HEADER IMMUNE SYSTEM 27-FEB-15 4YH6
TITLE CRYSTAL STRUCTURE OF IL1RAPL1 ECTODOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-1 RECEPTOR ACCESSORY PROTEIN-LIKE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 19-352;
COMPND 5 SYNONYM: IL1RAPL-1,X-LINKED INTERLEUKIN-1 RECEPTOR ACCESSORY PROTEIN-
COMPND 6 LIKE 1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: IL1RAPL1;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: FREESTYLE 293-F
KEYWDS SYNAPSE ORGANIZER, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.YAMAGATA,S.FUKAI
REVDAT 3 29-JUL-20 4YH6 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 05-FEB-20 4YH6 1 SOURCE REMARK
REVDAT 1 06-MAY-15 4YH6 0
JRNL AUTH A.YAMAGATA,T.YOSHIDA,Y.SATO,S.GOTO-ITO,T.UEMURA,A.MAEDA,
JRNL AUTH 2 T.SHIROSHIMA,S.IWASAWA-OKAMOTO,H.MORI,M.MISHINA,S.FUKAI
JRNL TITL MECHANISMS OF SPLICING-DEPENDENT TRANS-SYNAPTIC ADHESION BY
JRNL TITL 2 PTP DELTA-IL1RAPL1/IL-1RACP FOR SYNAPTIC DIFFERENTIATION.
JRNL REF NAT COMMUN V. 6 6926 2015
JRNL REFN ESSN 2041-1723
JRNL PMID 25908590
JRNL DOI 10.1038/NCOMMS7926
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.510
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 23998
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.265
REMARK 3 R VALUE (WORKING SET) : 0.263
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1210
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 40.8527 - 6.2337 0.99 2784 134 0.2670 0.2895
REMARK 3 2 6.2337 - 4.9506 0.99 2613 142 0.2345 0.2605
REMARK 3 3 4.9506 - 4.3256 0.99 2552 140 0.1876 0.2314
REMARK 3 4 4.3256 - 3.9305 0.99 2542 144 0.2148 0.2615
REMARK 3 5 3.9305 - 3.6489 0.98 2497 131 0.2562 0.3023
REMARK 3 6 3.6489 - 3.4339 0.98 2502 133 0.2803 0.3162
REMARK 3 7 3.4339 - 3.2620 0.97 2442 150 0.3097 0.3390
REMARK 3 8 3.2620 - 3.1201 0.96 2432 126 0.3538 0.4019
REMARK 3 9 3.1201 - 3.0000 0.95 2424 110 0.3842 0.4259
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) : 0.610
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.190
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 : 0.004 5424
REMARK 3 ANGLE : 0.891 7349
REMARK 3 CHIRALITY : 0.041 880
REMARK 3 PLANARITY : 0.003 877
REMARK 3 DIHEDRAL : 17.453 2077
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 31 THROUGH 136 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.8786 -3.5282 49.6783
REMARK 3 T TENSOR
REMARK 3 T11: 0.4283 T22: 0.3226
REMARK 3 T33: 0.3809 T12: -0.0005
REMARK 3 T13: -0.0348 T23: 0.0815
REMARK 3 L TENSOR
REMARK 3 L11: 4.7294 L22: 2.4917
REMARK 3 L33: 4.4919 L12: 0.9868
REMARK 3 L13: 3.2421 L23: 2.4127
REMARK 3 S TENSOR
REMARK 3 S11: 0.4004 S12: -0.1433 S13: -0.1256
REMARK 3 S21: 0.5219 S22: -0.3252 S23: -0.2537
REMARK 3 S31: 0.3664 S32: -0.2531 S33: -0.1121
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 137 THROUGH 234 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.2140 -12.1943 25.0477
REMARK 3 T TENSOR
REMARK 3 T11: 0.7191 T22: 1.0023
