HEADER VIRAL PROTEIN/IMMUNE SYSTEM 14-NOV-13 4NM8
TITLE CRYSTAL STRUCTURE OF BROADLY NEUTRALIZING ANTIBODY CR8043 BOUND TO H3
TITLE 2 INFLUENZA HEMAGGLUTININ
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMAGGLUTININ HA1 CHAIN;
COMPND 3 CHAIN: A, C, E;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HEMAGGLUTININ HA2 CHAIN;
COMPND 7 CHAIN: B, D, F;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: ANTIBODY CR8043, LIGHT CHAIN;
COMPND 11 CHAIN: L, M, N;
COMPND 12 SYNONYM: IMMUNOGLOBULIN KAPPA LIGHT CHAIN EU;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 4;
COMPND 15 MOLECULE: ANTIBODY CR8043, HEAVY CHAIN;
COMPND 16 CHAIN: H, I, J;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (STRAIN A/HONG KONG/1/1968
SOURCE 3 H3N2);
SOURCE 4 ORGANISM_TAXID: 506350;
SOURCE 5 STRAIN: A/HONG KONG/1/1968 H3N2;
SOURCE 6 GENE: HA;
SOURCE 7 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (STRAIN A/HONG KONG/1/1968
SOURCE 11 H3N2);
SOURCE 12 ORGANISM_TAXID: 506350;
SOURCE 13 STRAIN: A/HONG KONG/1/1968 H3N2;
SOURCE 14 GENE: HA;
SOURCE 15 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 19 ORGANISM_COMMON: HUMAN, HUMAN;
SOURCE 20 ORGANISM_TAXID: 9606;
SOURCE 21 GENE: IGKC;
SOURCE 22 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 24 MOL_ID: 4;
SOURCE 25 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 26 ORGANISM_COMMON: HUMAN, HUMAN;
SOURCE 27 ORGANISM_TAXID: 9606;
SOURCE 28 GENE: DKFZP686I15212, DKFZP686P15220;
SOURCE 29 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 30 EXPRESSION_SYSTEM_TAXID: 7111
KEYWDS VIRAL FUSION PROTEIN, IMMUNOGLOBULIN, VIRUS ATTACHMENT AND ENTRY,
KEYWDS 2 IMMUNE RECOGNITION, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX,
KEYWDS 3 IMMUNOGLOBULIN'
EXPDTA X-RAY DIFFRACTION
AUTHOR P.S.LEE,I.A.WILSON
REVDAT 6 20-SEP-23 4NM8 1 HETSYN
REVDAT 5 29-JUL-20 4NM8 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 06-DEC-17 4NM8 1 REMARK
REVDAT 3 21-JUN-17 4NM8 1 DBREF
REVDAT 2 22-JAN-14 4NM8 1 JRNL
REVDAT 1 25-DEC-13 4NM8 0
JRNL AUTH R.H.FRIESEN,P.S.LEE,E.J.STOOP,R.M.HOFFMAN,D.C.EKIERT,
JRNL AUTH 2 G.BHABHA,W.YU,J.JURASZEK,W.KOUDSTAAL,M.JONGENEELEN,
JRNL AUTH 3 H.J.KORSE,C.OPHORST,E.C.BRINKMAN-VAN DER LINDEN,M.THROSBY,
JRNL AUTH 4 M.J.KWAKKENBOS,A.Q.BAKKER,T.BEAUMONT,H.SPITS,T.KWAKS,
JRNL AUTH 5 R.VOGELS,A.B.WARD,J.GOUDSMIT,I.A.WILSON
JRNL TITL A COMMON SOLUTION TO GROUP 2 INFLUENZA VIRUS NEUTRALIZATION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 111 445 2014
JRNL REFN ISSN 0027-8424
JRNL PMID 24335589
JRNL DOI 10.1073/PNAS.1319058110
REMARK 2
REMARK 2 RESOLUTION. 4.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
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) : 4.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 34531
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.242
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.292
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1730
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 43.8237 - 9.1416 0.97 2790 151 0.2366 0.2872
REMARK 3 2 9.1416 - 7.2667 0.98 2746 169 0.2231 0.2761
REMARK 3 3 7.2667 - 6.3513 1.00 2800 158 0.2442 0.3103
REMARK 3 4 6.3513 - 5.7720 0.98 2753 124 0.2412 0.3223
REMARK 3 5 5.7720 - 5.3591 0.99 2776 140 0.2352 0.2772
REMARK 3 6 5.3591 - 5.0436 0.99 2784 129 0.2246 0.2896
REMARK 3 7 5.0436 - 4.7913 1.00 2799 145 0.2354 0.2737
REMARK 3 8 4.7913 - 4.5830 0.97 2739 143 0.2373 0.2774
REMARK 3 9 4.5830 - 4.4067 0.98 2708 152 0.2381 0.2894
REMARK 3 10 4.4067 - 4.2548 0.99 2774 142 0.2508 0.3070
REMARK 3 11 4.2548 - 4.1218 0.99 2767 136 0.2681 0.3101
REMARK 3 12 4.1218 - 4.0041 0.85 2365 141 0.2962 0.3386
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) : 0.550
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.610
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 92.50
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 : 0.006 22207
REMARK 3 ANGLE : 1.227 30148
REMARK 3 CHIRALITY : 0.078 3378
REMARK 3 PLANARITY : 0.006 3860
REMARK 3 DIHEDRAL : 16.276 8067
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A OR CHAIN B OR CHAIN C OR CHAIN D OR CHAIN E
REMARK 3 OR CHAIN F
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9309 10.0932 41.1245
REMARK 3 T TENSOR
REMARK 3 T11: 0.1626 T22: 0.2801
REMARK 3 T33: 0.3797 T12: -0.0617
REMARK 3 T13: -0.0026 T23: -0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 0.2559 L22: 0.5955
REMARK 3 L33: 0.5536 L12: -0.1296
REMARK 3 L13: -0.0428 L23: -0.0695
REMARK 3 S TENSOR
REMARK 3 S11: -0.0585 S12: 0.0494 S13: 0.0559
REMARK 3 S21: 0.0233 S22: 0.0035 S23: -0.2257
REMARK 3 S31: -0.0337 S32: 0.1954 S33: 0.0193
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN H AND RESID 1:121 OR CHAIN L AND RESID 1:114
REMARK 3 ORIGIN FOR THE GROUP (A): -28.6797 53.8479 37.2112
REMARK 3 T TENSOR
REMARK 3 T11: 0.4247 T22: 0.2573
REMARK 3 T33: 0.3722 T12: 0.0879
REMARK 3 T13: -0.1771 T23: 0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 1.1024 L22: 0.8778
REMARK 3 L33: 1.1807 L12: -0.3210
REMARK 3 L13: 0.1435 L23: -0.2474
REMARK 3 S TENSOR
REMARK 3 S11: -0.0523 S12: 0.2871 S13: 0.3905
REMARK 3 S21: -0.2744 S22: -0.0278 S23: -0.0283
REMARK 3 S31: -0.2659 S32: -0.1079 S33: 0.0431
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN H AND RESID 122:213 OR CHAIN L AND RESID
REMARK 3 115:211
REMARK 3 ORIGIN FOR THE GROUP (A): -20.1789 85.4533 26.9066
REMARK 3 T TENSOR
REMARK 3 T11: 1.5198 T22: 0.7201
REMARK 3 T33: 1.4158 T12: -0.2449
REMARK 3 T13: -0.0335 T23: 0.3042
REMARK 3 L TENSOR
REMARK 3 L11: 1.1024 L22: 0.6522
REMARK 3 L33: 0.4148 L12: 0.2694
REMARK 3 L13: 0.3565 L23: 0.5056
REMARK 3 S TENSOR
REMARK 3 S11: -0.1507 S12: 0.5738 S13: 0.9215
REMARK 3 S21: -0.2242 S22: 0.2584 S23: -0.2219
REMARK 3 S31: -0.9483 S32: 0.0431 S33: -0.0892
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN I AND RESID 1:121 OR CHAIN M AND RESID 1:114
REMARK 3 ORIGIN FOR THE GROUP (A): -27.4465 -7.3185 82.4404
REMARK 3 T TENSOR
REMARK 3 T11: 0.4879 T22: 0.3322
REMARK 3 T33: 0.2369 T12: 0.1248
REMARK 3 T13: 0.1731 T23: 0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 0.7092 L22: 0.6861
REMARK 3 L33: 0.8784 L12: -0.1282
REMARK 3 L13: -0.2379 L23: 0.3103
REMARK 3 S TENSOR
REMARK 3 S11: 0.0271 S12: -0.2751 S13: 0.1150
REMARK 3 S21: 0.2762 S22: 0.0773 S23: 0.1479
