HEADER IMMUNE SYSTEM 09-JUL-13 4LL9
TITLE CRYSTAL STRUCTURE OF D3D4 DOMAIN OF THE LILRB1 MOLECULE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEUKOCYTE IMMUNOGLOBULIN-LIKE RECEPTOR SUBFAMILY B MEMBER
COMPND 3 1;
COMPND 4 CHAIN: A, B, C;
COMPND 5 FRAGMENT: D3D4 DOMAIN, UNP RESIDUES 222-417;
COMPND 6 SYNONYM: LIR-1, LEUKOCYTE IMMUNOGLOBULIN-LIKE RECEPTOR 1, CD85
COMPND 7 ANTIGEN-LIKE FAMILY MEMBER J, IMMUNOGLOBULIN-LIKE TRANSCRIPT 2, ILT-
COMPND 8 2, MONOCYTE/MACROPHAGE IMMUNOGLOBULIN-LIKE RECEPTOR 7, MIR-7;
COMPND 9 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: LILRB1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS IG-LIKE DOMAIN, IMMUNE-MODULATORY MOLECULE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR G.NAM,Y.SHI,M.RYU,Q.WANG,H.SONG,J.LIU,J.YAN,J.QI,G.F.GAO
REVDAT 2 06-NOV-13 4LL9 1 JRNL
REVDAT 1 11-SEP-13 4LL9 0
JRNL AUTH G.NAM,Y.SHI,M.RYU,Q.WANG,H.SONG,J.LIU,J.YAN,J.QI,G.F.GAO
JRNL TITL CRYSTAL STRUCTURES OF THE TWO MEMBRANE-PROXIMAL IG-LIKE
JRNL TITL 2 DOMAINS (D3D4) OF LILRB1/B2: ALTERNATIVE MODELS FOR THEIR
JRNL TITL 3 INVOLVEMENT IN PEPTIDE-HLA BINDING
JRNL REF PROTEIN CELL V. 4 761 2013
JRNL REFN ISSN 1674-800X
JRNL PMID 23955630
JRNL DOI 10.1007/S13238-013-3908-X
REMARK 2
REMARK 2 RESOLUTION. 2.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 17590
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.246
REMARK 3 R VALUE (WORKING SET) : 0.245
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 889
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 32.8106 - 4.8767 0.98 2856 160 0.2299 0.2372
REMARK 3 2 4.8767 - 3.8727 0.98 2825 150 0.2008 0.2409
REMARK 3 3 3.8727 - 3.3838 0.98 2791 164 0.2469 0.2832
REMARK 3 4 3.3838 - 3.0746 0.97 2775 134 0.2802 0.3518
REMARK 3 5 3.0746 - 2.8544 0.97 2790 145 0.3221 0.3492
REMARK 3 6 2.8544 - 2.6862 0.95 2664 136 0.3315 0.3735
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) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.510
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.04
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.13
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 : 0.005 4616
REMARK 3 ANGLE : 1.239 6282
REMARK 3 CHIRALITY : 0.043 665
REMARK 3 PLANARITY : 0.007 834
REMARK 3 DIHEDRAL : 16.734 1680
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 13
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 2:46 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.0277 -24.9937 -17.2445
REMARK 3 T TENSOR
REMARK 3 T11: 0.3716 T22: 0.3280
REMARK 3 T33: 0.3083 T12: 0.0114
REMARK 3 T13: 0.1086 T23: -0.0426
REMARK 3 L TENSOR
REMARK 3 L11: 3.1940 L22: 5.7713
REMARK 3 L33: 4.8626 L12: 2.2827
REMARK 3 L13: -1.2064 L23: -0.5389
REMARK 3 S TENSOR
REMARK 3 S11: -0.5362 S12: 0.2339 S13: -0.7057
REMARK 3 S21: -0.6144 S22: 0.3315 S23: -0.6253
REMARK 3 S31: 0.6131 S32: 0.1215 S33: 0.2223
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 47:58 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.2671 -37.0163 -19.4600
REMARK 3 T TENSOR
REMARK 3 T11: 0.6443 T22: 0.4195
REMARK 3 T33: 1.2152 T12: -0.1459
REMARK 3 T13: 0.1069 T23: 0.0592
REMARK 3 L TENSOR
