HEADER SIGNALING PROTEIN 29-JAN-13 4IYP
TITLE STRUCTURE OF THE NPP2AC-ALPHA4 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMMUNOGLOBULIN-BINDING PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: B-CELL SIGNAL TRANSDUCTION MOLECULE ALPHA 4, PROTEIN ALPHA-
COMPND 5 4, CD79A-BINDING PROTEIN 1, PROTEIN PHOSPHATASE 2/4/6 REGULATORY
COMPND 6 SUBUNIT, RENAL CARCINOMA ANTIGEN NY-REN-16;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE 2A CATALYTIC SUBUNIT
COMPND 10 ALPHA ISOFORM;
COMPND 11 CHAIN: C;
COMPND 12 SYNONYM: PP2A-ALPHA, REPLICATION PROTEIN C, RP-C;
COMPND 13 EC: 3.1.3.16;
COMPND 14 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: ALPHA4, IBP1, IGBP1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PQLINK;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQLINK;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: PP2AC, PPP2C, PPP2CA;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: PP2A;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PQLINK;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PQLINK
KEYWDS ALPHA4, PP2A, LATENCY, HELIX MOTIF, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.JIANG,V.STANEVICH,K.A.SATYSHUR,Y.XING
REVDAT 3 15-NOV-17 4IYP 1 REMARK
REVDAT 2 29-MAY-13 4IYP 1 JRNL
REVDAT 1 17-APR-13 4IYP 0
JRNL AUTH L.JIANG,V.STANEVICH,K.A.SATYSHUR,M.KONG,G.R.WATKINS,
JRNL AUTH 2 B.E.WADZINSKI,R.SENGUPTA,Y.XING
JRNL TITL STRUCTURAL BASIS OF PROTEIN PHOSPHATASE 2A STABLE LATENCY.
JRNL REF NAT COMMUN V. 4 1699 2013
JRNL REFN ESSN 2041-1723
JRNL PMID 23591866
JRNL DOI 10.1038/NCOMMS2663
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) : 34.43
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.610
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 15885
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 796
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 34.4310 - 5.0774 0.99 2622 127 0.1841 0.1856
REMARK 3 2 5.0774 - 4.0321 1.00 2542 117 0.1492 0.2196
REMARK 3 3 4.0321 - 3.5230 1.00 2516 124 0.1661 0.2064
REMARK 3 4 3.5230 - 3.2011 1.00 2494 143 0.1944 0.2474
REMARK 3 5 3.2011 - 2.9718 1.00 2464 144 0.2178 0.2872
REMARK 3 6 2.9718 - 2.7967 0.99 2451 141 0.2449 0.3225
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) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.590
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) : 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 : 0.009 2715
REMARK 3 ANGLE : 1.207 3648
REMARK 3 CHIRALITY : 0.079 403
REMARK 3 PLANARITY : 0.005 467
REMARK 3 DIHEDRAL : 18.266 1035
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 0:28)
REMARK 3 ORIGIN FOR THE GROUP (A): 72.1813 -6.4288 -19.3837
REMARK 3 T TENSOR
REMARK 3 T11: 0.6265 T22: 0.7445
REMARK 3 T33: 0.6403 T12: -0.0321
REMARK 3 T13: -0.1058 T23: -0.0652
REMARK 3 L TENSOR
REMARK 3 L11: 4.4692 L22: 4.8414
REMARK 3 L33: 5.4764 L12: -0.8326
REMARK 3 L13: -0.8991 L23: -0.5385
REMARK 3 S TENSOR
REMARK 3 S11: 0.4764 S12: -0.7370 S13: -0.5738
REMARK 3 S21: 0.9037 S22: -0.6941 S23: -1.5646
REMARK 3 S31: 0.2213 S32: 0.4425 S33: -0.1403
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 29:72)
REMARK 3 ORIGIN FOR THE GROUP (A): 64.9580 -11.4909 -24.7391
REMARK 3 T TENSOR
REMARK 3 T11: 0.4168 T22: 0.4092