REMARK 3 S31: -0.0672 S32: 0.0063 S33: 0.0246
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN I AND RESID 122:213 OR CHAIN M AND RESID
REMARK 3 115:211
REMARK 3 ORIGIN FOR THE GROUP (A): -18.1730 -13.9497 114.7687
REMARK 3 T TENSOR
REMARK 3 T11: 1.6978 T22: 1.4738
REMARK 3 T33: 0.6472 T12: 0.1798
REMARK 3 T13: -0.2514 T23: 0.0563
REMARK 3 L TENSOR
REMARK 3 L11: 0.9357 L22: 0.2883
REMARK 3 L33: 0.2273 L12: -0.0727
REMARK 3 L13: -0.2286 L23: -0.1337
REMARK 3 S TENSOR
REMARK 3 S11: -0.0078 S12: -0.9948 S13: -0.0296
REMARK 3 S21: 0.8913 S22: -0.2960 S23: -0.2888
REMARK 3 S31: 0.3940 S32: 0.2433 S33: 0.2687
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN J AND RESID 1:121 OR CHAIN N AND RESID 1:114
REMARK 3 ORIGIN FOR THE GROUP (A): -29.5611 -15.9570 6.5667
REMARK 3 T TENSOR
REMARK 3 T11: 0.3633 T22: 0.3778
REMARK 3 T33: 0.3522 T12: -0.1823
REMARK 3 T13: -0.0107 T23: -0.0301
REMARK 3 L TENSOR
REMARK 3 L11: 1.2275 L22: 2.0885
REMARK 3 L33: 0.6185 L12: 0.3815
REMARK 3 L13: -0.1945 L23: -0.3960
REMARK 3 S TENSOR
REMARK 3 S11: -0.0453 S12: 0.1503 S13: -0.2671
REMARK 3 S21: -0.2715 S22: -0.0342 S23: -0.0419
REMARK 3 S31: 0.4331 S32: -0.2475 S33: 0.0241
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN J AND RESID 122:213 OR CHAIN N AND RESID
REMARK 3 115:211
REMARK 3 ORIGIN FOR THE GROUP (A): -21.8725 -40.6146 -16.1887
REMARK 3 T TENSOR
REMARK 3 T11: 1.7548 T22: 1.0410
REMARK 3 T33: 1.2374 T12: 0.0470
REMARK 3 T13: 0.3695 T23: -0.5404
REMARK 3 L TENSOR
REMARK 3 L11: 0.5118 L22: 0.3623
REMARK 3 L33: 0.3854 L12: -0.0549
REMARK 3 L13: -0.1853 L23: -0.1048
REMARK 3 S TENSOR
REMARK 3 S11: -0.0119 S12: 0.4195 S13: -0.7242
REMARK 3 S21: -0.2388 S22: -0.0560 S23: 0.3094
REMARK 3 S31: 0.7859 S32: 0.3209 S33: 0.0850
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 4NM8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1000083378.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97950
REMARK 200 MONOCHROMATOR : LIQUID NITROGEN-COOLED DOUBLE
REMARK 200 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34622
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.000
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 (%) : 97.7
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.20100
REMARK 200 R SYM (I) : 0.20100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.82600
REMARK 200 R SYM FOR SHELL (I) : 0.82600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: PDB ENTRY 4FNK, 4NM4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2 M AMMONIUM SULFATE, 0.1 M SODIUM
REMARK 280 ACETATE PH 5.5, 3% PEG 400, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 120.74550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 71.17750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 120.74550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 71.17750
REMARK 290 SMTRY3 4 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: DODECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, L, H, M, I,
REMARK 350 AND CHAINS: N, J, G, K, O, P, Q, R
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 7
REMARK 465 ASP A 8
REMARK 465 GLN A 327
REMARK 465 THR A 328
REMARK 465 ARG A 329
REMARK 465 ILE B 173
REMARK 465 LYS B 174
REMARK 465 GLY B 175
REMARK 465 VAL B 176
REMARK 465 ALA C 7
REMARK 465 ASP C 8
REMARK 465 GLN C 327
REMARK 465 THR C 328
REMARK 465 ARG C 329
REMARK 465 GLN D 172
REMARK 465 ILE D 173
REMARK 465 LYS D 174
REMARK 465 GLY D 175
REMARK 465 VAL D 176
REMARK 465 ALA E 7
REMARK 465 ASP E 8
REMARK 465 LYS E 326
REMARK 465 GLN E 327
REMARK 465 THR E 328
REMARK 465 ARG E 329
REMARK 465 GLN F 172
REMARK 465 ILE F 173
REMARK 465 LYS F 174
REMARK 465 GLY F 175
REMARK 465 VAL F 176
REMARK 465 GLY L 212
REMARK 465 GLU L 213
REMARK 465 CYS L 214
REMARK 465 SER H 127
REMARK 465 SER H 128
REMARK 465 LYS H 129
REMARK 465 SER H 130
REMARK 465 THR H 131
REMARK 465 SER H 132
REMARK 465 LYS H 214
REMARK 465 SER H 215
REMARK 465 CYS H 216
REMARK 465 HIS H 217
REMARK 465 HIS H 218
REMARK 465 HIS H 219
REMARK 465 HIS H 220
REMARK 465 HIS H 221
REMARK 465 HIS H 222
REMARK 465 GLY M 212
REMARK 465 GLU M 213
REMARK 465 CYS M 214
REMARK 465 ALA I 125
REMARK 465 PRO I 126
REMARK 465 SER I 127
REMARK 465 SER I 128
REMARK 465 LYS I 129
REMARK 465 SER I 130
REMARK 465 THR I 131
REMARK 465 SER I 132
REMARK 465 GLY I 133
REMARK 465 GLY I 134
REMARK 465 LYS I 214
REMARK 465 SER I 215
REMARK 465 CYS I 216
REMARK 465 HIS I 217
REMARK 465 HIS I 218
REMARK 465 HIS I 219
REMARK 465 HIS I 220
REMARK 465 HIS I 221
REMARK 465 HIS I 222
REMARK 465 GLY N 212
REMARK 465 GLU N 213
REMARK 465 CYS N 214
REMARK 465 SER J 127
REMARK 465 SER J 128
REMARK 465 LYS J 129
REMARK 465 SER J 130
REMARK 465 THR J 131
REMARK 465 SER J 132
REMARK 465 GLY J 133
REMARK 465 GLY J 134
REMARK 465 LYS J 214
REMARK 465 SER J 215
REMARK 465 CYS J 216
REMARK 465 HIS J 217
REMARK 465 HIS J 218
REMARK 465 HIS J 219
REMARK 465 HIS J 220
REMARK 465 HIS J 221
REMARK 465 HIS J 222
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU B 52 CB - CG - CD2 ANGL. DEV. = -13.9 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 ILE A 62 -114.33 50.01
REMARK 500 ASN A 96 42.86 -145.00
REMARK 500 CYS A 97 -155.15 -138.59
REMARK 500 VAL A 196 -56.76 67.83
REMARK 500 THR A 206 -167.74 -119.24
REMARK 500 GLU A 325 168.39 73.72
REMARK 500 ALA B 5 -66.61 -92.64
REMARK 500 LYS B 58 75.07 50.36
REMARK 500 PHE B 63 -108.08 -120.65
REMARK 500 GLN B 65 -140.82 -127.89
REMARK 500 ARG B 127 -124.54 52.28
REMARK 500 TYR B 141 38.14 -95.86
REMARK 500 ILE C 62 -113.14 50.37
REMARK 500 ASN C 96 42.96 -144.73
REMARK 500 CYS C 97 -155.82 -138.95
REMARK 500 VAL C 196 -56.93 68.04
REMARK 500 THR C 206 -168.23 -119.98
REMARK 500 ALA D 5 -66.24 -92.43
REMARK 500 LYS D 58 75.62 49.99
REMARK 500 PHE D 63 -108.15 -120.24
REMARK 500 GLN D 65 -140.37 -127.76
REMARK 500 ARG D 127 -124.18 52.07
REMARK 500 TYR D 141 38.55 -95.23
REMARK 500 ILE E 62 -113.41 49.92
REMARK 500 ASN E 96 43.27 -144.92
REMARK 500 CYS E 97 -155.37 -138.53
REMARK 500 VAL E 196 -57.72 67.76
REMARK 500 THR E 206 -168.16 -118.97
REMARK 500 ALA F 5 -66.57 -92.91
REMARK 500 LYS F 58 75.58 50.37
REMARK 500 PHE F 63 -108.28 -120.69
REMARK 500 GLN F 65 -140.89 -127.88
REMARK 500 ARG F 127 -123.84 52.51
REMARK 500 TYR F 141 38.66 -95.56
REMARK 500 SER L 51 -24.56 59.41
REMARK 500 ALA L 84 -177.35 -173.37