REMARK 3 L11: 3.8258 L22: 7.5896
REMARK 3 L33: 2.0033 L12: -1.4536
REMARK 3 L13: -1.3970 L23: -5.2309
REMARK 3 S TENSOR
REMARK 3 S11: -0.0956 S12: 0.0239 S13: -1.2585
REMARK 3 S21: -0.6908 S22: 0.5133 S23: 0.7612
REMARK 3 S31: 2.0044 S32: -1.1342 S33: 0.9114
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 59:93 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.1571 -25.9907 -16.7779
REMARK 3 T TENSOR
REMARK 3 T11: 0.3679 T22: 0.4693
REMARK 3 T33: 0.4907 T12: 0.0185
REMARK 3 T13: 0.1494 T23: -0.0358
REMARK 3 L TENSOR
REMARK 3 L11: 3.3476 L22: 7.1638
REMARK 3 L33: 6.2894 L12: -0.3455
REMARK 3 L13: -0.4090 L23: 0.1545
REMARK 3 S TENSOR
REMARK 3 S11: -0.4128 S12: 0.2380 S13: -0.5489
REMARK 3 S21: -0.0876 S22: 0.2702 S23: -0.8342
REMARK 3 S31: 0.8227 S32: 0.3214 S33: 0.1041
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 94:140 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.2915 -0.0062 -19.3214
REMARK 3 T TENSOR
REMARK 3 T11: 0.6006 T22: 0.7076
REMARK 3 T33: 0.3927 T12: 0.3268
REMARK 3 T13: 0.0373 T23: 0.0495
REMARK 3 L TENSOR
REMARK 3 L11: 2.8375 L22: 2.0433
REMARK 3 L33: 3.7003 L12: -0.7447
REMARK 3 L13: 1.0011 L23: -0.9340
REMARK 3 S TENSOR
REMARK 3 S11: 0.0749 S12: 0.3100 S13: 0.3573
REMARK 3 S21: -0.1593 S22: -0.1762 S23: 0.2729
REMARK 3 S31: -1.1361 S32: -1.3893 S33: 0.1182
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 141:150 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.0313 -6.7699 -25.7430
REMARK 3 T TENSOR
REMARK 3 T11: 0.7007 T22: 0.7409
REMARK 3 T33: 0.6989 T12: 0.3880
REMARK 3 T13: 0.0718 T23: 0.1764
REMARK 3 L TENSOR
REMARK 3 L11: 5.5754 L22: 9.4647
REMARK 3 L33: 5.0391 L12: 7.0964
REMARK 3 L13: -0.0180 L23: -1.5719
REMARK 3 S TENSOR
REMARK 3 S11: 0.5562 S12: -0.2705 S13: -2.1712
REMARK 3 S21: -0.8670 S22: -0.7881 S23: -1.8866
REMARK 3 S31: -0.2486 S32: -0.1112 S33: -0.0237
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 151:197 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.5952 -0.0120 -20.5077
REMARK 3 T TENSOR
REMARK 3 T11: 0.4394 T22: 0.4771
REMARK 3 T33: 0.3496 T12: 0.1836
REMARK 3 T13: 0.0835 T23: 0.0988
REMARK 3 L TENSOR
REMARK 3 L11: 3.1280 L22: 2.3756
REMARK 3 L33: 3.5830 L12: -0.4346
REMARK 3 L13: 1.2132 L23: -0.0092
REMARK 3 S TENSOR
REMARK 3 S11: -0.1486 S12: 0.1533 S13: -0.2365
REMARK 3 S21: -0.0769 S22: 0.1114 S23: -0.0746
REMARK 3 S31: -0.5812 S32: -0.6636 S33: 0.0805
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 2:58 )
REMARK 3 ORIGIN FOR THE GROUP (A): -43.7570 3.1685 2.6695
REMARK 3 T TENSOR
REMARK 3 T11: 0.2825 T22: 0.2789
REMARK 3 T33: 0.4048 T12: -0.0279
REMARK 3 T13: 0.0296 T23: -0.0243
REMARK 3 L TENSOR
REMARK 3 L11: 6.0951 L22: 1.4889
REMARK 3 L33: 7.7344 L12: -0.4762
REMARK 3 L13: 2.6799 L23: -0.7573
REMARK 3 S TENSOR
REMARK 3 S11: -0.2413 S12: 0.5550 S13: 0.0338
REMARK 3 S21: -0.1476 S22: 0.2176 S23: 0.3064
REMARK 3 S31: -0.2053 S32: -0.1306 S33: -0.2403
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 59:139 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.2681 -0.8896 5.2064
REMARK 3 T TENSOR
REMARK 3 T11: 0.4288 T22: 0.2600
REMARK 3 T33: 0.2232 T12: 0.0057