REMARK 3 T33: 0.4610 T12: -0.0970
REMARK 3 T13: -0.1204 T23: -0.0291
REMARK 3 L TENSOR
REMARK 3 L11: 7.8738 L22: 7.0905
REMARK 3 L33: 5.1890 L12: -0.4268
REMARK 3 L13: -0.9339 L23: -0.5925
REMARK 3 S TENSOR
REMARK 3 S11: 0.6717 S12: 0.1245 S13: 0.9635
REMARK 3 S21: -0.0078 S22: -0.3357 S23: -0.5172
REMARK 3 S31: -1.1327 S32: -0.2429 S33: -0.2711
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 73:154)
REMARK 3 ORIGIN FOR THE GROUP (A): 55.2101 -16.2999 -29.7107
REMARK 3 T TENSOR
REMARK 3 T11: 0.4451 T22: 0.3647
REMARK 3 T33: 0.4045 T12: -0.0411
REMARK 3 T13: 0.0058 T23: 0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 8.2236 L22: 3.9742
REMARK 3 L33: 5.8002 L12: -1.5319
REMARK 3 L13: -1.3652 L23: 1.5963
REMARK 3 S TENSOR
REMARK 3 S11: 0.3764 S12: 0.0621 S13: 0.2543
REMARK 3 S21: -0.3219 S22: -0.4080 S23: 0.2734
REMARK 3 S31: -0.3037 S32: -0.4131 S33: -0.0168
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 155:180)
REMARK 3 ORIGIN FOR THE GROUP (A): 58.6864 -32.8752 -21.0238
REMARK 3 T TENSOR
REMARK 3 T11: 0.5637 T22: 0.5494
REMARK 3 T33: 0.5502 T12: -0.0322
REMARK 3 T13: -0.0376 T23: 0.0424
REMARK 3 L TENSOR
REMARK 3 L11: 5.2452 L22: 8.1459
REMARK 3 L33: 4.1088 L12: 2.1115
REMARK 3 L13: 4.4850 L23: 2.2867
REMARK 3 S TENSOR
REMARK 3 S11: 0.3998 S12: 0.3929 S13: 0.3219
REMARK 3 S21: -0.3794 S22: -0.5019 S23: 0.7526
REMARK 3 S31: 0.3850 S32: -0.0251 S33: 0.1293
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 181:221)
REMARK 3 ORIGIN FOR THE GROUP (A): 57.5126 -23.0830 -25.5446
REMARK 3 T TENSOR
REMARK 3 T11: 0.5104 T22: 0.3891
REMARK 3 T33: 0.3253 T12: -0.0177
REMARK 3 T13: 0.0452 T23: -0.0488
REMARK 3 L TENSOR
REMARK 3 L11: 3.6365 L22: 5.6731
REMARK 3 L33: 4.4630 L12: -0.7534
REMARK 3 L13: 2.5382 L23: -1.5906
REMARK 3 S TENSOR
REMARK 3 S11: 0.2747 S12: -0.6837 S13: -0.3845
REMARK 3 S21: -0.0651 S22: -0.1538 S23: 0.3749
REMARK 3 S31: 0.3051 S32: -0.3517 S33: -0.0558
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 6:64)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.3649 -29.3743 -5.4084
REMARK 3 T TENSOR
REMARK 3 T11: 0.6187 T22: 1.1513
REMARK 3 T33: 0.5521 T12: -0.2214
REMARK 3 T13: 0.0926 T23: 0.1371
REMARK 3 L TENSOR
REMARK 3 L11: 5.4314 L22: 7.0185
REMARK 3 L33: 5.8825 L12: 1.2183
REMARK 3 L13: 0.0545 L23: 0.0221
REMARK 3 S TENSOR
REMARK 3 S11: 0.3258 S12: -1.5977 S13: -0.1195
REMARK 3 S21: 1.2324 S22: -0.5034 S23: -0.6658
REMARK 3 S31: -0.3173 S32: 0.9198 S33: 0.1957
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 65:126)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.1864 -32.6750 -11.2736
REMARK 3 T TENSOR
REMARK 3 T11: 0.4803 T22: 0.9709
REMARK 3 T33: 0.6362 T12: -0.1946
REMARK 3 T13: 0.1697 T23: 0.1771
REMARK 3 L TENSOR
REMARK 3 L11: 5.9476 L22: 4.7243
REMARK 3 L33: 2.3474 L12: 5.3145
REMARK 3 L13: -1.5008 L23: -0.9613
REMARK 3 S TENSOR
REMARK 3 S11: 0.0956 S12: -0.9672 S13: -0.2686
REMARK 3 S21: 0.3537 S22: -0.1581 S23: -0.1377
REMARK 3 S31: 0.1762 S32: -0.1139 S33: 0.1452
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 127:153)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.1582 -18.5754 -15.9322
REMARK 3 T TENSOR
REMARK 3 T11: 0.5341 T22: 0.8212
REMARK 3 T33: 0.6723 T12: -0.0377