REMARK 500 LYS L 188 -29.70 -144.12
REMARK 500 ASP H 99 -7.04 92.26
REMARK 500 ALA H 100 -5.66 77.42
REMARK 500 SER M 51 -24.37 59.34
REMARK 500 ALA M 84 -177.41 -173.42
REMARK 500 LYS M 188 -29.50 -144.13
REMARK 500 ASP I 99 -7.02 89.53
REMARK 500 ALA I 100 -6.02 77.11
REMARK 500 SER N 51 -24.69 59.56
REMARK 500 ALA N 84 -177.09 -173.49
REMARK 500 LYS N 188 -29.84 -144.11
REMARK 500 ASP J 99 -6.34 93.70
REMARK 500 ALA J 100 -4.52 76.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 57 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NM4 RELATED DB: PDB
REMARK 900 RELATED ID: EMD-5793 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-5794 RELATED DB: EMDB
DBREF 4NM8 A 11 329 UNP Q91MA7 HEMA_I68A4 27 345
DBREF 4NM8 B 1 176 UNP Q91MA7 HEMA_I68A4 346 521
DBREF 4NM8 C 11 329 UNP Q91MA7 HEMA_I68A4 27 345
DBREF 4NM8 D 1 176 UNP Q91MA7 HEMA_I68A4 346 521
DBREF 4NM8 E 11 329 UNP Q91MA7 HEMA_I68A4 27 345
DBREF 4NM8 F 1 176 UNP Q91MA7 HEMA_I68A4 346 521
DBREF 4NM8 L 1 114 PDB 4NM8 4NM8 1 114
DBREF 4NM8 L 115 214 UNP P0DOX7 IGK_HUMAN 115 214
DBREF 4NM8 H 1 121 PDB 4NM8 4NM8 1 121
DBREF 4NM8 H 122 216 UNP Q6N089 Q6N089_HUMAN 151 245
DBREF 4NM8 M 1 114 PDB 4NM8 4NM8 1 114
DBREF 4NM8 M 115 214 UNP P0DOX7 IGK_HUMAN 115 214
DBREF 4NM8 I 1 121 PDB 4NM8 4NM8 1 121
DBREF 4NM8 I 122 216 UNP Q6N089 Q6N089_HUMAN 151 245
DBREF 4NM8 N 1 114 PDB 4NM8 4NM8 1 114
DBREF 4NM8 N 115 214 UNP P0DOX7 IGK_HUMAN 115 214
DBREF 4NM8 J 1 121 PDB 4NM8 4NM8 1 121
DBREF 4NM8 J 122 216 UNP Q6N089 Q6N089_HUMAN 151 245
SEQADV 4NM8 ALA A 7 UNP Q91MA7 EXPRESSION TAG
SEQADV 4NM8 ASP A 8 UNP Q91MA7 EXPRESSION TAG
SEQADV 4NM8 PRO A 9 UNP Q91MA7 EXPRESSION TAG
SEQADV 4NM8 GLY A 10 UNP Q91MA7 EXPRESSION TAG
SEQADV 4NM8 GLY B 123 UNP Q91MA7 ARG 468 CONFLICT
SEQADV 4NM8 ALA C 7 UNP Q91MA7 EXPRESSION TAG
SEQADV 4NM8 ASP C 8 UNP Q91MA7 EXPRESSION TAG
SEQADV 4NM8 PRO C 9 UNP Q91MA7 EXPRESSION TAG
SEQADV 4NM8 GLY C 10 UNP Q91MA7 EXPRESSION TAG
SEQADV 4NM8 GLY D 123 UNP Q91MA7 ARG 468 CONFLICT
SEQADV 4NM8 ALA E 7 UNP Q91MA7 EXPRESSION TAG
SEQADV 4NM8 ASP E 8 UNP Q91MA7 EXPRESSION TAG
SEQADV 4NM8 PRO E 9 UNP Q91MA7 EXPRESSION TAG
SEQADV 4NM8 GLY E 10 UNP Q91MA7 EXPRESSION TAG
SEQADV 4NM8 GLY F 123 UNP Q91MA7 ARG 468 CONFLICT
SEQADV 4NM8 HIS H 217 UNP Q6N089 EXPRESSION TAG
SEQADV 4NM8 HIS H 218 UNP Q6N089 EXPRESSION TAG
SEQADV 4NM8 HIS H 219 UNP Q6N089 EXPRESSION TAG
SEQADV 4NM8 HIS H 220 UNP Q6N089 EXPRESSION TAG
SEQADV 4NM8 HIS H 221 UNP Q6N089 EXPRESSION TAG
SEQADV 4NM8 HIS H 222 UNP Q6N089 EXPRESSION TAG
SEQADV 4NM8 HIS I 217 UNP Q6N089 EXPRESSION TAG
SEQADV 4NM8 HIS I 218 UNP Q6N089 EXPRESSION TAG
SEQADV 4NM8 HIS I 219 UNP Q6N089 EXPRESSION TAG
SEQADV 4NM8 HIS I 220 UNP Q6N089 EXPRESSION TAG
SEQADV 4NM8 HIS I 221 UNP Q6N089 EXPRESSION TAG
SEQADV 4NM8 HIS I 222 UNP Q6N089 EXPRESSION TAG
SEQADV 4NM8 HIS J 217 UNP Q6N089 EXPRESSION TAG
SEQADV 4NM8 HIS J 218 UNP Q6N089 EXPRESSION TAG
SEQADV 4NM8 HIS J 219 UNP Q6N089 EXPRESSION TAG
SEQADV 4NM8 HIS J 220 UNP Q6N089 EXPRESSION TAG
SEQADV 4NM8 HIS J 221 UNP Q6N089 EXPRESSION TAG
SEQADV 4NM8 HIS J 222 UNP Q6N089 EXPRESSION TAG
SEQRES 1 A 323 ALA ASP PRO GLY ALA THR LEU CYS LEU GLY HIS HIS ALA
SEQRES 2 A 323 VAL PRO ASN GLY THR LEU VAL LYS THR ILE THR ASP ASP
SEQRES 3 A 323 GLN ILE GLU VAL THR ASN ALA THR GLU LEU VAL GLN SER
SEQRES 4 A 323 SER SER THR GLY LYS ILE CYS ASN ASN PRO HIS ARG ILE
SEQRES 5 A 323 LEU ASP GLY ILE ASP CYS THR LEU ILE ASP ALA LEU LEU
SEQRES 6 A 323 GLY ASP PRO HIS CYS ASP VAL PHE GLN ASN GLU THR TRP
SEQRES 7 A 323 ASP LEU PHE VAL GLU ARG SER LYS ALA PHE SER ASN CYS
SEQRES 8 A 323 TYR PRO TYR ASP VAL PRO ASP TYR ALA SER LEU ARG SER
SEQRES 9 A 323 LEU VAL ALA SER SER GLY THR LEU GLU PHE ILE THR GLU
SEQRES 10 A 323 GLY PHE THR TRP THR GLY VAL THR GLN ASN GLY GLY SER
SEQRES 11 A 323 ASN ALA CYS LYS ARG GLY PRO GLY SER GLY PHE PHE SER
SEQRES 12 A 323 ARG LEU ASN TRP LEU THR LYS SER GLY SER THR TYR PRO
SEQRES 13 A 323 VAL LEU ASN VAL THR MET PRO ASN ASN ASP ASN PHE ASP
SEQRES 14 A 323 LYS LEU TYR ILE TRP GLY VAL HIS HIS PRO SER THR ASN
SEQRES 15 A 323 GLN GLU GLN THR SER LEU TYR VAL GLN ALA SER GLY ARG
SEQRES 16 A 323 VAL THR VAL SER THR ARG ARG SER GLN GLN THR ILE ILE
SEQRES 17 A 323 PRO ASN ILE GLY SER ARG PRO TRP VAL ARG GLY LEU SER
SEQRES 18 A 323 SER ARG ILE SER ILE TYR TRP THR ILE VAL LYS PRO GLY
SEQRES 19 A 323 ASP VAL LEU VAL ILE ASN SER ASN GLY ASN LEU ILE ALA
SEQRES 20 A 323 PRO ARG GLY TYR PHE LYS MET ARG THR GLY LYS SER SER
SEQRES 21 A 323 ILE MET ARG SER ASP ALA PRO ILE ASP THR CYS ILE SER
SEQRES 22 A 323 GLU CYS ILE THR PRO ASN GLY SER ILE PRO ASN ASP LYS
SEQRES 23 A 323 PRO PHE GLN ASN VAL ASN LYS ILE THR TYR GLY ALA CYS
SEQRES 24 A 323 PRO LYS TYR VAL LYS GLN ASN THR LEU LYS LEU ALA THR
SEQRES 25 A 323 GLY MET ARG ASN VAL PRO GLU LYS GLN THR ARG
SEQRES 1 B 176 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU ASN GLY
SEQRES 2 B 176 TRP GLU GLY MET ILE ASP GLY TRP TYR GLY PHE ARG HIS
SEQRES 3 B 176 GLN ASN SER GLU GLY THR GLY GLN ALA ALA ASP LEU LYS
SEQRES 4 B 176 SER THR GLN ALA ALA ILE ASP GLN ILE ASN GLY LYS LEU
SEQRES 5 B 176 ASN ARG VAL ILE GLU LYS THR ASN GLU LYS PHE HIS GLN
SEQRES 6 B 176 ILE GLU LYS GLU PHE SER GLU VAL GLU GLY ARG ILE GLN
SEQRES 7 B 176 ASP LEU GLU LYS TYR VAL GLU ASP THR LYS ILE ASP LEU
SEQRES 8 B 176 TRP SER TYR ASN ALA GLU LEU LEU VAL ALA LEU GLU ASN
SEQRES 9 B 176 GLN HIS THR ILE ASP LEU THR ASP SER GLU MET ASN LYS
SEQRES 10 B 176 LEU PHE GLU LYS THR GLY ARG GLN LEU ARG GLU ASN ALA
SEQRES 11 B 176 GLU ASP MET GLY ASN GLY CYS PHE LYS ILE TYR HIS LYS
SEQRES 12 B 176 CYS ASP ASN ALA CYS ILE GLU SER ILE ARG ASN GLY THR
SEQRES 13 B 176 TYR ASP HIS ASP VAL TYR ARG ASP GLU ALA LEU ASN ASN
SEQRES 14 B 176 ARG PHE GLN ILE LYS GLY VAL
SEQRES 1 C 323 ALA ASP PRO GLY ALA THR LEU CYS LEU GLY HIS HIS ALA
SEQRES 2 C 323 VAL PRO ASN GLY THR LEU VAL LYS THR ILE THR ASP ASP
SEQRES 3 C 323 GLN ILE GLU VAL THR ASN ALA THR GLU LEU VAL GLN SER
SEQRES 4 C 323 SER SER THR GLY LYS ILE CYS ASN ASN PRO HIS ARG ILE
SEQRES 5 C 323 LEU ASP GLY ILE ASP CYS THR LEU ILE ASP ALA LEU LEU
SEQRES 6 C 323 GLY ASP PRO HIS CYS ASP VAL PHE GLN ASN GLU THR TRP
SEQRES 7 C 323 ASP LEU PHE VAL GLU ARG SER LYS ALA PHE SER ASN CYS
SEQRES 8 C 323 TYR PRO TYR ASP VAL PRO ASP TYR ALA SER LEU ARG SER
SEQRES 9 C 323 LEU VAL ALA SER SER GLY THR LEU GLU PHE ILE THR GLU