REMARK 3 T13: 0.0116 T23: -0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 5.6576 L22: 1.4097
REMARK 3 L33: 2.3286 L12: -0.1875
REMARK 3 L13: 1.2158 L23: -0.3172
REMARK 3 S TENSOR
REMARK 3 S11: -0.1988 S12: -0.1772 S13: -0.0685
REMARK 3 S21: -0.0857 S22: 0.0712 S23: 0.1114
REMARK 3 S31: -0.1987 S32: 0.1387 S33: -0.0007
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 140:197 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.7776 -1.1747 4.5426
REMARK 3 T TENSOR
REMARK 3 T11: 0.3763 T22: 0.3111
REMARK 3 T33: 0.2670 T12: 0.0429
REMARK 3 T13: -0.0185 T23: -0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 5.2534 L22: 4.8376
REMARK 3 L33: 4.3294 L12: 3.9896
REMARK 3 L13: -2.0601 L23: -0.6196
REMARK 3 S TENSOR
REMARK 3 S11: -0.1686 S12: 0.2728 S13: -0.0732
REMARK 3 S21: -0.4954 S22: 0.0949 S23: 0.2267
REMARK 3 S31: -0.0462 S32: 0.1757 S33: 0.2351
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 2:39 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.0877 9.8072 29.0561
REMARK 3 T TENSOR
REMARK 3 T11: 0.8419 T22: 0.4768
REMARK 3 T33: 0.4073 T12: 0.0226
REMARK 3 T13: 0.0124 T23: 0.1156
REMARK 3 L TENSOR
REMARK 3 L11: 4.1599 L22: 3.4522
REMARK 3 L33: 0.7079 L12: 0.6898
REMARK 3 L13: 0.3982 L23: -1.1637
REMARK 3 S TENSOR
REMARK 3 S11: 0.1354 S12: 0.6766 S13: 0.2485
REMARK 3 S21: -0.1669 S22: -0.1306 S23: -0.4282
REMARK 3 S31: -0.9484 S32: 0.0134 S33: -0.1815
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 40:58 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.8359 16.7769 30.8594
REMARK 3 T TENSOR
REMARK 3 T11: 1.0193 T22: 0.5030
REMARK 3 T33: 0.5406 T12: 0.1429
REMARK 3 T13: -0.0517 T23: 0.1447
REMARK 3 L TENSOR
REMARK 3 L11: 4.6963 L22: 7.1666
REMARK 3 L33: 3.0654 L12: -1.1254
REMARK 3 L13: 2.4819 L23: 0.5567
REMARK 3 S TENSOR
REMARK 3 S11: 0.8196 S12: 1.0520 S13: 1.6918
REMARK 3 S21: 0.1068 S22: -0.1537 S23: -1.2828
REMARK 3 S31: 0.3204 S32: -0.4580 S33: -0.3185
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 59:133 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.3569 0.5061 30.6268
REMARK 3 T TENSOR
REMARK 3 T11: 0.4568 T22: 0.3588
REMARK 3 T33: 0.1741 T12: 0.1275
REMARK 3 T13: -0.0756 T23: 0.0459
REMARK 3 L TENSOR
REMARK 3 L11: 4.0335 L22: 2.8928
REMARK 3 L33: 5.2155 L12: 0.4729
REMARK 3 L13: -1.3363 L23: -1.0047
REMARK 3 S TENSOR
REMARK 3 S11: -0.2683 S12: 0.1866 S13: 0.1797
REMARK 3 S21: -0.4405 S22: 0.1276 S23: 0.5134
REMARK 3 S31: 0.3009 S32: -0.1546 S33: -0.0605
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 134:197 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.1135 -9.4141 28.3687
REMARK 3 T TENSOR
REMARK 3 T11: 0.5712 T22: 0.4729
REMARK 3 T33: 0.3019 T12: -0.0061
REMARK 3 T13: -0.0315 T23: 0.0286
REMARK 3 L TENSOR
REMARK 3 L11: 3.9495 L22: 8.1108
REMARK 3 L33: 8.5116 L12: 0.2495
REMARK 3 L13: 0.8834 L23: 0.2735
REMARK 3 S TENSOR
REMARK 3 S11: 0.0064 S12: 0.1940 S13: -0.1008
REMARK 3 S21: -0.6494 S22: -0.1137 S23: -0.0538
REMARK 3 S31: 0.9242 S32: -0.5597 S33: 0.1345
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 4LL9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUL-13.
