HEADER STRUCTURAL PROTEIN 03-MAR-16 5IK8
TITLE LAMININ A2LG45 I-FORM, G6/7 BOUND.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LAMININ SUBUNIT ALPHA-2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: LAMININ M CHAIN,LAMININ-12 SUBUNIT ALPHA,LAMININ-2 SUBUNIT
COMPND 5 ALPHA,LAMININ-4 SUBUNIT ALPHA,MEROSIN HEAVY CHAIN;
COMPND 6 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: LAMA2;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293
KEYWDS EXTRACELLULAR MATRIX, LIGAND BINDING, LG DOMAIN, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.C.BRIGGS,E.HOHENESTER,K.P.CAMPBELL
REVDAT 5 10-JAN-24 5IK8 1 HETSYN LINK
REVDAT 4 29-JUL-20 5IK8 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 28-SEP-16 5IK8 1 JRNL
REVDAT 2 24-AUG-16 5IK8 1 JRNL
REVDAT 1 10-AUG-16 5IK8 0
JRNL AUTH D.C.BRIGGS,T.YOSHIDA-MORIGUCHI,T.ZHENG,D.VENZKE,
JRNL AUTH 2 M.E.ANDERSON,A.STRAZZULLI,M.MORACCI,L.YU,E.HOHENESTER,
JRNL AUTH 3 K.P.CAMPBELL
JRNL TITL STRUCTURAL BASIS OF LAMININ BINDING TO THE LARGE GLYCANS ON
JRNL TITL 2 DYSTROGLYCAN.
JRNL REF NAT.CHEM.BIOL. V. 12 810 2016
JRNL REFN ESSN 1552-4469
JRNL PMID 27526028
JRNL DOI 10.1038/NCHEMBIO.2146
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 68768
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3436
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 55.7917 - 5.8459 1.00 2772 151 0.1943 0.2062
REMARK 3 2 5.8459 - 4.6408 1.00 2674 154 0.1416 0.1801
REMARK 3 3 4.6408 - 4.0543 1.00 2652 148 0.1253 0.1572
REMARK 3 4 4.0543 - 3.6837 1.00 2607 156 0.1447 0.1733
REMARK 3 5 3.6837 - 3.4197 1.00 2633 150 0.1580 0.1612
REMARK 3 6 3.4197 - 3.2181 1.00 2625 135 0.1758 0.2004
REMARK 3 7 3.2181 - 3.0570 1.00 2631 125 0.1889 0.2659
REMARK 3 8 3.0570 - 2.9239 1.00 2614 132 0.1921 0.2515
REMARK 3 9 2.9239 - 2.8114 1.00 2622 140 0.1969 0.2468
REMARK 3 10 2.8114 - 2.7144 1.00 2571 144 0.1964 0.2329
REMARK 3 11 2.7144 - 2.6295 1.00 2606 131 0.1965 0.2344
REMARK 3 12 2.6295 - 2.5543 1.00 2641 122 0.1928 0.2544
REMARK 3 13 2.5543 - 2.4871 1.00 2609 124 0.1900 0.2430
REMARK 3 14 2.4871 - 2.4264 1.00 2602 136 0.1980 0.2526
REMARK 3 15 2.4264 - 2.3712 1.00 2612 117 0.2062 0.2468
REMARK 3 16 2.3712 - 2.3208 1.00 2586 124 0.2096 0.2897
REMARK 3 17 2.3208 - 2.2743 1.00 2591 136 0.2060 0.2358
REMARK 3 18 2.2743 - 2.2314 1.00 2612 134 0.2089 0.2493
REMARK 3 19 2.2314 - 2.1916 1.00 2561 139 0.2177 0.2615
REMARK 3 20 2.1916 - 2.1544 1.00 2622 133 0.2236 0.2768
REMARK 3 21 2.1544 - 2.1197 1.00 2563 141 0.2298 0.2562
REMARK 3 22 2.1197 - 2.0871 1.00 2599 127 0.2497 0.2793
REMARK 3 23 2.0871 - 2.0564 1.00 2573 146 0.2617 0.3224
REMARK 3 24 2.0564 - 2.0274 1.00 2569 148 0.2781 0.3008
REMARK 3 25 2.0274 - 2.0000 1.00 2585 143 0.2848 0.3682
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.110
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 6073
REMARK 3 ANGLE : 0.664 8203
REMARK 3 CHIRALITY : 0.069 933
REMARK 3 PLANARITY : 0.003 1068
REMARK 3 DIHEDRAL : 11.912 3586
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2738 THROUGH 2944 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.5490 24.4530 45.2682
REMARK 3 T TENSOR
REMARK 3 T11: 0.4083 T22: 0.3644
REMARK 3 T33: 0.4995 T12: 0.0314
REMARK 3 T13: 0.0781 T23: 0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 2.8617 L22: 1.3966