REMARK 3 T33: 0.7041 T12: -0.3183
REMARK 3 T13: -0.2146 T23: -0.0356
REMARK 3 L TENSOR
REMARK 3 L11: 2.1544 L22: 2.2472
REMARK 3 L33: 2.3785 L12: -0.3839
REMARK 3 L13: 0.3325 L23: -0.0924
REMARK 3 S TENSOR
REMARK 3 S11: 0.4405 S12: -0.0694 S13: -0.5302
REMARK 3 S21: 0.0269 S22: -0.2571 S23: -0.0331
REMARK 3 S31: 0.7613 S32: -1.1068 S33: -0.1685
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 235 THROUGH 351 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.9433 8.7150 -5.0368
REMARK 3 T TENSOR
REMARK 3 T11: 0.5166 T22: 0.9068
REMARK 3 T33: 0.3631 T12: 0.0718
REMARK 3 T13: 0.0338 T23: -0.0933
REMARK 3 L TENSOR
REMARK 3 L11: 2.0327 L22: 4.8498
REMARK 3 L33: 3.0914 L12: 0.9928
REMARK 3 L13: -1.3103 L23: -2.1624
REMARK 3 S TENSOR
REMARK 3 S11: -0.1493 S12: -0.3133 S13: 0.3175
REMARK 3 S21: -0.3860 S22: 0.2052 S23: 0.3777
REMARK 3 S31: 0.0504 S32: -0.1320 S33: -0.0213
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 31 THROUGH 72 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.1129 12.7719 21.7227
REMARK 3 T TENSOR
REMARK 3 T11: 0.5347 T22: 0.8102
REMARK 3 T33: 0.7769 T12: 0.0103
REMARK 3 T13: 0.1905 T23: -0.1022
REMARK 3 L TENSOR
REMARK 3 L11: 3.7973 L22: 1.5282
REMARK 3 L33: 1.8725 L12: -0.1489
REMARK 3 L13: -2.2712 L23: 0.8165
REMARK 3 S TENSOR
REMARK 3 S11: -0.0814 S12: -0.2067 S13: 0.0157
REMARK 3 S21: -0.1990 S22: 0.4643 S23: -1.5048
REMARK 3 S31: 0.4506 S32: 0.9802 S33: 0.3848
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 73 THROUGH 234 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.2415 19.7185 32.2998
REMARK 3 T TENSOR
REMARK 3 T11: 0.4213 T22: 0.1988
REMARK 3 T33: 0.3537 T12: 0.0988
REMARK 3 T13: 0.0982 T23: -0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 1.4004 L22: 2.2468
REMARK 3 L33: 4.9655 L12: 0.1625
REMARK 3 L13: 0.0982 L23: 2.3907
REMARK 3 S TENSOR
REMARK 3 S11: -0.0161 S12: 0.1100 S13: -0.0351
REMARK 3 S21: -0.4950 S22: -0.0277 S23: -0.2926
REMARK 3 S31: -0.3025 S32: -0.2154 S33: 0.0343
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 235 THROUGH 351 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.1590 -3.4635 72.9109
REMARK 3 T TENSOR
REMARK 3 T11: 0.2157 T22: 0.2210
REMARK 3 T33: 0.2148 T12: -0.1550
REMARK 3 T13: 0.0084 T23: -0.0543
REMARK 3 L TENSOR
REMARK 3 L11: 2.2514 L22: 2.8145
REMARK 3 L33: 2.7679 L12: -0.0277
REMARK 3 L13: 0.3047 L23: -1.8689
REMARK 3 S TENSOR
REMARK 3 S11: -0.0151 S12: -0.1511 S13: 0.0549
REMARK 3 S21: 0.2003 S22: 0.1385 S23: 0.3336
REMARK 3 S31: 0.2086 S32: -0.4834 S33: 0.0257
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 4YH6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207455.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23998
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.38200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0-2.4 M AMMONIUM SULFATE, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 51.22700