REMARK 3 T13: 0.1825 T23: -0.0627
REMARK 3 L TENSOR
REMARK 3 L11: 8.6805 L22: 5.2365
REMARK 3 L33: 4.3211 L12: -0.2288
REMARK 3 L13: -1.8949 L23: 3.6545
REMARK 3 S TENSOR
REMARK 3 S11: 0.6632 S12: -0.6421 S13: 0.7349
REMARK 3 S21: -0.2257 S22: -0.6850 S23: 1.1362
REMARK 3 S31: -0.8952 S32: -0.6069 S33: 0.0613
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 4IYP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1000077376.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15948
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.797
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 20.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.7000
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) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 10.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.54500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.220
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: CRANK
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12-15% PEG3350 (V/V), 0.3 M NA/K
REMARK 280 TARTRATE, PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.15333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.07667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 27.07667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 54.15333
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: DIMERIC
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 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 MSE A 151
REMARK 465 ALA A 152
REMARK 465 SER A 153
REMARK 465 ASP A 222
REMARK 465 SER A 223
REMARK 465 SER A 224
REMARK 465 ARG A 225
REMARK 465 GLU A 226
REMARK 465 ALA A 227
REMARK 465 SER A 228
REMARK 465 THR A 229
REMARK 465 SER A 230
REMARK 465 ASN A 231
REMARK 465 SER A 232
REMARK 465 SER A 233
REMARK 465 ARG A 234
REMARK 465 GLY C 3
REMARK 465 SER C 4
REMARK 465 MSE C 5
REMARK 465 SER C 43
REMARK 465 ASN C 44
REMARK 465 VAL C 45
REMARK 465 GLN C 46
REMARK 465 GLU C 47
REMARK 465 VAL C 48
REMARK 465 ARG C 49
REMARK 465 CYS C 50
REMARK 465 PRO C 51
REMARK 465 VAL C 52
REMARK 465 THR C 53
REMARK 465 VAL C 54
REMARK 465 VAL C 58
REMARK 465 HIS C 59
REMARK 465 ARG C 70
REMARK 465 ILE C 71
REMARK 465 GLY C 72
REMARK 465 GLY C 73
REMARK 465 LYS C 74
REMARK 465 SER C 75
REMARK 465 PRO C 76
REMARK 465 ARG C 89
REMARK 465 GLY C 90
REMARK 465 TYR C 91
REMARK 465 HIS C 118
REMARK 465 GLU C 119
REMARK 465 SER C 120
REMARK 465 ARG C 121
REMARK 465 GLN C 122
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 CYS C 55 SG
REMARK 470 ASP C 57 CG OD1 OD2
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 LEU A 7 CA - CB - CG ANGL. DEV. = 16.7 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 ASN A 65 54.47 -114.70
REMARK 500 ASN A 94 78.25 -179.00
REMARK 500 THR C 7 75.09 -118.25
REMARK 500 THR C 40 45.91 -82.14
REMARK 500 LYS C 41 -40.21 -134.96
REMARK 500 LEU C 68 97.51 67.50
REMARK 500 ASP C 85 -97.95 -76.50
REMARK 500 VAL C 87 -127.36 79.50
REMARK 500 ARG C 108 -131.06 57.02
REMARK 500 ASN C 139 -166.13 -175.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4I5L RELATED DB: PDB
REMARK 900 TRIMER COMPLEX INVOLVING A AND C.
REMARK 900 RELATED ID: 4I5N RELATED DB: PDB
REMARK 900 TRIMER COMPLEX INVOLVING A AND C.