REMARK 3 L33: 0.9368 L12: -0.7784
REMARK 3 L13: 0.0259 L23: 0.7586
REMARK 3 S TENSOR
REMARK 3 S11: -0.1463 S12: -0.2316 S13: 0.2932
REMARK 3 S21: 0.1089 S22: -0.0295 S23: 0.3194
REMARK 3 S31: -0.0119 S32: -0.1942 S33: 0.1907
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2945 THROUGH 3118 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6611 13.5968 24.4349
REMARK 3 T TENSOR
REMARK 3 T11: 0.3654 T22: 0.2787
REMARK 3 T33: 0.3480 T12: 0.0611
REMARK 3 T13: 0.0245 T23: 0.0388
REMARK 3 L TENSOR
REMARK 3 L11: 2.1467 L22: 1.5710
REMARK 3 L33: 2.2911 L12: 0.6100
REMARK 3 L13: -0.2121 L23: -0.0785
REMARK 3 S TENSOR
REMARK 3 S11: 0.0339 S12: 0.1732 S13: 0.1737
REMARK 3 S21: -0.0022 S22: 0.0544 S23: 0.0043
REMARK 3 S31: -0.1700 S32: -0.1168 S33: -0.0855
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2741 THROUGH 2760 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.2768 76.3114 17.2087
REMARK 3 T TENSOR
REMARK 3 T11: 0.6201 T22: 0.4362
REMARK 3 T33: 0.7123 T12: -0.0559
REMARK 3 T13: -0.1916 T23: 0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 5.7194 L22: 2.9397
REMARK 3 L33: 2.6032 L12: -0.9932
REMARK 3 L13: 0.9054 L23: 0.2374
REMARK 3 S TENSOR
REMARK 3 S11: -0.6380 S12: -0.4991 S13: 0.8213
REMARK 3 S21: 0.2140 S22: 0.0512 S23: -0.6968
REMARK 3 S31: -0.3235 S32: 0.1307 S33: 0.3351
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2761 THROUGH 2790 )
REMARK 3 ORIGIN FOR THE GROUP (A): -58.5444 73.5378 8.7945
REMARK 3 T TENSOR
REMARK 3 T11: 0.4795 T22: 0.7507
REMARK 3 T33: 0.4043 T12: 0.2172
REMARK 3 T13: -0.0819 T23: -0.1577
REMARK 3 L TENSOR
REMARK 3 L11: 3.4466 L22: 2.5209
REMARK 3 L33: 2.7027 L12: -0.5565
REMARK 3 L13: 1.1007 L23: -0.4234
REMARK 3 S TENSOR
REMARK 3 S11: -0.1272 S12: -0.5196 S13: 0.2233
REMARK 3 S21: 0.0785 S22: 0.1331 S23: 0.3556
REMARK 3 S31: -0.5896 S32: -0.9815 S33: 0.1481
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2791 THROUGH 2917 )
REMARK 3 ORIGIN FOR THE GROUP (A): -59.3303 68.4756 2.0967
REMARK 3 T TENSOR
REMARK 3 T11: 0.4077 T22: 0.6556
REMARK 3 T33: 0.3646 T12: 0.1275
REMARK 3 T13: -0.0590 T23: -0.0856
REMARK 3 L TENSOR
REMARK 3 L11: 3.1386 L22: 2.3383
REMARK 3 L33: 2.8841 L12: 0.4326
REMARK 3 L13: 0.8548 L23: 0.1525
REMARK 3 S TENSOR
REMARK 3 S11: -0.1870 S12: -0.0916 S13: 0.1565
REMARK 3 S21: -0.0377 S22: 0.0290 S23: 0.2463
REMARK 3 S31: -0.3155 S32: -0.7586 S33: 0.1559
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2918 THROUGH 2947 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.2646 70.1367 18.1615
REMARK 3 T TENSOR
REMARK 3 T11: 0.5243 T22: 0.5716
REMARK 3 T33: 0.3514 T12: 0.1266
REMARK 3 T13: -0.0657 T23: -0.1209
REMARK 3 L TENSOR
REMARK 3 L11: 2.8395 L22: 0.4638
REMARK 3 L33: 2.0335 L12: -0.8902
REMARK 3 L13: 1.1128 L23: -0.5897
REMARK 3 S TENSOR
REMARK 3 S11: -0.1844 S12: -0.0629 S13: 0.2106
REMARK 3 S21: 0.1265 S22: -0.0615 S23: 0.0592
REMARK 3 S31: -0.5708 S32: -0.7196 S33: 0.2326
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2948 THROUGH 3075 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.4848 50.9020 23.2802
REMARK 3 T TENSOR
REMARK 3 T11: 0.3575 T22: 0.3128
REMARK 3 T33: 0.3246 T12: -0.0404
REMARK 3 T13: -0.0322 T23: -0.0245
REMARK 3 L TENSOR