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 51.22700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 111.35600
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 51.22700
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 51.22700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 111.35600
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 51.22700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.22700
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 111.35600
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 51.22700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.22700
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 111.35600
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 65.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
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 ALA A 12
REMARK 465 GLN A 13
REMARK 465 PRO A 14
REMARK 465 ALA A 15
REMARK 465 ALA A 16
REMARK 465 ARG A 17
REMARK 465 ASP A 18
REMARK 465 LEU A 19
REMARK 465 LYS A 20
REMARK 465 VAL A 21
REMARK 465 VAL A 22
REMARK 465 THR A 23
REMARK 465 LYS A 24
REMARK 465 ARG A 25
REMARK 465 GLY A 26
REMARK 465 SER A 27
REMARK 465 ALA A 28
REMARK 465 ASP A 29
REMARK 465 GLY A 30
REMARK 465 LEU A 172
REMARK 465 PRO A 173
REMARK 465 THR A 174
REMARK 465 ARG A 175
REMARK 465 GLU A 176
REMARK 465 PRO A 177
REMARK 465 GLY A 275
REMARK 465 ASP A 276
REMARK 465 ARG A 352
REMARK 465 LYS A 353
REMARK 465 HIS A 354
REMARK 465 HIS A 355
REMARK 465 HIS A 356
REMARK 465 HIS A 357
REMARK 465 HIS A 358
REMARK 465 HIS A 359
REMARK 465 ALA B 12
REMARK 465 GLN B 13
REMARK 465 PRO B 14
REMARK 465 ALA B 15
REMARK 465 ALA B 16
REMARK 465 ARG B 17
REMARK 465 ASP B 18
REMARK 465 LEU B 19
REMARK 465 LYS B 20
REMARK 465 VAL B 21
REMARK 465 VAL B 22
REMARK 465 THR B 23
REMARK 465 LYS B 24
REMARK 465 ARG B 25
REMARK 465 GLY B 26
REMARK 465 SER B 27
REMARK 465 ALA B 28
REMARK 465 ASP B 29
REMARK 465 GLY B 30
REMARK 465 SER B 35
REMARK 465 VAL B 36
REMARK 465 PHE B 56
REMARK 465 TYR B 57
REMARK 465 GLY B 58
REMARK 465 TYR B 59
REMARK 465 ILE B 60
REMARK 465 ARG B 61
REMARK 465 THR B 62
REMARK 465 ASN B 63
REMARK 465 TYR B 64
REMARK 465 SER B 65
REMARK 465 ARG B 175
REMARK 465 GLU B 176
REMARK 465 GLY B 275
REMARK 465 ASP B 276
REMARK 465 ARG B 352
REMARK 465 LYS B 353
REMARK 465 HIS B 354
REMARK 465 HIS B 355
REMARK 465 HIS B 356
REMARK 465 HIS B 357
REMARK 465 HIS B 358
REMARK 465 HIS B 359
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 SG CYS A 31 CB CYS A 126 2.08
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 GLU A 86 64.85 61.08
REMARK 500 PHE A 91 -74.99 -57.32
REMARK 500 GLU A 100 -120.35 55.79
REMARK 500 THR A 140 73.00 52.58
REMARK 500 ASP A 169 -3.69 70.42
REMARK 500 ARG A 198 115.59 -26.74
REMARK 500 ASP A 239 -1.18 68.70
REMARK 500 LEU A 252 72.72 53.21
REMARK 500 ASP A 294 42.89 35.81
REMARK 500 SER B 80 -1.77 72.43
REMARK 500 GLU B 86 64.87 60.49
REMARK 500 ARG B 95 -60.05 -99.66
REMARK 500 GLU B 100 -121.90 56.75