DBREF 4IYP A 2 234 UNP P78318 IGBP1_HUMAN 2 234
DBREF 4IYP C 6 153 UNP P67775 PP2AA_HUMAN 6 153
SEQADV 4IYP GLY A -1 UNP P78318 EXPRESSION TAG
SEQADV 4IYP SER A 0 UNP P78318 EXPRESSION TAG
SEQADV 4IYP MSE A 1 UNP P78318 EXPRESSION TAG
SEQADV 4IYP A UNP P78318 LYS 128 DELETION
SEQADV 4IYP A UNP P78318 THR 129 DELETION
SEQADV 4IYP A UNP P78318 MET 130 DELETION
SEQADV 4IYP A UNP P78318 ASN 131 DELETION
SEQADV 4IYP A UNP P78318 ASN 132 DELETION
SEQADV 4IYP A UNP P78318 SER 133 DELETION
SEQADV 4IYP A UNP P78318 ALA 134 DELETION
SEQADV 4IYP A UNP P78318 GLU 135 DELETION
SEQADV 4IYP A UNP P78318 ASN 136 DELETION
SEQADV 4IYP A UNP P78318 HIS 137 DELETION
SEQADV 4IYP A UNP P78318 THR 138 DELETION
SEQADV 4IYP A UNP P78318 ALA 139 DELETION
SEQADV 4IYP A UNP P78318 ASN 140 DELETION
SEQADV 4IYP A UNP P78318 SER 141 DELETION
SEQADV 4IYP GLY C 3 UNP P67775 EXPRESSION TAG
SEQADV 4IYP SER C 4 UNP P67775 EXPRESSION TAG
SEQADV 4IYP MSE C 5 UNP P67775 EXPRESSION TAG
SEQRES 1 A 222 GLY SER MSE ALA ALA GLU ASP GLU LEU GLN LEU PRO ARG
SEQRES 2 A 222 LEU PRO GLU LEU PHE GLU THR GLY ARG GLN LEU LEU ASP
SEQRES 3 A 222 GLU VAL GLU VAL ALA THR GLU PRO ALA GLY SER ARG ILE
SEQRES 4 A 222 VAL GLN GLU LYS VAL PHE LYS GLY LEU ASP LEU LEU GLU
SEQRES 5 A 222 LYS ALA ALA GLU MSE LEU SER GLN LEU ASP LEU PHE SER
SEQRES 6 A 222 ARG ASN GLU ASP LEU GLU GLU ILE ALA SER THR ASP LEU
SEQRES 7 A 222 LYS TYR LEU LEU VAL PRO ALA PHE GLN GLY ALA LEU THR
SEQRES 8 A 222 MSE LYS GLN VAL ASN PRO SER LYS ARG LEU ASP HIS LEU
SEQRES 9 A 222 GLN ARG ALA ARG GLU HIS PHE ILE ASN TYR LEU THR GLN
SEQRES 10 A 222 CYS HIS CYS TYR HIS VAL ALA GLU PHE GLU LEU PRO SER
SEQRES 11 A 222 MSE ALA TYR PRO SER LEU VAL ALA MSE ALA SER GLN ARG
SEQRES 12 A 222 GLN ALA LYS ILE GLN ARG TYR LYS GLN LYS LYS GLU LEU
SEQRES 13 A 222 GLU HIS ARG LEU SER ALA MSE LYS SER ALA VAL GLU SER
SEQRES 14 A 222 GLY GLN ALA ASP ASP GLU ARG VAL ARG GLU TYR TYR LEU
SEQRES 15 A 222 LEU HIS LEU GLN ARG TRP ILE ASP ILE SER LEU GLU GLU
SEQRES 16 A 222 ILE GLU SER ILE ASP GLN GLU ILE LYS ILE LEU ARG GLU
SEQRES 17 A 222 ARG ASP SER SER ARG GLU ALA SER THR SER ASN SER SER
SEQRES 18 A 222 ARG
SEQRES 1 C 151 GLY SER MSE PHE THR LYS GLU LEU ASP GLN TRP ILE GLU
SEQRES 2 C 151 GLN LEU ASN GLU CYS LYS GLN LEU SER GLU SER GLN VAL
SEQRES 3 C 151 LYS SER LEU CYS GLU LYS ALA LYS GLU ILE LEU THR LYS
SEQRES 4 C 151 GLU SER ASN VAL GLN GLU VAL ARG CYS PRO VAL THR VAL
SEQRES 5 C 151 CYS GLY ASP VAL HIS GLY GLN PHE HIS ASP LEU MSE GLU
SEQRES 6 C 151 LEU PHE ARG ILE GLY GLY LYS SER PRO ASP THR ASN TYR