REMARK 3 L11: 2.4575 L22: 2.6399
REMARK 3 L33: 2.0048 L12: -1.0487
REMARK 3 L13: 0.0755 L23: 0.3493
REMARK 3 S TENSOR
REMARK 3 S11: -0.0077 S12: 0.0225 S13: -0.2517
REMARK 3 S21: 0.2408 S22: -0.1017 S23: 0.0418
REMARK 3 S31: 0.1550 S32: -0.0805 S33: 0.0843
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3076 THROUGH 3118 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.8703 58.3955 18.4980
REMARK 3 T TENSOR
REMARK 3 T11: 0.3663 T22: 0.4439
REMARK 3 T33: 0.3374 T12: -0.0180
REMARK 3 T13: -0.0313 T23: -0.0475
REMARK 3 L TENSOR
REMARK 3 L11: 2.8006 L22: 3.0802
REMARK 3 L33: 2.3520 L12: -1.0473
REMARK 3 L13: 0.5820 L23: 0.1417
REMARK 3 S TENSOR
REMARK 3 S11: 0.0988 S12: 0.2469 S13: -0.1234
REMARK 3 S21: -0.1580 S22: -0.2342 S23: 0.3538
REMARK 3 S31: -0.0332 S32: -0.4178 S33: 0.1798
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 5IK8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000218953.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68770
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 55.770
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.50
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 13.60
REMARK 200 R MERGE FOR SHELL (I) : 1.64000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1DYK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM AMMONIUM CITRATE DIABASIC 18%
REMARK 280 PEG3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y,-Z
REMARK 290 8555 X,-Y,-Z+1/2
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 55.77000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 63.14500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 55.77000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 63.14500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 55.77000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.14500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 72.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.14500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 55.77000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 72.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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 APPLY THE FOLLOWING TO CHAINS: B, 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 HOH B4338 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 B 2738
REMARK 465 PRO B 2739
REMARK 465 LEU B 2740
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 ARG A2766 CG CD NE CZ NH1 NH2
REMARK 470 ILE A2804 CG1 CG2 CD1
REMARK 470 GLU A2854 CG CD OE1 OE2
REMARK 470 LYS A2871 CG CD CE NZ
REMARK 470 MET B2742 CG SD CE
REMARK 470 LYS B2778 CD CE NZ
REMARK 470 LYS B2852 CG CD CE NZ
REMARK 470 ARG B2893 CG CD NE CZ NH1 NH2
REMARK 470 LYS B2953 CG CD CE NZ
REMARK 470 LYS B3095 CG CD CE NZ
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 B 2905 HG CYS B 2930 0.85
REMARK 500 O MET B 2742 H GLU B 2750 1.47
REMARK 500 O HOH A 4301 O HOH A 4340 2.03
REMARK 500 O HOH B 4319 O HOH B 4340 2.03
REMARK 500 OG2 FLC A 4005 O HOH A 4101 2.06
REMARK 500 O HOH A 4281 O HOH A 4334 2.09
REMARK 500 O HOH B 4123 O HOH B 4177 2.09
REMARK 500 O HOH A 4157 O HOH A 4281 2.09
REMARK 500 OD2 ASP B 2829 O HOH B 4101 2.11
REMARK 500 O HOH A 4312 O HOH A 4333 2.11
REMARK 500 OD2 ASP B 2824 NH2 ARG B 2894 2.11