REMARK 100 THE RCSB ID CODE IS RCSB080770.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17596
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.686
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 (%) : 97.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: SAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NAI, PH 6.9, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 X+1/2,Y+1/2,Z
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 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 1.000000 0.000000 0.000000 60.62850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.98800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 60.62850
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.98800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 350
REMARK 350 BIOMOLECULE: 3
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: 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 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 I IOD B 204 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 321 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 ALA A 55
REMARK 465 GLY A 56
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 LEU A 83 CG CD1 CD2
REMARK 470 LEU B 83 CG CD1 CD2
REMARK 470 LEU C 83 CG CD1 CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLY B 165 O HOH B 313 2.04
REMARK 500 OG SER A 3 OH TYR A 32 2.13
REMARK 500 O PRO B 18 O HOH B 314 2.14
REMARK 500 O GLY B 56 O HOH B 309 2.14
REMARK 500 O PHE A 102 O HOH A 307 2.14
REMARK 500 OE1 GLN B 11 NE2 GLN B 25 2.14
REMARK 500 O LEU A 64 O HOH A 306 2.15
REMARK 500 O GLY A 173 O HOH A 308 2.15
REMARK 500 OG1 THR B 174 OE2 GLU B 196 2.16
REMARK 500 O LYS C 5 O HOH C 303 2.19
REMARK 500 NE2 GLN C 133 O HOH C 307 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OG1 THR C 63 OG1 THR C 63 2556 2.04
REMARK 500
REMARK 500 REMARK: NULL
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 PRO B 12 C - N - CA ANGL. DEV. = -14.1 DEGREES
REMARK 500 PRO B 66 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500 PRO B 146 C - N - CA ANGL. DEV. = 11.5 DEGREES
REMARK 500 GLY C 56 N - CA - C ANGL. DEV. = 15.6 DEGREES
REMARK 500 PRO C 66 C - N - CA ANGL. DEV. = 9.0 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 GLU A 19 -3.52 75.66
REMARK 500 ALA A 49 -165.70 -128.10
REMARK 500 PRO A 66 95.23 -8.60
REMARK 500 PRO A 112 -86.59 -83.20
REMARK 500 SER A 128 140.58 -170.39
REMARK 500 GLU A 140 71.22 -63.82
REMARK 500 ASP A 144 -19.50 103.56
REMARK 500 ASP A 145 128.80 163.35
REMARK 500 LYS A 157 115.06 -168.04
REMARK 500 ALA A 172 49.40 -86.13
REMARK 500 GLN B 11 -74.14 -59.52
REMARK 500 GLU B 19 -5.33 75.70
REMARK 500 ALA B 49 -164.07 -125.81
REMARK 500 GLN B 52 69.16 -117.95