SEQRES 10 C 323 GLY PHE THR TRP THR GLY VAL THR GLN ASN GLY GLY SER
SEQRES 11 C 323 ASN ALA CYS LYS ARG GLY PRO GLY SER GLY PHE PHE SER
SEQRES 12 C 323 ARG LEU ASN TRP LEU THR LYS SER GLY SER THR TYR PRO
SEQRES 13 C 323 VAL LEU ASN VAL THR MET PRO ASN ASN ASP ASN PHE ASP
SEQRES 14 C 323 LYS LEU TYR ILE TRP GLY VAL HIS HIS PRO SER THR ASN
SEQRES 15 C 323 GLN GLU GLN THR SER LEU TYR VAL GLN ALA SER GLY ARG
SEQRES 16 C 323 VAL THR VAL SER THR ARG ARG SER GLN GLN THR ILE ILE
SEQRES 17 C 323 PRO ASN ILE GLY SER ARG PRO TRP VAL ARG GLY LEU SER
SEQRES 18 C 323 SER ARG ILE SER ILE TYR TRP THR ILE VAL LYS PRO GLY
SEQRES 19 C 323 ASP VAL LEU VAL ILE ASN SER ASN GLY ASN LEU ILE ALA
SEQRES 20 C 323 PRO ARG GLY TYR PHE LYS MET ARG THR GLY LYS SER SER
SEQRES 21 C 323 ILE MET ARG SER ASP ALA PRO ILE ASP THR CYS ILE SER
SEQRES 22 C 323 GLU CYS ILE THR PRO ASN GLY SER ILE PRO ASN ASP LYS
SEQRES 23 C 323 PRO PHE GLN ASN VAL ASN LYS ILE THR TYR GLY ALA CYS
SEQRES 24 C 323 PRO LYS TYR VAL LYS GLN ASN THR LEU LYS LEU ALA THR
SEQRES 25 C 323 GLY MET ARG ASN VAL PRO GLU LYS GLN THR ARG
SEQRES 1 D 176 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU ASN GLY
SEQRES 2 D 176 TRP GLU GLY MET ILE ASP GLY TRP TYR GLY PHE ARG HIS
SEQRES 3 D 176 GLN ASN SER GLU GLY THR GLY GLN ALA ALA ASP LEU LYS
SEQRES 4 D 176 SER THR GLN ALA ALA ILE ASP GLN ILE ASN GLY LYS LEU
SEQRES 5 D 176 ASN ARG VAL ILE GLU LYS THR ASN GLU LYS PHE HIS GLN
SEQRES 6 D 176 ILE GLU LYS GLU PHE SER GLU VAL GLU GLY ARG ILE GLN
SEQRES 7 D 176 ASP LEU GLU LYS TYR VAL GLU ASP THR LYS ILE ASP LEU
SEQRES 8 D 176 TRP SER TYR ASN ALA GLU LEU LEU VAL ALA LEU GLU ASN
SEQRES 9 D 176 GLN HIS THR ILE ASP LEU THR ASP SER GLU MET ASN LYS
SEQRES 10 D 176 LEU PHE GLU LYS THR GLY ARG GLN LEU ARG GLU ASN ALA
SEQRES 11 D 176 GLU ASP MET GLY ASN GLY CYS PHE LYS ILE TYR HIS LYS
SEQRES 12 D 176 CYS ASP ASN ALA CYS ILE GLU SER ILE ARG ASN GLY THR
SEQRES 13 D 176 TYR ASP HIS ASP VAL TYR ARG ASP GLU ALA LEU ASN ASN
SEQRES 14 D 176 ARG PHE GLN ILE LYS GLY VAL
SEQRES 1 E 323 ALA ASP PRO GLY ALA THR LEU CYS LEU GLY HIS HIS ALA
SEQRES 2 E 323 VAL PRO ASN GLY THR LEU VAL LYS THR ILE THR ASP ASP
SEQRES 3 E 323 GLN ILE GLU VAL THR ASN ALA THR GLU LEU VAL GLN SER
SEQRES 4 E 323 SER SER THR GLY LYS ILE CYS ASN ASN PRO HIS ARG ILE
SEQRES 5 E 323 LEU ASP GLY ILE ASP CYS THR LEU ILE ASP ALA LEU LEU
SEQRES 6 E 323 GLY ASP PRO HIS CYS ASP VAL PHE GLN ASN GLU THR TRP
SEQRES 7 E 323 ASP LEU PHE VAL GLU ARG SER LYS ALA PHE SER ASN CYS
SEQRES 8 E 323 TYR PRO TYR ASP VAL PRO ASP TYR ALA SER LEU ARG SER
SEQRES 9 E 323 LEU VAL ALA SER SER GLY THR LEU GLU PHE ILE THR GLU
SEQRES 10 E 323 GLY PHE THR TRP THR GLY VAL THR GLN ASN GLY GLY SER
SEQRES 11 E 323 ASN ALA CYS LYS ARG GLY PRO GLY SER GLY PHE PHE SER
SEQRES 12 E 323 ARG LEU ASN TRP LEU THR LYS SER GLY SER THR TYR PRO
SEQRES 13 E 323 VAL LEU ASN VAL THR MET PRO ASN ASN ASP ASN PHE ASP
SEQRES 14 E 323 LYS LEU TYR ILE TRP GLY VAL HIS HIS PRO SER THR ASN
SEQRES 15 E 323 GLN GLU GLN THR SER LEU TYR VAL GLN ALA SER GLY ARG
SEQRES 16 E 323 VAL THR VAL SER THR ARG ARG SER GLN GLN THR ILE ILE
SEQRES 17 E 323 PRO ASN ILE GLY SER ARG PRO TRP VAL ARG GLY LEU SER
SEQRES 18 E 323 SER ARG ILE SER ILE TYR TRP THR ILE VAL LYS PRO GLY
SEQRES 19 E 323 ASP VAL LEU VAL ILE ASN SER ASN GLY ASN LEU ILE ALA
SEQRES 20 E 323 PRO ARG GLY TYR PHE LYS MET ARG THR GLY LYS SER SER
SEQRES 21 E 323 ILE MET ARG SER ASP ALA PRO ILE ASP THR CYS ILE SER
SEQRES 22 E 323 GLU CYS ILE THR PRO ASN GLY SER ILE PRO ASN ASP LYS
SEQRES 23 E 323 PRO PHE GLN ASN VAL ASN LYS ILE THR TYR GLY ALA CYS
SEQRES 24 E 323 PRO LYS TYR VAL LYS GLN ASN THR LEU LYS LEU ALA THR
SEQRES 25 E 323 GLY MET ARG ASN VAL PRO GLU LYS GLN THR ARG
SEQRES 1 F 176 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU ASN GLY
SEQRES 2 F 176 TRP GLU GLY MET ILE ASP GLY TRP TYR GLY PHE ARG HIS
SEQRES 3 F 176 GLN ASN SER GLU GLY THR GLY GLN ALA ALA ASP LEU LYS
SEQRES 4 F 176 SER THR GLN ALA ALA ILE ASP GLN ILE ASN GLY LYS LEU
SEQRES 5 F 176 ASN ARG VAL ILE GLU LYS THR ASN GLU LYS PHE HIS GLN
SEQRES 6 F 176 ILE GLU LYS GLU PHE SER GLU VAL GLU GLY ARG ILE GLN
SEQRES 7 F 176 ASP LEU GLU LYS TYR VAL GLU ASP THR LYS ILE ASP LEU
SEQRES 8 F 176 TRP SER TYR ASN ALA GLU LEU LEU VAL ALA LEU GLU ASN
SEQRES 9 F 176 GLN HIS THR ILE ASP LEU THR ASP SER GLU MET ASN LYS
SEQRES 10 F 176 LEU PHE GLU LYS THR GLY ARG GLN LEU ARG GLU ASN ALA
SEQRES 11 F 176 GLU ASP MET GLY ASN GLY CYS PHE LYS ILE TYR HIS LYS
SEQRES 12 F 176 CYS ASP ASN ALA CYS ILE GLU SER ILE ARG ASN GLY THR
SEQRES 13 F 176 TYR ASP HIS ASP VAL TYR ARG ASP GLU ALA LEU ASN ASN
SEQRES 14 F 176 ARG PHE GLN ILE LYS GLY VAL
SEQRES 1 L 220 ASP ILE GLN MET THR GLN SER PRO ASP SER LEU ALA VAL
SEQRES 2 L 220 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER
SEQRES 3 L 220 GLN SER VAL PHE SER SER SER THR ASN LYS ASN TYR LEU
SEQRES 4 L 220 ALA TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS VAL
SEQRES 5 L 220 LEU ILE TYR TRP SER SER THR ARG GLU SER GLY VAL PRO
SEQRES 6 L 220 ASP ARG PHE SER ALA SER GLY SER GLY THR ASP PHE THR
SEQRES 7 L 220 LEU THR ILE SER SER LEU GLN ALA ALA ASP VAL ALA VAL
SEQRES 8 L 220 TYR TYR CYS HIS GLN TYR TYR THR ALA PRO TRP THR PHE
SEQRES 9 L 220 GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA
SEQRES 10 L 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN
SEQRES 11 L 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN
SEQRES 12 L 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL
SEQRES 13 L 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL
SEQRES 14 L 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER
SEQRES 15 L 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS
SEQRES 16 L 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER
SEQRES 17 L 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS
SEQRES 1 H 230 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 H 230 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY
SEQRES 3 H 230 TYR THR PHE THR ALA TYR SER MET HIS TRP VAL ARG GLN
SEQRES 4 H 230 ALA PRO GLY GLN SER LEU GLU TRP LEU GLY TRP ILE ASN
SEQRES 5 H 230 THR ALA ILE GLY ASN THR GLN TYR SER GLN LYS PHE GLN
SEQRES 6 H 230 ASP ARG VAL THR ILE THR ARG ASP THR SER ALA ARG THR
SEQRES 7 H 230 SER TYR MET GLU LEU SER SER LEU ARG SER GLY ASP THR
SEQRES 8 H 230 ALA VAL TYR PHE CYS ALA ARG GLY ALA SER TRP ASP ALA