REMARK 500 O HOH A 4288 O HOH A 4319 2.12
REMARK 500 O HOH B 4185 O HOH B 4336 2.13
REMARK 500 O3 XYS C 2 O5 BDP C 3 2.13
REMARK 500 OD1 ASN A 3070 O HOH A 4102 2.14
REMARK 500 O HOH B 4283 O HOH B 4325 2.15
REMARK 500 O HOH B 4180 O HOH B 4262 2.15
REMARK 500 O HOH A 4268 O HOH A 4336 2.16
REMARK 500 O HOH B 4104 O HOH B 4330 2.16
REMARK 500 OD1 ASP B 2917 O HOH B 4102 2.16
REMARK 500 O HOH A 4157 O HOH A 4313 2.19
REMARK 500 OE1 GLN B 2920 O HOH B 4103 2.19
REMARK 500 O HOH B 4111 O HOH B 4163 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 HD22 ASN A 3077 OG1 FLC A 4005 8555 1.59
REMARK 500 O HOH A 4289 O HOH B 4301 4555 2.06
REMARK 500 NZ LYS A 2980 OD1 ASP B 2829 4555 2.11
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 LYS A2852 -119.30 56.87
REMARK 500 ASP A2860 -112.46 55.42
REMARK 500 LYS A2870 -143.44 51.85
REMARK 500 ASN A2889 -3.22 76.86
REMARK 500 LYS A2980 -69.60 -101.77
REMARK 500 MET A2981 -45.64 -154.05
REMARK 500 GLU A3011 -45.96 79.77
REMARK 500 CYS A3017 49.26 -98.16
REMARK 500 LYS A3030 -106.60 59.05
REMARK 500 ASN A3057 58.07 -155.43
REMARK 500 HIS B2744 73.34 -112.74
REMARK 500 LYS B2852 -121.73 59.96
REMARK 500 ASP B2860 -118.50 52.95
REMARK 500 LYS B2870 -146.52 70.53
REMARK 500 ASN B2889 11.02 52.90
REMARK 500 ASP B2982 141.18 88.78
REMARK 500 GLU B3011 -49.97 76.70
REMARK 500 CYS B3017 52.43 -93.72
REMARK 500 LYS B3030 -112.91 56.81
REMARK 500 ASN B3057 60.63 -158.36
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 A4379 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH B4353 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH B4354 DISTANCE = 6.73 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A4001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A2808 OD2
REMARK 620 2 LEU A2825 O 78.4
REMARK 620 3 ILE A2874 O 89.3 79.0
REMARK 620 4 ASP A2876 OD2 95.1 167.8 90.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A4002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A2982 OD2
REMARK 620 2 ASN A2999 O 87.7
REMARK 620 3 SER A3053 O 78.1 86.7
REMARK 620 4 ASP A3055 OD2 84.0 169.4 85.2
REMARK 620 5 FLC A4004 OHB 141.9 116.8 128.7 73.7
REMARK 620 6 FLC A4004 OB2 152.9 83.9 75.8 100.6 63.5
REMARK 620 7 HOH A4131 O 73.9 79.6 149.2 104.3 82.0 129.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B4001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B2808 OD1
REMARK 620 2 ASP B2808 OD2 51.7
REMARK 620 3 LEU B2825 O 74.9 87.6
REMARK 620 4 ILE B2874 O 117.5 69.6 84.1
REMARK 620 5 ASP B2876 OD2 119.5 92.7 161.3 78.5
REMARK 620 6 XYS C 2 O4 68.0 119.7 78.0 159.1 117.5
REMARK 620 7 BDP C 3 O5 135.0 158.1 114.0 107.5 65.7 71.0
REMARK 620 8 BDP C 3 O6B 148.5 134.1 74.7 66.8 92.0 97.9 54.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B4002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B2982 OD2
REMARK 620 2 ASN B2999 O 86.2
REMARK 620 3 SER B3053 O 80.4 87.4
REMARK 620 4 ASP B3055 OD2 82.8 167.3 96.9
REMARK 620 5 FLC B4010 OB2 150.5 84.4 71.3 108.2
REMARK 620 6 FLC B4010 OHB 148.2 97.6 131.2 88.6 61.0
REMARK 620 7 HOH B4225 O 74.9 78.3 152.1 92.8 129.9 75.0
REMARK 620 N 1 2 3 4 5 6
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5IK7 RELATED DB: PDB
REMARK 900 THIS IS THE LIGAND BOUND FORM.