SEQRES 7 C 151 LEU PHE MSE GLY ASP TYR VAL ASP ARG GLY TYR TYR SER
SEQRES 8 C 151 VAL GLU THR VAL THR LEU LEU VAL ALA LEU LYS VAL ARG
SEQRES 9 C 151 TYR ARG GLU ARG ILE THR ILE LEU ARG GLY ASN HIS GLU
SEQRES 10 C 151 SER ARG GLN ILE THR GLN VAL TYR GLY PHE TYR ASP GLU
SEQRES 11 C 151 CYS LEU ARG LYS TYR GLY ASN ALA ASN VAL TRP LYS TYR
SEQRES 12 C 151 PHE THR ASP LEU PHE ASP TYR LEU
MODRES 4IYP MSE A 1 MET SELENOMETHIONINE
MODRES 4IYP MSE A 55 MET SELENOMETHIONINE
MODRES 4IYP MSE A 90 MET SELENOMETHIONINE
MODRES 4IYP MSE A 143 MET SELENOMETHIONINE
MODRES 4IYP MSE A 175 MET SELENOMETHIONINE
MODRES 4IYP MSE C 66 MET SELENOMETHIONINE
MODRES 4IYP MSE C 83 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 55 8
HET MSE A 90 8
HET MSE A 143 8
HET MSE A 175 8
HET MSE C 66 8
HET MSE C 83 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 7(C5 H11 N O2 SE)
FORMUL 3 HOH *34(H2 O)
HELIX 1 1 MSE A 1 GLU A 6 1 6
HELIX 2 2 ARG A 11 VAL A 28 1 18
HELIX 3 3 SER A 35 ASP A 60 1 26
HELIX 4 4 ASP A 67 ILE A 71 5 5
HELIX 5 5 ASP A 75 LEU A 79 5 5
HELIX 6 6 LEU A 80 LYS A 91 1 12
HELIX 7 7 ASN A 94 SER A 96 5 3
HELIX 8 8 LYS A 97 TYR A 119 1 23
HELIX 9 9 ARG A 155 SER A 181 1 27
HELIX 10 10 ASP A 185 GLU A 220 1 36
HELIX 11 11 LYS C 8 GLU C 19 1 12
HELIX 12 12 SER C 24 THR C 40 1 17
HELIX 13 13 SER C 93 ARG C 108 1 16
HELIX 14 14 VAL C 126 TYR C 137 1 12
HELIX 15 15 ALA C 140 ASP C 151 1 12
SHEET 1 A 3 GLN C 61 HIS C 63 0
SHEET 2 A 3 ASN C 79 MSE C 83 -1 O PHE C 82 N PHE C 62
SHEET 3 A 3 ILE C 111 LEU C 114 1 O LEU C 114 N LEU C 81
LINK C SER A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N ALA A 2 1555 1555 1.33
LINK C GLU A 54 N MSE A 55 1555 1555 1.32
LINK C MSE A 55 N LEU A 56 1555 1555 1.34
LINK C THR A 89 N MSE A 90 1555 1555 1.34
LINK C MSE A 90 N LYS A 91 1555 1555 1.33
LINK C SER A 142 N MSE A 143 1555 1555 1.33
LINK C MSE A 143 N ALA A 144 1555 1555 1.33
LINK C ALA A 174 N MSE A 175 1555 1555 1.33
LINK C MSE A 175 N LYS A 176 1555 1555 1.34
LINK C LEU C 65 N MSE C 66 1555 1555 1.32
LINK C MSE C 66 N GLU C 67 1555 1555 1.34
LINK C PHE C 82 N MSE C 83 1555 1555 1.33
LINK C MSE C 83 N GLY C 84 1555 1555 1.34
CISPEP 1 TYR A 145 PRO A 146 0 0.62
CRYST1 116.127 116.127 81.230 90.00 90.00 120.00 P 32 2 1 6
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 0.008611 0.004972 0.000000 0.00000
SCALE2 0.000000 0.009943 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012311 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