REMARK 500 SER B 58 70.19 47.23
REMARK 500 PRO B 66 92.31 -11.46
REMARK 500 PRO B 112 -155.89 -83.74
REMARK 500 SER B 128 141.71 -171.50
REMARK 500 ALA B 143 80.18 -68.32
REMARK 500 LYS B 157 117.00 -170.60
REMARK 500 ALA B 170 21.81 -73.69
REMARK 500 ALA B 172 44.96 -70.58
REMARK 500 GLU C 19 -3.96 76.89
REMARK 500 ALA C 49 -163.93 -128.08
REMARK 500 PRO C 53 -63.50 -91.10
REMARK 500 LEU C 57 131.72 -171.08
REMARK 500 PRO C 66 93.85 -8.14
REMARK 500 HIS C 171 -132.22 -102.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 143 ASP A 144 132.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 301 DISTANCE = 5.39 ANGSTROMS
REMARK 525 HOH C 302 DISTANCE = 5.06 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LLA RELATED DB: PDB
DBREF 4LL9 A 2 197 UNP Q8NHL6 LIRB1_HUMAN 222 417
DBREF 4LL9 B 2 197 UNP Q8NHL6 LIRB1_HUMAN 222 417
DBREF 4LL9 C 2 197 UNP Q8NHL6 LIRB1_HUMAN 222 417
SEQRES 1 A 196 VAL SER LYS LYS PRO SER LEU SER VAL GLN PRO GLY PRO
SEQRES 2 A 196 ILE VAL ALA PRO GLU GLU THR LEU THR LEU GLN CYS GLY
SEQRES 3 A 196 SER ASP ALA GLY TYR ASN ARG PHE VAL LEU TYR LYS ASP
SEQRES 4 A 196 GLY GLU ARG ASP PHE LEU GLN LEU ALA GLY ALA GLN PRO
SEQRES 5 A 196 GLN ALA GLY LEU SER GLN ALA ASN PHE THR LEU GLY PRO
SEQRES 6 A 196 VAL SER ARG SER TYR GLY GLY GLN TYR ARG CYS TYR GLY
SEQRES 7 A 196 ALA HIS ASN LEU SER SER GLU TRP SER ALA PRO SER ASP
SEQRES 8 A 196 PRO LEU ASP ILE LEU ILE ALA GLY GLN PHE TYR ASP ARG
SEQRES 9 A 196 VAL SER LEU SER VAL GLN PRO GLY PRO THR VAL ALA SER
SEQRES 10 A 196 GLY GLU ASN VAL THR LEU LEU CYS GLN SER GLN GLY TRP
SEQRES 11 A 196 MET GLN THR PHE LEU LEU THR LYS GLU GLY ALA ALA ASP
SEQRES 12 A 196 ASP PRO TRP ARG LEU ARG SER THR TYR GLN SER GLN LYS
SEQRES 13 A 196 TYR GLN ALA GLU PHE PRO MET GLY PRO VAL THR SER ALA
SEQRES 14 A 196 HIS ALA GLY THR TYR ARG CYS TYR GLY SER GLN SER SER
SEQRES 15 A 196 LYS PRO TYR LEU LEU THR HIS PRO SER ASP PRO LEU GLU
SEQRES 16 A 196 LEU
SEQRES 1 B 196 VAL SER LYS LYS PRO SER LEU SER VAL GLN PRO GLY PRO
SEQRES 2 B 196 ILE VAL ALA PRO GLU GLU THR LEU THR LEU GLN CYS GLY
SEQRES 3 B 196 SER ASP ALA GLY TYR ASN ARG PHE VAL LEU TYR LYS ASP
SEQRES 4 B 196 GLY GLU ARG ASP PHE LEU GLN LEU ALA GLY ALA GLN PRO
SEQRES 5 B 196 GLN ALA GLY LEU SER GLN ALA ASN PHE THR LEU GLY PRO
SEQRES 6 B 196 VAL SER ARG SER TYR GLY GLY GLN TYR ARG CYS TYR GLY
SEQRES 7 B 196 ALA HIS ASN LEU SER SER GLU TRP SER ALA PRO SER ASP
SEQRES 8 B 196 PRO LEU ASP ILE LEU ILE ALA GLY GLN PHE TYR ASP ARG
SEQRES 9 B 196 VAL SER LEU SER VAL GLN PRO GLY PRO THR VAL ALA SER
SEQRES 10 B 196 GLY GLU ASN VAL THR LEU LEU CYS GLN SER GLN GLY TRP
SEQRES 11 B 196 MET GLN THR PHE LEU LEU THR LYS GLU GLY ALA ALA ASP