DBREF 5IK8 A 2742 3118 UNP Q60675 LAMA2_MOUSE 2742 3118
DBREF 5IK8 B 2742 3118 UNP Q60675 LAMA2_MOUSE 2742 3118
SEQADV 5IK8 ALA A 2738 UNP Q60675 EXPRESSION TAG
SEQADV 5IK8 PRO A 2739 UNP Q60675 EXPRESSION TAG
SEQADV 5IK8 LEU A 2740 UNP Q60675 EXPRESSION TAG
SEQADV 5IK8 ALA A 2741 UNP Q60675 EXPRESSION TAG
SEQADV 5IK8 GLU A 3011 UNP Q60675 GLY 3011 CONFLICT
SEQADV 5IK8 ALA B 2738 UNP Q60675 EXPRESSION TAG
SEQADV 5IK8 PRO B 2739 UNP Q60675 EXPRESSION TAG
SEQADV 5IK8 LEU B 2740 UNP Q60675 EXPRESSION TAG
SEQADV 5IK8 ALA B 2741 UNP Q60675 EXPRESSION TAG
SEQADV 5IK8 GLU B 3011 UNP Q60675 GLY 3011 CONFLICT
SEQRES 1 A 381 ALA PRO LEU ALA MET VAL HIS GLY PRO CYS VAL ALA GLU
SEQRES 2 A 381 SER GLU PRO ALA LEU LEU THR GLY SER LYS GLN PHE GLY
SEQRES 3 A 381 LEU SER ARG ASN SER HIS ILE ALA ILE ALA PHE ASP ASP
SEQRES 4 A 381 THR LYS VAL LYS ASN ARG LEU THR ILE GLU LEU GLU VAL
SEQRES 5 A 381 ARG THR GLU ALA GLU SER GLY LEU LEU PHE TYR MET ALA
SEQRES 6 A 381 ARG ILE ASN HIS ALA ASP PHE ALA THR VAL GLN LEU ARG
SEQRES 7 A 381 ASN GLY PHE PRO TYR PHE SER TYR ASP LEU GLY SER GLY
SEQRES 8 A 381 ASP THR SER THR MET ILE PRO THR LYS ILE ASN ASP GLY
SEQRES 9 A 381 GLN TRP HIS LYS ILE LYS ILE VAL ARG VAL LYS GLN GLU
SEQRES 10 A 381 GLY ILE LEU TYR VAL ASP ASP ALA SER SER GLN THR ILE
SEQRES 11 A 381 SER PRO LYS LYS ALA ASP ILE LEU ASP VAL VAL GLY ILE
SEQRES 12 A 381 LEU TYR VAL GLY GLY LEU PRO ILE ASN TYR THR THR ARG
SEQRES 13 A 381 ARG ILE GLY PRO VAL THR TYR SER LEU ASP GLY CYS VAL
SEQRES 14 A 381 ARG ASN LEU HIS MET GLU GLN ALA PRO VAL ASP LEU ASP
SEQRES 15 A 381 GLN PRO THR SER SER PHE HIS VAL GLY THR CYS PHE ALA
SEQRES 16 A 381 ASN ALA GLU SER GLY THR TYR PHE ASP GLY THR GLY PHE
SEQRES 17 A 381 ALA LYS ALA VAL GLY GLY PHE LYS VAL GLY LEU ASP LEU
SEQRES 18 A 381 LEU VAL GLU PHE GLU PHE ARG THR THR ARG PRO THR GLY
SEQRES 19 A 381 VAL LEU LEU GLY VAL SER SER GLN LYS MET ASP GLY MET
SEQRES 20 A 381 GLY ILE GLU MET ILE ASP GLU LYS LEU MET PHE HIS VAL
SEQRES 21 A 381 ASP ASN GLY ALA GLY ARG PHE THR ALA ILE TYR ASP ALA
SEQRES 22 A 381 GLU ILE PRO GLY HIS MET CYS ASN GLY GLN TRP HIS LYS
SEQRES 23 A 381 VAL THR ALA LYS LYS ILE LYS ASN ARG LEU GLU LEU VAL
SEQRES 24 A 381 VAL ASP GLY ASN GLN VAL ASP ALA GLN SER PRO ASN SER
SEQRES 25 A 381 ALA SER THR SER ALA ASP THR ASN ASP PRO VAL PHE VAL
SEQRES 26 A 381 GLY GLY PHE PRO GLY GLY LEU ASN GLN PHE GLY LEU THR
SEQRES 27 A 381 THR ASN ILE ARG PHE ARG GLY CYS ILE ARG SER LEU LYS
SEQRES 28 A 381 LEU THR LYS GLY THR GLY LYS PRO LEU GLU VAL ASN PHE
SEQRES 29 A 381 ALA LYS ALA LEU GLU LEU ARG GLY VAL GLN PRO VAL SER
SEQRES 30 A 381 CYS PRO THR THR
SEQRES 1 B 381 ALA PRO LEU ALA MET VAL HIS GLY PRO CYS VAL ALA GLU
SEQRES 2 B 381 SER GLU PRO ALA LEU LEU THR GLY SER LYS GLN PHE GLY
SEQRES 3 B 381 LEU SER ARG ASN SER HIS ILE ALA ILE ALA PHE ASP ASP