SEQRES 9 H 230 ARG GLY TRP SER GLY TYR TRP GLY LYS GLY THR LEU VAL
SEQRES 10 H 230 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE
SEQRES 11 H 230 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR
SEQRES 12 H 230 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU
SEQRES 13 H 230 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER
SEQRES 14 H 230 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY
SEQRES 15 H 230 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER
SEQRES 16 H 230 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS
SEQRES 17 H 230 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO
SEQRES 18 H 230 LYS SER CYS HIS HIS HIS HIS HIS HIS
SEQRES 1 M 220 ASP ILE GLN MET THR GLN SER PRO ASP SER LEU ALA VAL
SEQRES 2 M 220 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER
SEQRES 3 M 220 GLN SER VAL PHE SER SER SER THR ASN LYS ASN TYR LEU
SEQRES 4 M 220 ALA TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS VAL
SEQRES 5 M 220 LEU ILE TYR TRP SER SER THR ARG GLU SER GLY VAL PRO
SEQRES 6 M 220 ASP ARG PHE SER ALA SER GLY SER GLY THR ASP PHE THR
SEQRES 7 M 220 LEU THR ILE SER SER LEU GLN ALA ALA ASP VAL ALA VAL
SEQRES 8 M 220 TYR TYR CYS HIS GLN TYR TYR THR ALA PRO TRP THR PHE
SEQRES 9 M 220 GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA
SEQRES 10 M 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN
SEQRES 11 M 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN
SEQRES 12 M 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL
SEQRES 13 M 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL
SEQRES 14 M 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER
SEQRES 15 M 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS
SEQRES 16 M 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER
SEQRES 17 M 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS
SEQRES 1 I 230 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 I 230 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY
SEQRES 3 I 230 TYR THR PHE THR ALA TYR SER MET HIS TRP VAL ARG GLN
SEQRES 4 I 230 ALA PRO GLY GLN SER LEU GLU TRP LEU GLY TRP ILE ASN
SEQRES 5 I 230 THR ALA ILE GLY ASN THR GLN TYR SER GLN LYS PHE GLN
SEQRES 6 I 230 ASP ARG VAL THR ILE THR ARG ASP THR SER ALA ARG THR
SEQRES 7 I 230 SER TYR MET GLU LEU SER SER LEU ARG SER GLY ASP THR
SEQRES 8 I 230 ALA VAL TYR PHE CYS ALA ARG GLY ALA SER TRP ASP ALA
SEQRES 9 I 230 ARG GLY TRP SER GLY TYR TRP GLY LYS GLY THR LEU VAL
SEQRES 10 I 230 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE
SEQRES 11 I 230 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR
SEQRES 12 I 230 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU
SEQRES 13 I 230 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER
SEQRES 14 I 230 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY
SEQRES 15 I 230 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER
SEQRES 16 I 230 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS
SEQRES 17 I 230 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO
SEQRES 18 I 230 LYS SER CYS HIS HIS HIS HIS HIS HIS
SEQRES 1 N 220 ASP ILE GLN MET THR GLN SER PRO ASP SER LEU ALA VAL
SEQRES 2 N 220 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER
SEQRES 3 N 220 GLN SER VAL PHE SER SER SER THR ASN LYS ASN TYR LEU
SEQRES 4 N 220 ALA TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS VAL
SEQRES 5 N 220 LEU ILE TYR TRP SER SER THR ARG GLU SER GLY VAL PRO
SEQRES 6 N 220 ASP ARG PHE SER ALA SER GLY SER GLY THR ASP PHE THR
SEQRES 7 N 220 LEU THR ILE SER SER LEU GLN ALA ALA ASP VAL ALA VAL
SEQRES 8 N 220 TYR TYR CYS HIS GLN TYR TYR THR ALA PRO TRP THR PHE
SEQRES 9 N 220 GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA
SEQRES 10 N 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN
SEQRES 11 N 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN
SEQRES 12 N 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL
SEQRES 13 N 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL
SEQRES 14 N 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER
SEQRES 15 N 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS
SEQRES 16 N 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER
SEQRES 17 N 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS
SEQRES 1 J 230 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 J 230 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY
SEQRES 3 J 230 TYR THR PHE THR ALA TYR SER MET HIS TRP VAL ARG GLN
SEQRES 4 J 230 ALA PRO GLY GLN SER LEU GLU TRP LEU GLY TRP ILE ASN
SEQRES 5 J 230 THR ALA ILE GLY ASN THR GLN TYR SER GLN LYS PHE GLN
SEQRES 6 J 230 ASP ARG VAL THR ILE THR ARG ASP THR SER ALA ARG THR
SEQRES 7 J 230 SER TYR MET GLU LEU SER SER LEU ARG SER GLY ASP THR
SEQRES 8 J 230 ALA VAL TYR PHE CYS ALA ARG GLY ALA SER TRP ASP ALA
SEQRES 9 J 230 ARG GLY TRP SER GLY TYR TRP GLY LYS GLY THR LEU VAL
SEQRES 10 J 230 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE
SEQRES 11 J 230 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR
SEQRES 12 J 230 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU
SEQRES 13 J 230 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER
SEQRES 14 J 230 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY
SEQRES 15 J 230 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER
SEQRES 16 J 230 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS
SEQRES 17 J 230 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO
SEQRES 18 J 230 LYS SER CYS HIS HIS HIS HIS HIS HIS
MODRES 4NM8 ASN C 81 ASN GLYCOSYLATION SITE
MODRES 4NM8 ASN C 285 ASN GLYCOSYLATION SITE
MODRES 4NM8 ASN B 154 ASN GLYCOSYLATION SITE
MODRES 4NM8 ASN A 165 ASN GLYCOSYLATION SITE
MODRES 4NM8 ASN E 81 ASN GLYCOSYLATION SITE
MODRES 4NM8 ASN E 285 ASN GLYCOSYLATION SITE
MODRES 4NM8 ASN C 38 ASN GLYCOSYLATION SITE
MODRES 4NM8 ASN E 165 ASN GLYCOSYLATION SITE
MODRES 4NM8 ASN F 154 ASN GLYCOSYLATION SITE
MODRES 4NM8 ASN E 38 ASN GLYCOSYLATION SITE
MODRES 4NM8 ASN A 285 ASN GLYCOSYLATION SITE
MODRES 4NM8 ASN C 165 ASN GLYCOSYLATION SITE
MODRES 4NM8 ASN A 38 ASN GLYCOSYLATION SITE
MODRES 4NM8 ASN D 154 ASN GLYCOSYLATION SITE
HET NAG G 1 14
HET NAG G 2 14
HET NAG K 1 14
HET NAG K 2 14
HET NAG O 1 14
HET NAG O 2 14
HET NAG P 1 14
HET NAG P 2 14
HET NAG Q 1 14
HET NAG Q 2 14
HET NAG R 1 14
HET NAG R 2 14