REMARK 500 THR B 140 75.38 54.47
REMARK 500 ARG B 198 73.93 28.42
REMARK 500 LEU B 252 73.17 54.94
REMARK 500 ASP B 294 74.15 36.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4YH7 RELATED DB: PDB
DBREF 4YH6 A 19 352 UNP P59823 IRPL1_MOUSE 19 352
DBREF 4YH6 B 19 352 UNP P59823 IRPL1_MOUSE 19 352
SEQADV 4YH6 ALA A 12 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 GLN A 13 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 PRO A 14 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 ALA A 15 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 ALA A 16 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 ARG A 17 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 ASP A 18 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 LYS A 353 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 HIS A 354 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 HIS A 355 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 HIS A 356 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 HIS A 357 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 HIS A 358 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 HIS A 359 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 ALA B 12 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 GLN B 13 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 PRO B 14 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 ALA B 15 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 ALA B 16 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 ARG B 17 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 ASP B 18 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 LYS B 353 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 HIS B 354 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 HIS B 355 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 HIS B 356 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 HIS B 357 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 HIS B 358 UNP P59823 EXPRESSION TAG
SEQADV 4YH6 HIS B 359 UNP P59823 EXPRESSION TAG
SEQRES 1 A 348 ALA GLN PRO ALA ALA ARG ASP LEU LYS VAL VAL THR LYS
SEQRES 2 A 348 ARG GLY SER ALA ASP GLY CYS THR ASP TRP SER VAL ASP
SEQRES 3 A 348 ILE LYS LYS TYR GLN VAL LEU VAL GLY GLU PRO VAL ARG
SEQRES 4 A 348 ILE LYS CYS ALA LEU PHE TYR GLY TYR ILE ARG THR ASN
SEQRES 5 A 348 TYR SER LEU ALA GLN SER ALA GLY LEU SER LEU MET TRP
SEQRES 6 A 348 TYR LYS SER SER GLY PRO GLY ASP PHE GLU GLU PRO ILE
SEQRES 7 A 348 ALA PHE ASP GLY SER ARG MET SER LYS GLU GLU ASP SER
SEQRES 8 A 348 ILE TRP PHE ARG PRO THR LEU LEU GLN ASP SER GLY LEU
SEQRES 9 A 348 TYR ALA CYS VAL ILE ARG ASN SER THR TYR CYS MET LYS
SEQRES 10 A 348 VAL SER ILE SER LEU THR VAL GLY GLU ASN ASP THR GLY
SEQRES 11 A 348 LEU CYS TYR ASN SER LYS MET LYS TYR PHE GLU LYS ALA
SEQRES 12 A 348 GLU LEU SER LYS SER LYS GLU ILE SER CYS ARG ASP ILE
SEQRES 13 A 348 GLU ASP PHE LEU LEU PRO THR ARG GLU PRO GLU ILE LEU