SEQRES 4 B 381 THR LYS VAL LYS ASN ARG LEU THR ILE GLU LEU GLU VAL
SEQRES 5 B 381 ARG THR GLU ALA GLU SER GLY LEU LEU PHE TYR MET ALA
SEQRES 6 B 381 ARG ILE ASN HIS ALA ASP PHE ALA THR VAL GLN LEU ARG
SEQRES 7 B 381 ASN GLY PHE PRO TYR PHE SER TYR ASP LEU GLY SER GLY
SEQRES 8 B 381 ASP THR SER THR MET ILE PRO THR LYS ILE ASN ASP GLY
SEQRES 9 B 381 GLN TRP HIS LYS ILE LYS ILE VAL ARG VAL LYS GLN GLU
SEQRES 10 B 381 GLY ILE LEU TYR VAL ASP ASP ALA SER SER GLN THR ILE
SEQRES 11 B 381 SER PRO LYS LYS ALA ASP ILE LEU ASP VAL VAL GLY ILE
SEQRES 12 B 381 LEU TYR VAL GLY GLY LEU PRO ILE ASN TYR THR THR ARG
SEQRES 13 B 381 ARG ILE GLY PRO VAL THR TYR SER LEU ASP GLY CYS VAL
SEQRES 14 B 381 ARG ASN LEU HIS MET GLU GLN ALA PRO VAL ASP LEU ASP
SEQRES 15 B 381 GLN PRO THR SER SER PHE HIS VAL GLY THR CYS PHE ALA
SEQRES 16 B 381 ASN ALA GLU SER GLY THR TYR PHE ASP GLY THR GLY PHE
SEQRES 17 B 381 ALA LYS ALA VAL GLY GLY PHE LYS VAL GLY LEU ASP LEU
SEQRES 18 B 381 LEU VAL GLU PHE GLU PHE ARG THR THR ARG PRO THR GLY
SEQRES 19 B 381 VAL LEU LEU GLY VAL SER SER GLN LYS MET ASP GLY MET
SEQRES 20 B 381 GLY ILE GLU MET ILE ASP GLU LYS LEU MET PHE HIS VAL
SEQRES 21 B 381 ASP ASN GLY ALA GLY ARG PHE THR ALA ILE TYR ASP ALA
SEQRES 22 B 381 GLU ILE PRO GLY HIS MET CYS ASN GLY GLN TRP HIS LYS
SEQRES 23 B 381 VAL THR ALA LYS LYS ILE LYS ASN ARG LEU GLU LEU VAL
SEQRES 24 B 381 VAL ASP GLY ASN GLN VAL ASP ALA GLN SER PRO ASN SER
SEQRES 25 B 381 ALA SER THR SER ALA ASP THR ASN ASP PRO VAL PHE VAL
SEQRES 26 B 381 GLY GLY PHE PRO GLY GLY LEU ASN GLN PHE GLY LEU THR
SEQRES 27 B 381 THR ASN ILE ARG PHE ARG GLY CYS ILE ARG SER LEU LYS
SEQRES 28 B 381 LEU THR LYS GLY THR GLY LYS PRO LEU GLU VAL ASN PHE
SEQRES 29 B 381 ALA LYS ALA LEU GLU LEU ARG GLY VAL GLN PRO VAL SER
SEQRES 30 B 381 CYS PRO THR THR
HET BDP C 1 19
HET XYS C 2 16
HET BDP C 3 19
HET XYS C 4 18
HET CA A4001 1
HET CA A4002 1
HET NAG A4003 27
HET FLC A4004 18
HET FLC A4005 18
HET EDO A4006 10
HET EDO A4007 10
HET EDO A4008 10
HET EDO A4009 10
HET EDO A4010 9
HET CA B4001 1
HET CA B4002 1
HET NAG B4003 27
HET 4MU B4004 20
HET FLC B4009 18
HET FLC B4010 18
HET EDO B4011 10
HET EDO B4012 10
HET EDO B4013 10
HET EDO B4014 10
HETNAM BDP BETA-D-GLUCOPYRANURONIC ACID
HETNAM XYS ALPHA-D-XYLOPYRANOSE
HETNAM CA CALCIUM ION
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FLC CITRATE ANION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM 4MU 7-HYDROXY-4-METHYL-2H-CHROMEN-2-ONE
HETSYN BDP BETA-D-GLUCURONIC ACID; D-GLUCURONIC ACID; GLUCURONIC
HETSYN 2 BDP ACID
HETSYN XYS ALPHA-D-XYLOSE; D-XYLOSE; XYLOSE; XYLOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN EDO ETHYLENE GLYCOL
HETSYN 4MU 4-METHYLUMBELLIFERONE
FORMUL 3 BDP 2(C6 H10 O7)
FORMUL 3 XYS 2(C5 H10 O5)
FORMUL 4 CA 4(CA 2+)
FORMUL 6 NAG 2(C8 H15 N O6)
FORMUL 7 FLC 4(C6 H5 O7 3-)