SEQRES 12 B 196 ASP PRO TRP ARG LEU ARG SER THR TYR GLN SER GLN LYS
SEQRES 13 B 196 TYR GLN ALA GLU PHE PRO MET GLY PRO VAL THR SER ALA
SEQRES 14 B 196 HIS ALA GLY THR TYR ARG CYS TYR GLY SER GLN SER SER
SEQRES 15 B 196 LYS PRO TYR LEU LEU THR HIS PRO SER ASP PRO LEU GLU
SEQRES 16 B 196 LEU
SEQRES 1 C 196 VAL SER LYS LYS PRO SER LEU SER VAL GLN PRO GLY PRO
SEQRES 2 C 196 ILE VAL ALA PRO GLU GLU THR LEU THR LEU GLN CYS GLY
SEQRES 3 C 196 SER ASP ALA GLY TYR ASN ARG PHE VAL LEU TYR LYS ASP
SEQRES 4 C 196 GLY GLU ARG ASP PHE LEU GLN LEU ALA GLY ALA GLN PRO
SEQRES 5 C 196 GLN ALA GLY LEU SER GLN ALA ASN PHE THR LEU GLY PRO
SEQRES 6 C 196 VAL SER ARG SER TYR GLY GLY GLN TYR ARG CYS TYR GLY
SEQRES 7 C 196 ALA HIS ASN LEU SER SER GLU TRP SER ALA PRO SER ASP
SEQRES 8 C 196 PRO LEU ASP ILE LEU ILE ALA GLY GLN PHE TYR ASP ARG
SEQRES 9 C 196 VAL SER LEU SER VAL GLN PRO GLY PRO THR VAL ALA SER
SEQRES 10 C 196 GLY GLU ASN VAL THR LEU LEU CYS GLN SER GLN GLY TRP
SEQRES 11 C 196 MET GLN THR PHE LEU LEU THR LYS GLU GLY ALA ALA ASP
SEQRES 12 C 196 ASP PRO TRP ARG LEU ARG SER THR TYR GLN SER GLN LYS
SEQRES 13 C 196 TYR GLN ALA GLU PHE PRO MET GLY PRO VAL THR SER ALA
SEQRES 14 C 196 HIS ALA GLY THR TYR ARG CYS TYR GLY SER GLN SER SER
SEQRES 15 C 196 LYS PRO TYR LEU LEU THR HIS PRO SER ASP PRO LEU GLU
SEQRES 16 C 196 LEU
HET IOD A 201 1
HET IOD A 202 1
HET IOD A 203 1
HET IOD A 204 1
HET IOD A 205 1
HET IOD B 201 1
HET IOD B 202 1
HET IOD B 203 1
HET IOD B 204 1
HET IOD C 201 1
HET IOD C 202 1
HET IOD C 203 1
HETNAM IOD IODIDE ION
FORMUL 4 IOD 12(I 1-)
FORMUL 16 HOH *90(H2 O)
HELIX 1 1 SER A 68 GLY A 72 5 5
HELIX 2 2 THR A 168 ALA A 172 5 5
HELIX 3 3 SER B 68 GLY B 72 5 5
HELIX 4 4 THR B 168 ALA B 172 5 5
HELIX 5 5 SER C 68 GLY C 72 5 5
SHEET 1 A 3 SER A 7 GLN A 11 0
SHEET 2 A 3 LEU A 22 SER A 28 -1 O GLN A 25 N SER A 9
SHEET 3 A 3 SER A 58 LEU A 64 -1 O PHE A 62 N LEU A 24
SHEET 1 B 5 ILE A 15 VAL A 16 0
SHEET 2 B 5 LEU A 94 ILE A 98 1 O LEU A 97 N VAL A 16
SHEET 3 B 5 GLY A 73 ALA A 80 -1 N GLY A 73 O ILE A 96
SHEET 4 B 5 ARG A 34 LYS A 39 -1 N TYR A 38 O ARG A 76
SHEET 5 B 5 GLN A 47 GLY A 50 -1 O GLN A 47 N LEU A 37
SHEET 1 C 4 VAL A 106 SER A 109 0
SHEET 2 C 4 ASN A 121 SER A 128 -1 O GLN A 127 N SER A 107
SHEET 3 C 4 TYR A 158 PRO A 166 -1 O MET A 164 N VAL A 122
SHEET 4 C 4 THR A 152 TYR A 153 -1 N THR A 152 O GLN A 159
SHEET 1 D 4 TRP A 147 ARG A 150 0
SHEET 2 D 4 THR A 134 GLU A 140 -1 N LEU A 137 O TRP A 147
SHEET 3 D 4 THR A 174 GLN A 181 -1 O THR A 174 N GLU A 140
SHEET 4 D 4 LYS A 184 LEU A 188 -1 O LYS A 184 N GLN A 181
SHEET 1 E 4 TRP A 147 ARG A 150 0
SHEET 2 E 4 THR A 134 GLU A 140 -1 N LEU A 137 O TRP A 147
SHEET 3 E 4 THR A 174 GLN A 181 -1 O THR A 174 N GLU A 140