HET NAG B 201 14
HET NAG C 501 14
HET NAG C 504 14
HET NAG D 201 14
HET NAG E 501 14
HET NAG E 502 14
HET NAG E 503 14
HET NAG F 201 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
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
FORMUL 13 NAG 20(C8 H15 N O6)
HELIX 1 1 THR A 65 GLY A 72 1 8
HELIX 2 2 ASP A 73 GLN A 80 5 8
HELIX 3 3 ASP A 104 GLY A 116 1 13
HELIX 4 4 THR A 187 VAL A 196 1 10
HELIX 5 5 ASP B 37 ILE B 56 1 20
HELIX 6 6 GLY B 75 ARG B 127 1 53
HELIX 7 7 ASP B 145 ASN B 154 1 10
HELIX 8 8 ASP B 158 GLN B 172 1 15
HELIX 9 9 THR C 65 GLY C 72 1 8
HELIX 10 10 ASP C 73 GLN C 80 5 8
HELIX 11 11 ASP C 104 GLY C 116 1 13
HELIX 12 12 THR C 187 VAL C 196 1 10
HELIX 13 13 ASP D 37 GLU D 57 1 21
HELIX 14 14 GLY D 75 ARG D 127 1 53
HELIX 15 15 ASP D 145 ASN D 154 1 10
HELIX 16 16 ASP D 158 PHE D 171 1 14
HELIX 17 17 THR E 65 GLY E 72 1 8
HELIX 18 18 ASP E 73 GLN E 80 5 8
HELIX 19 19 ASP E 104 GLY E 116 1 13
HELIX 20 20 THR E 187 VAL E 196 1 10
HELIX 21 21 ASP F 37 ILE F 56 1 20
HELIX 22 22 GLY F 75 ARG F 127 1 53
HELIX 23 23 ASP F 145 ASN F 154 1 10
HELIX 24 24 ASP F 158 PHE F 171 1 14
HELIX 25 25 GLN L 79 VAL L 83 5 5
HELIX 26 26 SER L 121 LYS L 126 1 6
HELIX 27 27 LYS L 183 GLU L 187 1 5
HELIX 28 28 THR H 28 TYR H 32 5 5
HELIX 29 29 GLN H 61 GLN H 64 5 4
HELIX 30 30 ARG H 83 THR H 87 5 5
HELIX 31 31 SER H 156 ALA H 158 5 3
HELIX 32 32 SER H 187 LEU H 189 5 3
HELIX 33 33 LYS H 201 ASN H 204 5 4
HELIX 34 34 GLN M 79 VAL M 83 5 5
HELIX 35 35 SER M 121 LYS M 126 1 6
HELIX 36 36 LYS M 183 GLU M 187 1 5
HELIX 37 37 THR I 28 TYR I 32 5 5
HELIX 38 38 ARG I 83 THR I 87 5 5
HELIX 39 39 SER I 156 ALA I 158 5 3
HELIX 40 40 PRO I 185 LEU I 189 5 5
HELIX 41 41 LYS I 201 ASN I 204 5 4
HELIX 42 42 GLN N 79 VAL N 83 5 5
HELIX 43 43 SER N 121 LYS N 126 1 6
HELIX 44 44 LYS N 183 GLU N 187 1 5
HELIX 45 45 THR J 28 TYR J 32 5 5
HELIX 46 46 ARG J 83 THR J 87 5 5
HELIX 47 47 SER J 156 ALA J 158 5 3
HELIX 48 48 PRO J 185 LEU J 189 5 5
HELIX 49 49 LYS J 201 ASN J 204 5 4
SHEET 1 A 5 GLY B 31 ALA B 36 0
SHEET 2 A 5 TYR B 22 ASN B 28 -1 N ASN B 28 O GLY B 31
SHEET 3 A 5 ALA A 11 HIS A 17 -1 N CYS A 14 O ARG B 25
SHEET 4 A 5 CYS B 137 ILE B 140 -1 O ILE B 140 N ALA A 11
SHEET 5 A 5 ALA B 130 ASP B 132 -1 N GLU B 131 O LYS B 139
SHEET 1 B 2 THR A 24 VAL A 26 0
SHEET 2 B 2 ILE A 34 VAL A 36 -1 O VAL A 36 N THR A 24
SHEET 1 C 2 ALA A 39 GLU A 41 0
SHEET 2 C 2 LYS A 315 ALA A 317 -1 O LEU A 316 N THR A 40
SHEET 1 D 3 VAL A 43 GLN A 44 0
SHEET 2 D 3 PHE A 294 GLN A 295 1 O PHE A 294 N GLN A 44
SHEET 3 D 3 LYS A 307 TYR A 308 1 O LYS A 307 N GLN A 295
SHEET 1 E 2 ILE A 51 ASN A 54 0
SHEET 2 E 2 ILE A 274 ILE A 278 1 O ASP A 275 N ILE A 51
SHEET 1 F 3 ILE A 58 ASP A 60 0
SHEET 2 F 3 LEU A 86 GLU A 89 1 O VAL A 88 N LEU A 59
SHEET 3 F 3 SER A 266 ARG A 269 1 O MET A 268 N PHE A 87
SHEET 1 G 5 TYR A 100 ASP A 101 0
SHEET 2 G 5 ARG A 229 VAL A 237 1 O ILE A 232 N ASP A 101
SHEET 3 G 5 LYS A 176 HIS A 184 -1 N VAL A 182 O SER A 231
SHEET 4 G 5 GLY A 256 LYS A 259 -1 O PHE A 258 N LEU A 177
SHEET 5 G 5 PHE A 120 THR A 122 -1 N ILE A 121 O TYR A 257
SHEET 1 H 5 TYR A 100 ASP A 101 0
SHEET 2 H 5 ARG A 229 VAL A 237 1 O ILE A 232 N ASP A 101
SHEET 3 H 5 LYS A 176 HIS A 184 -1 N VAL A 182 O SER A 231
SHEET 4 H 5 LEU A 251 PRO A 254 -1 O ILE A 252 N GLY A 181
SHEET 5 H 5 LEU A 151 TRP A 153 -1 N ASN A 152 O ALA A 253
SHEET 1 I 2 VAL A 130 THR A 131 0
SHEET 2 I 2 THR A 155 LYS A 156 -1 O THR A 155 N THR A 131
SHEET 1 J 2 SER A 136 ARG A 141 0
SHEET 2 J 2 GLY A 144 GLY A 146 -1 O GLY A 144 N ARG A 141
SHEET 1 K 4 LEU A 164 PRO A 169 0
SHEET 2 K 4 VAL A 242 SER A 247 -1 O SER A 247 N LEU A 164
SHEET 3 K 4 VAL A 202 SER A 205 -1 N THR A 203 O ASN A 246
SHEET 4 K 4 GLN A 210 ILE A 213 -1 O ILE A 213 N VAL A 202
SHEET 1 L 4 GLY A 286 ILE A 288 0
SHEET 2 L 4 CYS A 281 THR A 283 -1 N CYS A 281 O ILE A 288
SHEET 3 L 4 TYR A 302 ALA A 304 -1 O TYR A 302 N ILE A 282
SHEET 4 L 4 GLU B 61 LYS B 62 -1 O LYS B 62 N GLY A 303
SHEET 1 M 5 GLY D 31 ALA D 36 0
SHEET 2 M 5 TYR D 22 ASN D 28 -1 N ASN D 28 O GLY D 31
SHEET 3 M 5 ALA C 11 HIS C 17 -1 N CYS C 14 O ARG D 25
SHEET 4 M 5 CYS D 137 ILE D 140 -1 O PHE D 138 N LEU C 13
SHEET 5 M 5 ALA D 130 ASP D 132 -1 N GLU D 131 O LYS D 139
SHEET 1 N 2 THR C 24 VAL C 26 0
SHEET 2 N 2 ILE C 34 VAL C 36 -1 O VAL C 36 N THR C 24
SHEET 1 O 2 ALA C 39 GLU C 41 0
SHEET 2 O 2 LYS C 315 ALA C 317 -1 O LEU C 316 N THR C 40
SHEET 1 P 3 VAL C 43 GLN C 44 0
SHEET 2 P 3 PHE C 294 GLN C 295 1 O PHE C 294 N GLN C 44
SHEET 3 P 3 LYS C 307 TYR C 308 1 O LYS C 307 N GLN C 295
SHEET 1 Q 2 ILE C 51 ASN C 54 0
SHEET 2 Q 2 ILE C 274 ILE C 278 1 O ASP C 275 N ILE C 51
SHEET 1 R 3 ILE C 58 ASP C 60 0
SHEET 2 R 3 LEU C 86 GLU C 89 1 O VAL C 88 N LEU C 59
SHEET 3 R 3 SER C 266 ARG C 269 1 O MET C 268 N PHE C 87
SHEET 1 S 5 TYR C 100 ASP C 101 0
SHEET 2 S 5 ARG C 229 VAL C 237 1 O ILE C 232 N ASP C 101
SHEET 3 S 5 LYS C 176 HIS C 184 -1 N HIS C 184 O ARG C 229
SHEET 4 S 5 GLY C 256 LYS C 259 -1 O PHE C 258 N LEU C 177
SHEET 5 S 5 PHE C 120 THR C 122 -1 N ILE C 121 O TYR C 257
SHEET 1 T 5 TYR C 100 ASP C 101 0
SHEET 2 T 5 ARG C 229 VAL C 237 1 O ILE C 232 N ASP C 101
SHEET 3 T 5 LYS C 176 HIS C 184 -1 N HIS C 184 O ARG C 229
SHEET 4 T 5 LEU C 251 PRO C 254 -1 O ILE C 252 N GLY C 181
SHEET 5 T 5 LEU C 151 TRP C 153 -1 N ASN C 152 O ALA C 253
SHEET 1 U 2 VAL C 130 THR C 131 0
SHEET 2 U 2 THR C 155 LYS C 156 -1 O THR C 155 N THR C 131
SHEET 1 V 2 SER C 136 ARG C 141 0
SHEET 2 V 2 GLY C 144 GLY C 146 -1 O GLY C 144 N ARG C 141
SHEET 1 W 4 LEU C 164 PRO C 169 0
SHEET 2 W 4 VAL C 242 GLY C 249 -1 O SER C 247 N LEU C 164
SHEET 3 W 4 ARG C 201 SER C 205 -1 N THR C 203 O ASN C 246
SHEET 4 W 4 GLN C 210 ILE C 213 -1 O ILE C 213 N VAL C 202
SHEET 1 X 4 GLY C 286 ILE C 288 0
SHEET 2 X 4 CYS C 281 THR C 283 -1 N CYS C 281 O ILE C 288
SHEET 3 X 4 TYR C 302 ALA C 304 -1 O TYR C 302 N ILE C 282
SHEET 4 X 4 GLU D 61 LYS D 62 -1 O LYS D 62 N GLY C 303
SHEET 1 Y 5 GLY F 31 ALA F 36 0
SHEET 2 Y 5 TYR F 22 ASN F 28 -1 N ASN F 28 O GLY F 31
SHEET 3 Y 5 ALA E 11 HIS E 17 -1 N CYS E 14 O ARG F 25
SHEET 4 Y 5 CYS F 137 ILE F 140 -1 O PHE F 138 N LEU E 13
SHEET 5 Y 5 ALA F 130 ASP F 132 -1 N GLU F 131 O LYS F 139
SHEET 1 Z 2 THR E 24 VAL E 26 0
SHEET 2 Z 2 ILE E 34 VAL E 36 -1 O VAL E 36 N THR E 24
SHEET 1 AA 2 ALA E 39 GLU E 41 0