FORMUL 9 EDO 9(C2 H6 O2)
FORMUL 17 4MU C10 H8 O3
FORMUL 24 HOH *533(H2 O)
HELIX 1 AA1 ASP A 2775 LYS A 2780 5 6
HELIX 2 AA2 ASN A 3100 ALA A 3104 5 5
HELIX 3 AA3 ASP B 2775 LYS B 2780 5 6
HELIX 4 AA4 ASN B 3100 ALA B 3104 5 5
SHEET 1 AA1 6 LYS A2760 GLN A2761 0
SHEET 2 AA1 6 GLY A2904 MET A2911 -1 O VAL A2906 N LYS A2760
SHEET 3 AA1 6 ARG A2782 THR A2791 -1 N ARG A2790 O CYS A2905
SHEET 4 AA1 6 HIS A2844 VAL A2851 -1 O ILE A2846 N LEU A2787
SHEET 5 AA1 6 GLU A2854 VAL A2859 -1 O TYR A2858 N LYS A2847
SHEET 6 AA1 6 ALA A2862 ILE A2867 -1 O THR A2866 N GLY A2855
SHEET 1 AA2 7 ASP A2829 MET A2833 0
SHEET 2 AA2 7 PHE A2818 ASP A2824 -1 N PHE A2821 O THR A2832
SHEET 3 AA2 7 PHE A2809 ARG A2815 -1 N GLN A2813 O TYR A2820
SHEET 4 AA2 7 GLY A2796 ALA A2802 -1 N GLY A2796 O LEU A2814
SHEET 5 AA2 7 ILE A2880 VAL A2883 -1 O TYR A2882 N TYR A2800
SHEET 6 AA2 7 HIS A2769 ALA A2773 -1 N ILE A2772 O LEU A2881
SHEET 7 AA2 7 SER A2923 PHE A2925 -1 O SER A2923 N ALA A2771
SHEET 1 AA3 2 ALA A2934 SER A2936 0
SHEET 2 AA3 2 SER A3114 PRO A3116 -1 O CYS A3115 N GLU A2935
SHEET 1 AA4 8 ARG A3003 ASP A3009 0
SHEET 2 AA4 8 LYS A2992 ASP A2998 -1 N LEU A2993 O TYR A3008
SHEET 3 AA4 8 GLY A2983 ILE A2989 -1 N GLU A2987 O MET A2994
SHEET 4 AA4 8 GLY A2971 SER A2977 -1 N LEU A2974 O ILE A2986
SHEET 5 AA4 8 ASP A3058 VAL A3062 -1 O PHE A3061 N GLY A2975
SHEET 6 AA4 8 THR A2938 PHE A2952 -1 N ALA A2946 O VAL A3062
SHEET 7 AA4 8 ARG A3081 THR A3090 -1 O GLY A3082 N PHE A2940
SHEET 8 AA4 8 LEU A3097 GLU A3098 -1 O LEU A3097 N LEU A3089
SHEET 1 AA5 7 ASN A3040 GLN A3045 0
SHEET 2 AA5 7 ARG A3032 VAL A3037 -1 N LEU A3035 O VAL A3042
SHEET 3 AA5 7 HIS A3022 ILE A3029 -1 N LYS A3027 O GLU A3034
SHEET 4 AA5 7 ASP A2957 THR A2966 -1 N LEU A2958 O LYS A3028
SHEET 5 AA5 7 ARG A3081 THR A3090 -1 O LYS A3088 N GLU A2961
SHEET 6 AA5 7 THR A2938 PHE A2952 -1 N PHE A2940 O GLY A3082
SHEET 7 AA5 7 GLU A3106 GLN A3111 -1 O GLU A3106 N LYS A2947
SHEET 1 AA6 6 LYS B2760 GLN B2761 0
SHEET 2 AA6 6 GLY B2904 MET B2911 -1 O VAL B2906 N LYS B2760
SHEET 3 AA6 6 ARG B2782 THR B2791 -1 N ARG B2790 O CYS B2905
SHEET 4 AA6 6 HIS B2844 VAL B2851 -1 O ILE B2846 N LEU B2787
SHEET 5 AA6 6 GLU B2854 VAL B2859 -1 O TYR B2858 N LYS B2847
SHEET 6 AA6 6 ALA B2862 ILE B2867 -1 O SER B2864 N LEU B2857
SHEET 1 AA7 7 ASP B2829 MET B2833 0
SHEET 2 AA7 7 PHE B2818 ASP B2824 -1 N PHE B2821 O THR B2832
SHEET 3 AA7 7 PHE B2809 ARG B2815 -1 N GLN B2813 O TYR B2820
SHEET 4 AA7 7 GLY B2796 ALA B2802 -1 N GLY B2796 O LEU B2814
SHEET 5 AA7 7 ILE B2880 VAL B2883 -1 O TYR B2882 N TYR B2800
SHEET 6 AA7 7 HIS B2769 ALA B2773 -1 N ILE B2770 O VAL B2883
SHEET 7 AA7 7 SER B2923 PHE B2925 -1 O SER B2923 N ALA B2771
SHEET 1 AA8 2 ALA B2934 SER B2936 0
SHEET 2 AA8 2 SER B3114 PRO B3116 -1 O CYS B3115 N GLU B2935
SHEET 1 AA9 8 ARG B3003 ASP B3009 0
