR
SEQRES 15 B 214 TYR PHE LYS ASP GLY LYS ALA ILE ASN VAL PHE VAL SER
SEQRES 16 B 214 ALA ASN ARG LEU ILE HIS GLN THR ASN LEU ILE LEU GLN
SEQRES 17 B 214 THR PHE LYS THR VAL ALA
SEQRES 1 C 214 GLY HIS MET ARG MET THR MET GLU GLU MET LYS ASN GLU
SEQRES 2 C 214 ALA GLU THR THR SER MET VAL SER MET PRO LEU TYR ALA
SEQRES 3 C 214 VAL MET TYR PRO VAL PHE ASN GLU LEU GLU ARG VAL ASN
SEQRES 4 C 214 LEU SER ALA ALA GLN THR LEU ARG ALA ALA PHE ILE LYS
SEQRES 5 C 214 ALA GLU LYS GLU ASN PRO GLY LEU THR GLN ASP ILE ILE
SEQRES 6 C 214 MET LYS ILE LEU GLU LYS LYS SER VAL GLU VAL ASN PHE
SEQRES 7 C 214 THR GLU SER LEU LEU ARG MET ALA ALA ASP ASP VAL GLU
SEQRES 8 C 214 GLU TYR MET ILE GLU ARG PRO GLU PRO GLU PHE GLN ASP
SEQRES 9 C 214 LEU ASN GLU LYS ALA ARG ALA LEU LYS GLN ILE LEU SER
SEQRES 10 C 214 LYS ILE PRO ASP GLU ILE ASN ASP ARG VAL ARG PHE LEU
SEQRES 11 C 214 GLN THR ILE LYS ASP ILE ALA SER ALA ILE LYS GLU LEU
SEQRES 12 C 214 LEU ASP THR VAL ASN ASN VAL PHE LYS LYS TYR GLN TYR
SEQRES 13 C 214 GLN ASN ARG ARG ALA LEU GLU HIS GLN LYS LYS GLU PHE
SEQRES 14 C 214 VAL LYS TYR SER LYS SER PHE SER ASP THR LEU LYS THR
SEQRES 15 C 214 TYR PHE LYS ASP GLY LYS ALA ILE ASN VAL PHE VAL SER
SEQRES 16 C 214 ALA ASN ARG LEU ILE HIS GLN THR ASN LEU ILE LEU GLN
SEQRES 17 C 214 THR PHE LYS THR VAL ALA
SEQRES 1 D 214 GLY HIS MET ARG MET THR MET GLU GLU MET LYS ASN GLU
SEQRES 2 D 214 ALA GLU THR THR SER MET VAL SER MET PRO LEU TYR ALA
SEQRES 3 D 214 VAL MET TYR PRO VAL PHE ASN GLU LEU GLU ARG VAL ASN
SEQRES 4 D 214 LEU SER ALA ALA GLN THR LEU ARG ALA ALA PHE ILE LYS
SEQRES 5 D 214 ALA GLU LYS GLU ASN PRO GLY LEU THR GLN ASP ILE ILE
SEQRES 6 D 214 MET LYS ILE LEU GLU LYS LYS SER VAL GLU VAL ASN PHE
SEQRES 7 D 214 THR GLU SER LEU LEU ARG MET ALA ALA ASP ASP VAL GLU
SEQRES 8 D 214 GLU TYR MET ILE GLU ARG PRO GLU PRO GLU PHE GLN ASP
SEQRES 9 D 214 LEU ASN GLU LYS ALA ARG ALA LEU LYS GLN ILE LEU SER
SEQRES 10 D 214 LYS ILE PRO ASP GLU ILE ASN ASP ARG VAL ARG PHE LEU
SEQRES 11 D 214 GLN THR ILE LYS ASP ILE ALA SER ALA ILE LYS GLU LEU
SEQRES 12 D 214 LEU ASP THR VAL ASN ASN VAL PHE LYS LYS TYR GLN TYR
SEQRES 13 D 214 GLN ASN ARG ARG ALA LEU GLU HIS GLN LYS LYS GLU PHE
SEQRES 14 D 214 VAL LYS TYR SER LYS SER PHE SER ASP THR LEU LYS THR