SHEET 2 AA 2 LYS E 315 ALA E 317 -1 O LEU E 316 N THR E 40
SHEET 1 AB 3 VAL E 43 GLN E 44 0
SHEET 2 AB 3 PHE E 294 GLN E 295 1 O PHE E 294 N GLN E 44
SHEET 3 AB 3 LYS E 307 TYR E 308 1 O LYS E 307 N GLN E 295
SHEET 1 AC 2 ILE E 51 ASN E 54 0
SHEET 2 AC 2 ILE E 274 ILE E 278 1 O ASP E 275 N ASN E 53
SHEET 1 AD 3 ILE E 58 ASP E 60 0
SHEET 2 AD 3 LEU E 86 GLU E 89 1 O VAL E 88 N LEU E 59
SHEET 3 AD 3 SER E 266 ARG E 269 1 O SER E 266 N PHE E 87
SHEET 1 AE 5 TYR E 100 ASP E 101 0
SHEET 2 AE 5 ARG E 229 VAL E 237 1 O ILE E 230 N ASP E 101
SHEET 3 AE 5 LYS E 176 HIS E 184 -1 N VAL E 182 O SER E 231
SHEET 4 AE 5 GLY E 256 LYS E 259 -1 O PHE E 258 N LEU E 177
SHEET 5 AE 5 PHE E 120 THR E 122 -1 N ILE E 121 O TYR E 257
SHEET 1 AF 6 TYR E 100 ASP E 101 0
SHEET 2 AF 6 ARG E 229 VAL E 237 1 O ILE E 230 N ASP E 101
SHEET 3 AF 6 LYS E 176 HIS E 184 -1 N VAL E 182 O SER E 231
SHEET 4 AF 6 LEU E 251 PRO E 254 -1 O ILE E 252 N GLY E 181
SHEET 5 AF 6 LEU E 151 LYS E 156 -1 N ASN E 152 O ALA E 253
SHEET 6 AF 6 VAL E 130 GLY E 134 -1 N THR E 131 O THR E 155
SHEET 1 AG 2 SER E 136 ARG E 141 0
SHEET 2 AG 2 GLY E 144 GLY E 146 -1 O GLY E 146 N SER E 136
SHEET 1 AH 4 LEU E 164 PRO E 169 0
SHEET 2 AH 4 VAL E 242 SER E 247 -1 O SER E 247 N LEU E 164
SHEET 3 AH 4 VAL E 202 SER E 205 -1 N THR E 203 O ASN E 246
SHEET 4 AH 4 GLN E 210 ILE E 213 -1 O ILE E 213 N VAL E 202
SHEET 1 AI 4 GLY E 286 ILE E 288 0
SHEET 2 AI 4 CYS E 281 THR E 283 -1 N CYS E 281 O ILE E 288
SHEET 3 AI 4 TYR E 302 ALA E 304 -1 O TYR E 302 N ILE E 282
SHEET 4 AI 4 GLU F 61 LYS F 62 -1 O LYS F 62 N GLY E 303
SHEET 1 AJ 4 MET L 4 SER L 7 0
SHEET 2 AJ 4 ALA L 19 SER L 25 -1 O ASN L 22 N SER L 7
SHEET 3 AJ 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21
SHEET 4 AJ 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74
SHEET 1 AK 6 SER L 10 VAL L 13 0
SHEET 2 AK 6 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11
SHEET 3 AK 6 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104
SHEET 4 AK 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87
SHEET 5 AK 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35
SHEET 6 AK 6 THR L 53 ARG L 54 -1 O THR L 53 N TYR L 49
SHEET 1 AL 4 SER L 10 VAL L 13 0
SHEET 2 AL 4 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11
SHEET 3 AL 4 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104
SHEET 4 AL 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90
SHEET 1 AM 2 PHE L 27C SER L 27D 0
SHEET 2 AM 2 LYS L 30 ASN L 31 -1 O LYS L 30 N SER L 27D
SHEET 1 AN 4 SER L 114 PHE L 118 0
SHEET 2 AN 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116
SHEET 3 AN 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132
SHEET 4 AN 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176
SHEET 1 AO 4 ALA L 153 LEU L 154 0
SHEET 2 AO 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153
SHEET 3 AO 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147
SHEET 4 AO 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196
SHEET 1 AP 4 GLN H 3 GLN H 6 0
SHEET 2 AP 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5
SHEET 3 AP 4 THR H 77 LEU H 82 -1 O SER H 78 N CYS H 22
SHEET 4 AP 4 VAL H 67 ASP H 72 -1 N THR H 70 O TYR H 79
SHEET 1 AQ 6 GLU H 10 LYS H 12 0
SHEET 2 AQ 6 THR H 107 VAL H 111 1 O LEU H 108 N GLU H 10
SHEET 3 AQ 6 ALA H 88 GLY H 95 -1 N TYR H 90 O THR H 107
SHEET 4 AQ 6 MET H 34 GLN H 39 -1 N VAL H 37 O PHE H 91
SHEET 5 AQ 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38
SHEET 6 AQ 6 THR H 57 TYR H 59 -1 O GLN H 58 N TRP H 50
SHEET 1 AR 4 GLU H 10 LYS H 12 0
SHEET 2 AR 4 THR H 107 VAL H 111 1 O LEU H 108 N GLU H 10
SHEET 3 AR 4 ALA H 88 GLY H 95 -1 N TYR H 90 O THR H 107
SHEET 4 AR 4 SER H 100D TRP H 103 -1 O TYR H 102 N ARG H 94
SHEET 1 AS 4 SER H 120 LEU H 124 0
SHEET 2 AS 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122
SHEET 3 AS 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142
SHEET 4 AS 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181
SHEET 1 AT 4 SER H 120 LEU H 124 0
SHEET 2 AT 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122
SHEET 3 AT 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142
SHEET 4 AT 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177
SHEET 1 AU 3 THR H 151 TRP H 154 0
SHEET 2 AU 3 TYR H 194 HIS H 200 -1 O ASN H 197 N SER H 153
SHEET 3 AU 3 THR H 205 VAL H 211 -1 O THR H 205 N HIS H 200
SHEET 1 AV 4 MET M 4 SER M 7 0
SHEET 2 AV 4 ALA M 19 SER M 25 -1 O ASN M 22 N SER M 7
SHEET 3 AV 4 ASP M 70 ILE M 75 -1 O PHE M 71 N CYS M 23
SHEET 4 AV 4 PHE M 62 SER M 67 -1 N SER M 63 O THR M 74
SHEET 1 AW 6 SER M 10 VAL M 13 0
SHEET 2 AW 6 THR M 102 ILE M 106 1 O GLU M 105 N LEU M 11
SHEET 3 AW 6 ALA M 84 GLN M 90 -1 N ALA M 84 O VAL M 104
SHEET 4 AW 6 LEU M 33 GLN M 38 -1 N ALA M 34 O HIS M 89
SHEET 5 AW 6 LYS M 45 TYR M 49 -1 O LEU M 47 N TRP M 35
SHEET 6 AW 6 THR M 53 ARG M 54 -1 O THR M 53 N TYR M 49
SHEET 1 AX 4 SER M 10 VAL M 13 0
SHEET 2 AX 4 THR M 102 ILE M 106 1 O GLU M 105 N LEU M 11
SHEET 3 AX 4 ALA M 84 GLN M 90 -1 N ALA M 84 O VAL M 104
SHEET 4 AX 4 THR M 97 PHE M 98 -1 O THR M 97 N GLN M 90
SHEET 1 AY 2 PHE M 27C SER M 27D 0
SHEET 2 AY 2 LYS M 30 ASN M 31 -1 O LYS M 30 N SER M 27D
SHEET 1 AZ 4 SER M 114 PHE M 118 0
SHEET 2 AZ 4 THR M 129 PHE M 139 -1 O ASN M 137 N SER M 114
SHEET 3 AZ 4 TYR M 173 SER M 182 -1 O LEU M 179 N VAL M 132
SHEET 4 AZ 4 SER M 159 VAL M 163 -1 N SER M 162 O SER M 176
SHEET 1 BA 4 ALA M 153 LEU M 154 0
SHEET 2 BA 4 LYS M 145 VAL M 150 -1 N VAL M 150 O ALA M 153
SHEET 3 BA 4 VAL M 191 THR M 197 -1 O GLU M 195 N GLN M 147
SHEET 4 BA 4 VAL M 205 ASN M 210 -1 O VAL M 205 N VAL M 196
SHEET 1 BB 4 GLN I 3 GLN I 6 0
SHEET 2 BB 4 VAL I 18 SER I 25 -1 O LYS I 23 N VAL I 5
SHEET 3 BB 4 THR I 77 LEU I 82 -1 O MET I 80 N LEU I 20
SHEET 4 BB 4 VAL I 67 ASP I 72 -1 N ASP I 72 O THR I 77
SHEET 1 BC 6 GLU I 10 LYS I 12 0
SHEET 2 BC 6 THR I 107 VAL I 111 1 O THR I 110 N GLU I 10
SHEET 3 BC 6 ALA I 88 GLY I 95 -1 N TYR I 90 O THR I 107
SHEET 4 BC 6 MET I 34 GLN I 39 -1 N VAL I 37 O PHE I 91
SHEET 5 BC 6 LEU I 45 ILE I 51 -1 O GLU I 46 N ARG I 38
SHEET 6 BC 6 THR I 57 TYR I 59 -1 O GLN I 58 N TRP I 50
SHEET 1 BD 4 GLU I 10 LYS I 12 0
SHEET 2 BD 4 THR I 107 VAL I 111 1 O THR I 110 N GLU I 10
SHEET 3 BD 4 ALA I 88 GLY I 95 -1 N TYR I 90 O THR I 107
SHEET 4 BD 4 SER I 100D TRP I 103 -1 O TYR I 102 N ARG I 94