SHEET 2 AA9 8 LYS B2992 ASP B2998 -1 N LEU B2993 O TYR B3008
SHEET 3 AA9 8 GLY B2983 ILE B2989 -1 N GLU B2987 O MET B2994
SHEET 4 AA9 8 GLY B2971 SER B2977 -1 N LEU B2974 O ILE B2986
SHEET 5 AA9 8 ASP B3058 VAL B3062 -1 O PHE B3061 N GLY B2975
SHEET 6 AA9 8 THR B2938 PHE B2952 -1 N ALA B2946 O VAL B3062
SHEET 7 AA9 8 ARG B3081 THR B3090 -1 O GLY B3082 N PHE B2940
SHEET 8 AA9 8 LEU B3097 GLU B3098 -1 O LEU B3097 N LEU B3089
SHEET 1 AB1 7 ASN B3040 GLN B3045 0
SHEET 2 AB1 7 ARG B3032 VAL B3037 -1 N LEU B3035 O VAL B3042
SHEET 3 AB1 7 HIS B3022 ILE B3029 -1 N ILE B3029 O ARG B3032
SHEET 4 AB1 7 ASP B2957 THR B2966 -1 N LEU B2958 O LYS B3028
SHEET 5 AB1 7 ARG B3081 THR B3090 -1 O LYS B3088 N GLU B2961
SHEET 6 AB1 7 THR B2938 PHE B2952 -1 N PHE B2940 O GLY B3082
SHEET 7 AB1 7 GLU B3106 GLN B3111 -1 O GLU B3106 N LYS B2947
SSBOND 1 CYS A 2747 CYS A 3017 1555 1555 2.03
SSBOND 2 CYS A 2905 CYS A 2930 1555 1555 2.03
SSBOND 3 CYS A 3083 CYS A 3115 1555 1555 2.04
SSBOND 4 CYS B 2747 CYS B 3017 1555 1555 2.03
SSBOND 5 CYS B 2905 CYS B 2930 1555 1555 2.04
SSBOND 6 CYS B 3083 CYS B 3115 1555 1555 2.04
LINK ND2 ASN A2889 C1 NAG A4003 1555 1555 1.45
LINK ND2 ASN B2889 C1 NAG B4003 1555 1555 1.44
LINK O1' 4MU B4004 C1 BDP C 1 1555 1555 1.44
LINK O3 BDP C 1 C1 XYS C 2 1555 1555 1.44
LINK O3 XYS C 2 C1 BDP C 3 1555 1555 1.43
LINK O3 BDP C 3 C1 XYS C 4 1555 1555 1.43
LINK OD2 ASP A2808 CA CA A4001 1555 1555 2.38
LINK O LEU A2825 CA CA A4001 1555 1555 2.43
LINK O ILE A2874 CA CA A4001 1555 1555 2.41
LINK OD2 ASP A2876 CA CA A4001 1555 1555 2.36
LINK OD2 ASP A2982 CA CA A4002 1555 1555 2.31
LINK O ASN A2999 CA CA A4002 1555 1555 2.37
LINK O SER A3053 CA CA A4002 1555 1555 2.36
LINK OD2 ASP A3055 CA CA A4002 1555 1555 2.34
LINK CA CA A4002 OHB FLC A4004 1555 1555 2.50
LINK CA CA A4002 OB2 FLC A4004 1555 1555 2.37
LINK CA CA A4002 O HOH A4131 1555 1555 2.42
LINK OD1 ASP B2808 CA CA B4001 1555 1555 2.66
LINK OD2 ASP B2808 CA CA B4001 1555 1555 2.28
LINK O LEU B2825 CA CA B4001 1555 1555 2.32
LINK O ILE B2874 CA CA B4001 1555 1555 2.56
LINK OD2 ASP B2876 CA CA B4001 1555 1555 2.45
LINK OD2 ASP B2982 CA CA B4002 1555 1555 2.38
LINK O ASN B2999 CA CA B4002 1555 1555 2.40
LINK O SER B3053 CA CA B4002 1555 1555 2.33
LINK OD2 ASP B3055 CA CA B4002 1555 1555 2.42
LINK CA CA B4001 O4 XYS C 2 1555 1555 1.95
LINK CA CA B4001 O5 BDP C 3 1555 1555 2.98
LINK CA CA B4001 O6B BDP C 3 1555 1555 2.53
LINK CA CA B4002 OB2 FLC B4010 1555 1555 2.56
LINK CA CA B4002 OHB FLC B4010 1555 1555 2.58
LINK CA CA B4002 O HOH B4225 1555 1555 2.38
CRYST1 111.540 126.290 144.000 90.00 90.00 90.00 I 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 0.008965 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007918 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006944 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