SEQRES 14 A 348 TRP TYR LYS GLU CYS ARG THR LYS ALA TRP ARG PRO SER
SEQRES 15 A 348 ILE VAL PHE LYS ARG ASP THR LEU LEU ILE LYS GLU VAL
SEQRES 16 A 348 LYS GLU ASP ASP ILE GLY ASN TYR THR CYS GLU LEU LYS
SEQRES 17 A 348 TYR GLY GLY PHE VAL VAL ARG ARG THR THR GLU LEU THR
SEQRES 18 A 348 VAL THR ALA PRO LEU THR ASP LYS PRO PRO LYS LEU LEU
SEQRES 19 A 348 TYR PRO MET GLU SER LYS LEU THR VAL GLN GLU THR GLN
SEQRES 20 A 348 LEU GLY GLY SER ALA ASN LEU THR CYS ARG ALA PHE PHE
SEQRES 21 A 348 GLY TYR SER GLY ASP VAL SER PRO LEU ILE TYR TRP MET
SEQRES 22 A 348 LYS GLY GLU LYS PHE ILE GLU ASP LEU ASP GLU ASN ARG
SEQRES 23 A 348 VAL TRP GLU SER ASP ILE ARG ILE LEU LYS GLU HIS LEU
SEQRES 24 A 348 GLY GLU GLN GLU VAL SER ILE SER LEU ILE VAL ASP SER
SEQRES 25 A 348 VAL GLU GLU GLY ASP LEU GLY ASN TYR SER CYS TYR VAL
SEQRES 26 A 348 GLU ASN GLY ASN GLY ARG ARG HIS ALA SER VAL LEU LEU
SEQRES 27 A 348 HIS LYS ARG LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 348 ALA GLN PRO ALA ALA ARG ASP LEU LYS VAL VAL THR LYS
SEQRES 2 B 348 ARG GLY SER ALA ASP GLY CYS THR ASP TRP SER VAL ASP
SEQRES 3 B 348 ILE LYS LYS TYR GLN VAL LEU VAL GLY GLU PRO VAL ARG
SEQRES 4 B 348 ILE LYS CYS ALA LEU PHE TYR GLY TYR ILE ARG THR ASN
SEQRES 5 B 348 TYR SER LEU ALA GLN SER ALA GLY LEU SER LEU MET TRP
SEQRES 6 B 348 TYR LYS SER SER GLY PRO GLY ASP PHE GLU GLU PRO ILE
SEQRES 7 B 348 ALA PHE ASP GLY SER ARG MET SER LYS GLU GLU ASP SER
SEQRES 8 B 348 ILE TRP PHE ARG PRO THR LEU LEU GLN ASP SER GLY LEU
SEQRES 9 B 348 TYR ALA CYS VAL ILE ARG ASN SER THR TYR CYS MET LYS
SEQRES 10 B 348 VAL SER ILE SER LEU THR VAL GLY GLU ASN ASP THR GLY
SEQRES 11 B 348 LEU CYS TYR ASN SER LYS MET LYS TYR PHE GLU LYS ALA
SEQRES 12 B 348 GLU LEU SER LYS SER LYS GLU ILE SER CYS ARG ASP ILE
SEQRES 13 B 348 GLU ASP PHE LEU LEU PRO THR ARG GLU PRO GLU ILE LEU
SEQRES 14 B 348 TRP TYR LYS GLU CYS ARG THR LYS ALA TRP ARG PRO SER
SEQRES 15 B 348 ILE VAL PHE LYS ARG ASP THR LEU LEU ILE LYS GLU VAL
SEQRES 16 B 348 LYS GLU ASP ASP ILE GLY ASN TYR THR CYS GLU LEU LYS
SEQRES 17 B 348 TYR GLY GLY PHE VAL VAL ARG ARG THR THR GLU LEU THR
SEQRES 18 B 348 VAL THR ALA PRO LEU THR ASP LYS PRO PRO LYS LEU LEU
SEQRES 19 B 348 TYR PRO MET GLU SER LYS LEU THR VAL GLN GLU THR GLN
SEQRES 20 B 348 LEU GLY GLY SER ALA ASN LEU THR CYS ARG ALA PHE PHE
SEQRES 21 B 348 GLY TYR SER GLY ASP VAL SER PRO LEU ILE TYR TRP MET
SEQRES 22 B 348 LYS GLY GLU LYS PHE ILE GLU ASP LEU ASP GLU ASN ARG
SEQRES 23 B 348 VAL TRP GLU SER ASP ILE ARG ILE LEU LYS GLU HIS LEU
SEQRES 24 B 348 GLY GLU GLN GLU VAL SER ILE SER LEU ILE VAL ASP SER
SEQRES 25 B 348 VAL GLU GLU GLY ASP LEU GLY ASN TYR SER CYS TYR VAL
SEQRES 26 B 348 GLU ASN GLY ASN GLY ARG ARG HIS ALA SER VAL LEU LEU
SEQRES 27 B 348 HIS LYS ARG LYS HIS HIS HIS HIS HIS HIS
HET NAG C 1 14
HET NAG C 2 14
HET BMA C 3 11
HET NAG D 1 14
HET NAG D 2 14
HET BMA D 3 11
HET MAN D 4 11
HET MAN D 5 11