SHEET 1 BE 4 SER I 120 LEU I 124 0
SHEET 2 BE 4 ALA I 136 TYR I 145 -1 O LEU I 141 N PHE I 122
SHEET 3 BE 4 TYR I 176 VAL I 184 -1 O TYR I 176 N TYR I 145
SHEET 4 BE 4 VAL I 163 THR I 165 -1 N HIS I 164 O VAL I 181
SHEET 1 BF 4 SER I 120 LEU I 124 0
SHEET 2 BF 4 ALA I 136 TYR I 145 -1 O LEU I 141 N PHE I 122
SHEET 3 BF 4 TYR I 176 VAL I 184 -1 O TYR I 176 N TYR I 145
SHEET 4 BF 4 VAL I 169 LEU I 170 -1 N VAL I 169 O SER I 177
SHEET 1 BG 3 THR I 151 TRP I 154 0
SHEET 2 BG 3 TYR I 194 HIS I 200 -1 O ASN I 197 N SER I 153
SHEET 3 BG 3 THR I 205 VAL I 211 -1 O VAL I 207 N VAL I 198
SHEET 1 BH 4 MET N 4 SER N 7 0
SHEET 2 BH 4 ALA N 19 SER N 25 -1 O ASN N 22 N SER N 7
SHEET 3 BH 4 ASP N 70 ILE N 75 -1 O LEU N 73 N ILE N 21
SHEET 4 BH 4 PHE N 62 SER N 67 -1 N SER N 63 O THR N 74
SHEET 1 BI 6 SER N 10 VAL N 13 0
SHEET 2 BI 6 THR N 102 ILE N 106 1 O GLU N 105 N LEU N 11
SHEET 3 BI 6 ALA N 84 GLN N 90 -1 N ALA N 84 O VAL N 104
SHEET 4 BI 6 LEU N 33 GLN N 38 -1 N TYR N 36 O TYR N 87
SHEET 5 BI 6 LYS N 45 TYR N 49 -1 O LEU N 47 N TRP N 35
SHEET 6 BI 6 THR N 53 ARG N 54 -1 O THR N 53 N TYR N 49
SHEET 1 BJ 4 SER N 10 VAL N 13 0
SHEET 2 BJ 4 THR N 102 ILE N 106 1 O GLU N 105 N LEU N 11
SHEET 3 BJ 4 ALA N 84 GLN N 90 -1 N ALA N 84 O VAL N 104
SHEET 4 BJ 4 THR N 97 PHE N 98 -1 O THR N 97 N GLN N 90
SHEET 1 BK 2 PHE N 27C SER N 27D 0
SHEET 2 BK 2 LYS N 30 ASN N 31 -1 O LYS N 30 N SER N 27D
SHEET 1 BL 4 SER N 114 PHE N 118 0
SHEET 2 BL 4 THR N 129 PHE N 139 -1 O LEU N 135 N PHE N 116
SHEET 3 BL 4 TYR N 173 SER N 182 -1 O LEU N 179 N VAL N 132
SHEET 4 BL 4 SER N 159 VAL N 163 -1 N SER N 162 O SER N 176
SHEET 1 BM 4 ALA N 153 LEU N 154 0
SHEET 2 BM 4 LYS N 145 VAL N 150 -1 N VAL N 150 O ALA N 153
SHEET 3 BM 4 VAL N 191 THR N 197 -1 O GLU N 195 N GLN N 147
SHEET 4 BM 4 VAL N 205 ASN N 210 -1 O VAL N 205 N VAL N 196
SHEET 1 BN 4 GLN J 3 GLN J 6 0
SHEET 2 BN 4 VAL J 18 SER J 25 -1 O LYS J 23 N VAL J 5
SHEET 3 BN 4 THR J 77 LEU J 82 -1 O SER J 78 N CYS J 22
SHEET 4 BN 4 VAL J 67 ASP J 72 -1 N THR J 70 O TYR J 79
SHEET 1 BO 6 GLU J 10 LYS J 12 0
SHEET 2 BO 6 THR J 107 VAL J 111 1 O LEU J 108 N GLU J 10
SHEET 3 BO 6 ALA J 88 GLY J 95 -1 N TYR J 90 O THR J 107
SHEET 4 BO 6 MET J 34 GLN J 39 -1 N VAL J 37 O PHE J 91
SHEET 5 BO 6 LEU J 45 ILE J 51 -1 O GLU J 46 N ARG J 38
SHEET 6 BO 6 THR J 57 TYR J 59 -1 O GLN J 58 N TRP J 50
SHEET 1 BP 4 GLU J 10 LYS J 12 0
SHEET 2 BP 4 THR J 107 VAL J 111 1 O LEU J 108 N GLU J 10
SHEET 3 BP 4 ALA J 88 GLY J 95 -1 N TYR J 90 O THR J 107
SHEET 4 BP 4 SER J 100D TRP J 103 -1 O TYR J 102 N ARG J 94
SHEET 1 BQ 4 SER J 120 LEU J 124 0
SHEET 2 BQ 4 ALA J 136 TYR J 145 -1 O LEU J 141 N PHE J 122
SHEET 3 BQ 4 TYR J 176 VAL J 184 -1 O LEU J 178 N VAL J 142
SHEET 4 BQ 4 VAL J 163 THR J 165 -1 N HIS J 164 O VAL J 181
SHEET 1 BR 4 SER J 120 LEU J 124 0
SHEET 2 BR 4 ALA J 136 TYR J 145 -1 O LEU J 141 N PHE J 122
SHEET 3 BR 4 TYR J 176 VAL J 184 -1 O LEU J 178 N VAL J 142
SHEET 4 BR 4 VAL J 169 LEU J 170 -1 N VAL J 169 O SER J 177
SHEET 1 BS 3 THR J 151 TRP J 154 0
SHEET 2 BS 3 ILE J 195 HIS J 200 -1 O ASN J 197 N SER J 153
SHEET 3 BS 3 THR J 205 ARG J 210 -1 O THR J 205 N HIS J 200
SSBOND 1 CYS A 14 CYS B 137 1555 1555 2.04
SSBOND 2 CYS A 52 CYS A 277 1555 1555 2.04
SSBOND 3 CYS A 64 CYS A 76 1555 1555 2.04
SSBOND 4 CYS A 97 CYS A 139 1555 1555 2.04
SSBOND 5 CYS A 281 CYS A 305 1555 1555 2.04
SSBOND 6 CYS B 144 CYS B 148 1555 1555 2.05
SSBOND 7 CYS C 14 CYS D 137 1555 1555 2.03
SSBOND 8 CYS C 52 CYS C 277 1555 1555 2.05
SSBOND 9 CYS C 64 CYS C 76 1555 1555 2.04
SSBOND 10 CYS C 97 CYS C 139 1555 1555 2.04
SSBOND 11 CYS C 281 CYS C 305 1555 1555 2.04
SSBOND 12 CYS D 144 CYS D 148 1555 1555 2.05
SSBOND 13 CYS E 14 CYS F 137 1555 1555 2.04
SSBOND 14 CYS E 52 CYS E 277 1555 1555 2.04
SSBOND 15 CYS E 64 CYS E 76 1555 1555 2.04
SSBOND 16 CYS E 97 CYS E 139 1555 1555 2.03
SSBOND 17 CYS E 281 CYS E 305 1555 1555 2.04
SSBOND 18 CYS F 144 CYS F 148 1555 1555 2.04
SSBOND 19 CYS L 23 CYS L 88 1555 1555 2.04
SSBOND 20 CYS L 134 CYS L 194 1555 1555 2.03
SSBOND 21 CYS H 22 CYS H 92 1555 1555 2.04
SSBOND 22 CYS H 140 CYS H 196 1555 1555 2.03
SSBOND 23 CYS M 23 CYS M 88 1555 1555 2.04
SSBOND 24 CYS M 134 CYS M 194 1555 1555 2.04
SSBOND 25 CYS I 22 CYS I 92 1555 1555 2.03
SSBOND 26 CYS I 140 CYS I 196 1555 1555 2.03
SSBOND 27 CYS N 23 CYS N 88 1555 1555 2.03
SSBOND 28 CYS N 134 CYS N 194 1555 1555 2.03
SSBOND 29 CYS J 22 CYS J 92 1555 1555 2.03
SSBOND 30 CYS J 140 CYS J 196 1555 1555 2.03
LINK ND2 ASN A 38 C1 NAG G 1 1555 1555 1.45
LINK ND2 ASN A 165 C1 NAG K 1 1555 1555 1.44
LINK ND2 ASN A 285 C1 NAG O 1 1555 1555 1.45
LINK ND2 ASN B 154 C1 NAG B 201 1555 1555 1.44
LINK ND2 ASN C 38 C1 NAG C 501 1555 1555 1.45
LINK ND2 ASN C 81 C1 NAG P 1 1555 1555 1.44
LINK ND2 ASN C 165 C1 NAG C 504 1555 1555 1.45
LINK ND2 ASN C 285 C1 NAG Q 1 1555 1555 1.44
LINK ND2 ASN D 154 C1 NAG D 201 1555 1555 1.46
LINK ND2 ASN E 38 C1 NAG E 501 1555 1555 1.45
LINK ND2 ASN E 81 C1 NAG E 502 1555 1555 1.45
LINK ND2 ASN E 165 C1 NAG E 503 1555 1555 1.45
LINK ND2 ASN E 285 C1 NAG R 1 1555 1555 1.45
LINK ND2 ASN F 154 C1 NAG F 201 1555 1555 1.45
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44
LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.45
LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44
LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.45
LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44
CISPEP 1 ASN A 54 PRO A 55 0 4.47
CISPEP 2 ASN C 54 PRO C 55 0 5.19
CISPEP 3 ASN E 54 PRO E 55 0 4.51
CISPEP 4 SER L 7 PRO L 8 0 1.68
CISPEP 5 ALA L 94 PRO L 95 0 -3.28
CISPEP 6 TYR L 140 PRO L 141 0 3.57
CISPEP 7 PHE H 146 PRO H 147 0 -5.48
CISPEP 8 GLU H 148 PRO H 149 0 1.92
CISPEP 9 SER M 7 PRO M 8 0 1.37
CISPEP 10 ALA M 94 PRO M 95 0 -3.29
CISPEP 11 TYR M 140 PRO M 141 0 3.76
CISPEP 12 PHE I 146 PRO I 147 0 -5.83
CISPEP 13 GLU I 148 PRO I 149 0 1.84
CISPEP 14 SER N 7 PRO N 8 0 1.60
CISPEP 15 ALA N 94 PRO N 95 0 -3.07
CISPEP 16 TYR N 140 PRO N 141 0 3.52
CISPEP 17 PHE J 146 PRO J 147 0 -5.68
CISPEP 18 GLU J 148 PRO J 149 0 2.14
CRYST1 241.491 142.355 170.725 90.00 133.46 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 0.004141 0.000000 0.003924 0.00000
SCALE2 0.000000 0.007025 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008070 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