SEQRES 15 D 214 TYR PHE LYS ASP GLY LYS ALA ILE ASN VAL PHE VAL SER
SEQRES 16 D 214 ALA ASN ARG LEU ILE HIS GLN THR ASN LEU ILE LEU GLN
SEQRES 17 D 214 THR PHE LYS THR VAL ALA
SEQRES 1 E 16 SER THR ILE ASP PHE LEU ASP ARG ALA ILE PHE ASP GLY
SEQRES 2 E 16 ALA SER THR
HELIX 1 AA1 SER A 19 VAL A 25 1 7
HELIX 2 AA2 VAL A 25 GLU A 32 1 8
HELIX 3 AA3 LEU A 38 ASN A 55 1 18
HELIX 4 AA4 GLY A 57 LYS A 69 1 13
HELIX 5 AA5 LYS A 69 ALA A 84 1 16
HELIX 6 AA6 ALA A 109 LYS A 116 1 8
HELIX 7 AA7 LYS A 116 ILE A 121 1 6
HELIX 8 AA8 ASP A 123 ASP A 133 1 11
HELIX 9 AA9 PHE A 167 GLY A 185 1 19
HELIX 10 AB1 LYS A 186 THR A 207 1 22
HELIX 11 AB2 SER B 16 VAL B 18 5 3
HELIX 12 AB3 SER B 19 VAL B 25 1 7
HELIX 13 AB4 VAL B 25 ASN B 37 1 13
HELIX 14 AB5 ASN B 37 ASN B 55 1 19
HELIX 15 AB6 GLY B 57 LYS B 69 1 13
HELIX 16 AB7 LYS B 69 ALA B 84 1 16
HELIX 17 AB8 ALA B 85 ASP B 87 5 3
HELIX 18 AB9 GLU B 97 SER B 115 1 19
HELIX 19 AC1 LYS B 116 ILE B 121 1 6
HELIX 20 AC2 ASP B 123 PHE B 149 1 27
HELIX 21 AC3 HIS B 162 ASP B 184 1 23
HELIX 22 AC4 LYS B 186 LYS B 209 1 24
HELIX 23 AC5 THR C 4 GLU C 13 1 10
HELIX 24 AC6 SER C 16 VAL C 18 5 3
HELIX 25 AC7 SER C 19 VAL C 25 1 7
HELIX 26 AC8 VAL C 25 GLU C 34 1 10
HELIX 27 AC9 ASN C 37 ASN C 55 1 19
HELIX 28 AD1 GLY C 57 LYS C 69 1 13
HELIX 29 AD2 LYS C 69 ALA C 84 1 16
HELIX 30 AD3 GLU C 97 SER C 115 1 19
HELIX 31 AD4 LYS C 116 GLU C 120 5 5
HELIX 32 AD5 ASP C 123 PHE C 149 1 27
HELIX 33 AD6 ARG C 158 GLY C 185 1 28
HELIX 34 AD7 LYS C 186 THR C 210 1 25
HELIX 35 AD8 SER D 16 VAL D 18 5 3
HELIX 36 AD9 SER D 19 VAL D 25 1 7
HELIX 37 AE1 VAL D 25 GLU D 34 1 10
HELIX 38 AE2 ASN D 37 ASN D 55 1 19
HELIX 39 AE3 GLY D 57 GLU D 68 1 12
HELIX 40 AE4 LYS D 69 MET D 83 1 15
HELIX 41 AE5 ALA D 84 ASP D 86 5 3
HELIX 42 AE6 GLU D 97 LYS D 116 1 20
HELIX 43 AE7 LYS D 116 ILE D 121 1 6
HELIX 44 AE8 ASP D 123 PHE D 149 1 27
HELIX 45 AE9 ARG D 158 GLY D 185 1 28
HELIX 46 AF1 LYS D 186 THR D 210 1 25
HELIX 47 AF2 THR E 225 THR E 239 1 15
CRYST1 61.855 113.552 120.034 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 0.016167 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008807 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008331 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