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET MAN E 4 11
HET MAN E 5 11
HET NAG F 1 14
HET NAG F 2 14
HET BMA F 3 11
HET NAG G 1 14
HET NAG G 2 14
HET BMA G 3 11
HET MAN G 4 11
HET MAN G 5 11
HET NAG H 1 14
HET NAG H 2 14
HET BMA H 3 11
HET MAN H 4 11
HET NAG A 404 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
FORMUL 3 NAG 13(C8 H15 N O6)
FORMUL 3 BMA 6(C6 H12 O6)
FORMUL 4 MAN 7(C6 H12 O6)
HELIX 1 AA1 CYS A 53 GLY A 58 1 6
HELIX 2 AA2 ASN A 63 GLN A 68 1 6
HELIX 3 AA3 SER A 69 GLY A 71 5 3
HELIX 4 AA4 LEU A 109 SER A 113 5 5
HELIX 5 AA5 ILE A 290 ASP A 294 1 5
HELIX 6 AA6 LEU B 109 SER B 113 5 5
HELIX 7 AA7 ILE B 167 LEU B 171 5 5
SHEET 1 AA1 3 THR A 32 TRP A 34 0
SHEET 2 AA1 3 CYS A 126 GLY A 136 1 O LYS A 128 N TRP A 34
SHEET 3 AA1 3 LYS A 40 LEU A 44 1 N TYR A 41 O THR A 134
SHEET 1 AA2 5 THR A 32 TRP A 34 0
SHEET 2 AA2 5 CYS A 126 GLY A 136 1 O LYS A 128 N TRP A 34
SHEET 3 AA2 5 GLY A 114 ARG A 121 -1 N TYR A 116 O ILE A 131
SHEET 4 AA2 5 SER A 73 LYS A 78 -1 N MET A 75 O VAL A 119
SHEET 5 AA2 5 GLU A 87 PRO A 88 -1 O GLU A 87 N LYS A 78
SHEET 1 AA3 3 VAL A 49 LYS A 52 0
SHEET 2 AA3 3 SER A 102 PHE A 105 -1 O PHE A 105 N VAL A 49
SHEET 3 AA3 3 MET A 96 GLU A 99 -1 N GLU A 99 O SER A 102
SHEET 1 AA4 4 TYR A 150 GLU A 155 0
SHEET 2 AA4 4 VAL A 224 THR A 234 1 O THR A 228 N TYR A 150
SHEET 3 AA4 4 GLY A 212 LYS A 219 -1 N TYR A 214 O THR A 229
SHEET 4 AA4 4 LEU A 180 LYS A 183 -1 N LEU A 180 O GLU A 217
SHEET 1 AA5 3 LYS A 160 SER A 163 0
SHEET 2 AA5 3 THR A 200 ILE A 203 -1 O LEU A 201 N ILE A 162
SHEET 3 AA5 3 ILE A 194 LYS A 197 -1 N LYS A 197 O THR A 200
SHEET 1 AA6 4 LYS A 243 TYR A 246 0
SHEET 2 AA6 4 ALA A 263 PHE A 270 -1 O ARG A 268 N TYR A 246
SHEET 3 AA6 4 GLU A 312 VAL A 321 -1 O LEU A 319 N LEU A 265
SHEET 4 AA6 4 VAL A 298 GLU A 300 -1 N TRP A 299 O ILE A 320
SHEET 1 AA7 4 LYS A 243 TYR A 246 0
SHEET 2 AA7 4 ALA A 263 PHE A 270 -1 O ARG A 268 N TYR A 246
SHEET 3 AA7 4 GLU A 312 VAL A 321 -1 O LEU A 319 N LEU A 265
SHEET 4 AA7 4 ARG A 304 HIS A 309 -1 N ARG A 304 O SER A 316
SHEET 1 AA8 5 THR A 253 GLU A 256 0
SHEET 2 AA8 5 ARG A 342 HIS A 350 1 O LEU A 348 N GLN A 255
SHEET 3 AA8 5 ASN A 331 GLU A 337 -1 N TYR A 332 O VAL A 347
SHEET 4 AA8 5 LEU A 280 LYS A 285 -1 N MET A 284 O SER A 333
SHEET 5 AA8 5 LYS A 288 PHE A 289 -1 O LYS A 288 N LYS A 285
SHEET 1 AA9 5 LYS B 40 LEU B 44 0
SHEET 2 AA9 5 CYS B 126 GLY B 136 1 O THR B 134 N TYR B 41
SHEET 3 AA9 5 GLY B 114 ARG B 121 -1 N TYR B 116 O ILE B 131
SHEET 4 AA9 5 SER B 73 LYS B 78 -1 N MET B 75 O VAL B 119
SHEET 5 AA9 5 GLU B 87 PRO B 88 -1 O GLU B 87 N LYS B 78
SHEET 1 AB1 3 VAL B 49 LYS B 52 0
SHEET 2 AB1 3 SER B 102 PHE B 105 -1 O ILE B 103 N ILE B 51
SHEET 3 AB1 3 MET B 96 GLU B 99 -1 N GLU B 99 O SER B 102
SHEET 1 AB2 4 TYR B 150 GLU B 155 0
SHEET 2 AB2 4 VAL B 224 THR B 234 1 O THR B 228 N TYR B 150
SHEET 3 AB2 4 GLY B 212 LYS B 219 -1 N TYR B 214 O THR B 229
SHEET 4 AB2 4 ILE B 179 LYS B 183 -1 N LEU B 180 O GLU B 217