SHEET 4 E 4 LEU A 195 GLU A 196 -1 O LEU A 195 N TYR A 175
SHEET 1 F 3 SER B 7 VAL B 10 0
SHEET 2 F 3 LEU B 22 GLY B 27 -1 O GLY B 27 N SER B 7
SHEET 3 F 3 GLN B 59 LEU B 64 -1 O PHE B 62 N LEU B 24
SHEET 1 G 5 ILE B 15 VAL B 16 0
SHEET 2 G 5 LEU B 94 ILE B 98 1 O LEU B 97 N VAL B 16
SHEET 3 G 5 GLY B 73 ALA B 80 -1 N TYR B 75 O LEU B 94
SHEET 4 G 5 ARG B 34 LYS B 39 -1 N TYR B 38 O ARG B 76
SHEET 5 G 5 GLU B 42 LEU B 48 -1 O LEU B 46 N LEU B 37
SHEET 1 H 4 SER B 107 SER B 109 0
SHEET 2 H 4 ASN B 121 SER B 128 -1 O LEU B 125 N SER B 109
SHEET 3 H 4 TYR B 158 PRO B 166 -1 O PHE B 162 N LEU B 124
SHEET 4 H 4 THR B 152 TYR B 153 -1 N THR B 152 O GLN B 159
SHEET 1 I 4 TRP B 147 ARG B 150 0
SHEET 2 I 4 THR B 134 LYS B 139 -1 N PHE B 135 O LEU B 149
SHEET 3 I 4 THR B 174 SER B 180 -1 O ARG B 176 N THR B 138
SHEET 4 I 4 LEU B 195 GLU B 196 -1 O LEU B 195 N TYR B 175
SHEET 1 J 3 SER C 7 GLN C 11 0
SHEET 2 J 3 LEU C 22 SER C 28 -1 O GLN C 25 N SER C 9
SHEET 3 J 3 SER C 58 LEU C 64 -1 O PHE C 62 N LEU C 24
SHEET 1 K 5 ILE C 15 VAL C 16 0
SHEET 2 K 5 LEU C 94 ILE C 98 1 O LEU C 97 N VAL C 16
SHEET 3 K 5 GLY C 73 ALA C 80 -1 N TYR C 75 O LEU C 94
SHEET 4 K 5 ARG C 34 LYS C 39 -1 N TYR C 38 O ARG C 76
SHEET 5 K 5 GLN C 47 GLY C 50 -1 O GLN C 47 N LEU C 37
SHEET 1 L 4 VAL C 106 SER C 109 0
SHEET 2 L 4 ASN C 121 SER C 128 -1 O LEU C 125 N SER C 109
SHEET 3 L 4 TYR C 158 PRO C 166 -1 O MET C 164 N VAL C 122
SHEET 4 L 4 THR C 152 TYR C 153 -1 N THR C 152 O GLN C 159
SHEET 1 M 4 TRP C 147 ARG C 150 0
SHEET 2 M 4 THR C 134 LYS C 139 -1 N PHE C 135 O LEU C 149
SHEET 3 M 4 THR C 174 SER C 180 -1 O TYR C 178 N LEU C 136
SHEET 4 M 4 LEU C 195 GLU C 196 -1 O LEU C 195 N TYR C 175
SSBOND 1 CYS A 26 CYS A 77 1555 1555 2.03
SSBOND 2 CYS A 126 CYS A 177 1555 1555 2.04
SSBOND 3 CYS B 26 CYS B 77 1555 1555 2.03
SSBOND 4 CYS B 126 CYS B 177 1555 1555 2.04
SSBOND 5 CYS C 26 CYS C 77 1555 1555 2.03
SSBOND 6 CYS C 126 CYS C 177 1555 1555 2.04
CISPEP 1 GLN A 11 PRO A 12 0 -0.87
CISPEP 2 GLN B 111 PRO B 112 0 -4.02
CISPEP 3 GLN C 11 PRO C 12 0 -1.87
CISPEP 4 ALA C 55 GLY C 56 0 10.79
CISPEP 5 GLN C 111 PRO C 112 0 8.85
CISPEP 6 ALA C 143 ASP C 144 0 3.87
SITE 1 AC1 2 ARG A 150 ARG C 69
SITE 1 AC2 1 PRO A 185
SITE 1 AC3 2 ARG A 69 ARG B 150
SITE 1 AC4 2 HIS A 190 PRO A 191
SITE 1 AC5 1 LYS A 4
SITE 1 AC6 1 ARG B 69
SITE 1 AC7 2 PRO B 185 TYR B 186
SITE 1 AC8 2 HIS B 190 PRO B 191
SITE 1 AC9 1 GLN B 111
SITE 1 BC1 2 HIS C 190 PRO C 191
CRYST1 121.257 71.976 75.036 90.00 95.20 90.00 C 1 2 1 12
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 0.008247 0.000000 0.000751 0.00000
SCALE2 0.000000 0.013894 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013382 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