SHEET 1 AB3 3 LYS B 160 SER B 163 0
SHEET 2 AB3 3 THR B 200 ILE B 203 -1 O LEU B 201 N ILE B 162
SHEET 3 AB3 3 ILE B 194 LYS B 197 -1 N VAL B 195 O LEU B 202
SHEET 1 AB4 4 LYS B 243 TYR B 246 0
SHEET 2 AB4 4 ALA B 263 PHE B 270 -1 O ARG B 268 N LEU B 245
SHEET 3 AB4 4 GLU B 312 VAL B 321 -1 O LEU B 319 N LEU B 265
SHEET 4 AB4 4 VAL B 298 GLU B 300 -1 N TRP B 299 O ILE B 320
SHEET 1 AB5 4 LYS B 243 TYR B 246 0
SHEET 2 AB5 4 ALA B 263 PHE B 270 -1 O ARG B 268 N LEU B 245
SHEET 3 AB5 4 GLU B 312 VAL B 321 -1 O LEU B 319 N LEU B 265
SHEET 4 AB5 4 ARG B 304 HIS B 309 -1 N ARG B 304 O SER B 316
SHEET 1 AB6 5 THR B 253 GLU B 256 0
SHEET 2 AB6 5 ARG B 342 HIS B 350 1 O LEU B 348 N GLN B 255
SHEET 3 AB6 5 ASN B 331 GLU B 337 -1 N TYR B 332 O VAL B 347
SHEET 4 AB6 5 LEU B 280 LYS B 285 -1 N TYR B 282 O TYR B 335
SHEET 5 AB6 5 LYS B 288 PHE B 289 -1 O LYS B 288 N LYS B 285
SSBOND 1 CYS A 31 CYS A 126 1555 1555 2.03
SSBOND 2 CYS A 53 CYS A 118 1555 1555 2.03
SSBOND 3 CYS A 143 CYS A 185 1555 1555 2.03
SSBOND 4 CYS A 164 CYS A 216 1555 1555 2.03
SSBOND 5 CYS A 267 CYS A 334 1555 1555 2.03
SSBOND 6 CYS B 31 CYS B 126 1555 1555 2.03
SSBOND 7 CYS B 53 CYS B 118 1555 1555 2.03
SSBOND 8 CYS B 143 CYS B 185 1555 1555 2.04
SSBOND 9 CYS B 164 CYS B 216 1555 1555 2.03
SSBOND 10 CYS B 267 CYS B 334 1555 1555 2.03
LINK ND2 ASN A 122 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN A 138 C1 NAG A 404 1555 1555 1.44
LINK ND2 ASN A 213 C1 NAG D 1 1555 1555 1.44
LINK ND2 ASN A 264 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN B 138 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN B 213 C1 NAG G 1 1555 1555 1.45
LINK ND2 ASN B 264 C1 NAG H 1 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.46
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.44
LINK O3 BMA D 3 C1 MAN D 4 1555 1555 1.45
LINK O6 BMA D 3 C1 MAN D 5 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.44
LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.46
LINK O6 BMA E 3 C1 MAN E 5 1555 1555 1.46
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.43
LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.44
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44
LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.45
LINK O3 BMA G 3 C1 MAN G 4 1555 1555 1.44
LINK O6 BMA G 3 C1 MAN G 5 1555 1555 1.44
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44
LINK O4 NAG H 2 C1 BMA H 3 1555 1555 1.44
LINK O3 BMA H 3 C1 MAN H 4 1555 1555 1.45
CISPEP 1 ARG A 106 PRO A 107 0 -5.30
CISPEP 2 TYR A 246 PRO A 247 0 -6.30
CISPEP 3 ARG B 106 PRO B 107 0 -7.09
CISPEP 4 LEU B 172 PRO B 173 0 1.72
CISPEP 5 TYR B 246 PRO B 247 0 -4.88
CRYST1 102.454 102.454 222.712 90.00 90.00 90.00 P 42 21 2 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 0.009760 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009760 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004490 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
