HEADER IMMUNE SYSTEM 27-AUG-12 4GSD
TITLE H5.3 FAB STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: H5.3 FAB LIGHT CHAIN;
COMPND 3 CHAIN: L;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: H5.3 FAB HEAVY CHAIN;
COMPND 7 CHAIN: H;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: HEK293F;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: LONZA;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PEE12.4;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: HEK293F;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: LONZA;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PEE6.4
KEYWDS ANTIBODY, IMMUNE RESPONSE, INFLUENZA H5 HEMAGGLUTANIN, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR B.W.SPILLER,K.L.WINARSKI
REVDAT 5 03-APR-24 4GSD 1 REMARK
REVDAT 4 24-JAN-18 4GSD 1 AUTHOR
REVDAT 3 23-OCT-13 4GSD 1 JRNL
REVDAT 2 09-OCT-13 4GSD 1 JRNL
REVDAT 1 21-AUG-13 4GSD 0
JRNL AUTH N.J.THORNBURG,D.P.NANNEMANN,D.L.BLUM,J.A.BELSER,T.M.TUMPEY,
JRNL AUTH 2 S.DESHPANDE,G.A.FRITZ,G.SAPPARAPU,J.C.KRAUSE,J.H.LEE,
JRNL AUTH 3 A.B.WARD,D.E.LEE,S.LI,K.L.WINARSKI,B.W.SPILLER,J.MEILER,
JRNL AUTH 4 J.E.CROWE
JRNL TITL HUMAN ANTIBODIES THAT NEUTRALIZE RESPIRATORY DROPLET
JRNL TITL 2 TRANSMISSIBLE H5N1 INFLUENZA VIRUSES.
JRNL REF J.CLIN.INVEST. V. 123 4405 2013
JRNL REFN ISSN 0021-9738
JRNL PMID 23999429
JRNL DOI 10.1172/JCI69377
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.37
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 43167
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2173
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 40.3720 - 5.6661 0.98 2624 143 0.1741 0.2012
REMARK 3 2 5.6661 - 4.4992 0.99 2576 132 0.1415 0.1654
REMARK 3 3 4.4992 - 3.9310 1.00 2598 122 0.1423 0.1710
REMARK 3 4 3.9310 - 3.5719 0.99 2555 144 0.1649 0.1704
REMARK 3 5 3.5719 - 3.3160 1.00 2586 111 0.1806 0.2144
REMARK 3 6 3.3160 - 3.1205 1.00 2556 145 0.1819 0.2304
REMARK 3 7 3.1205 - 2.9643 1.00 2563 120 0.1795 0.2251
REMARK 3 8 2.9643 - 2.8353 1.00 2549 156 0.1817 0.2149
REMARK 3 9 2.8353 - 2.7262 1.00 2541 137 0.1792 0.2184
REMARK 3 10 2.7262 - 2.6321 1.00 2567 143 0.1883 0.2142
REMARK 3 11 2.6321 - 2.5498 1.00 2544 137 0.2003 0.2417
REMARK 3 12 2.5498 - 2.4770 1.00 2525 155 0.2018 0.2572
REMARK 3 13 2.4770 - 2.4118 1.00 2584 118 0.2081 0.2280
REMARK 3 14 2.4118 - 2.3529 1.00 2558 122 0.2100 0.2375
REMARK 3 15 2.3529 - 2.2995 1.00 2542 149 0.2163 0.2606
REMARK 3 16 2.2995 - 2.2510 1.00 2526 139 0.2360 0.2676
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.03
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 : 0.008 3299
REMARK 3 ANGLE : 1.136 4508
REMARK 3 CHIRALITY : 0.075 518
REMARK 3 PLANARITY : 0.005 572
REMARK 3 DIHEDRAL : 13.442 1161
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'L' AND (RESSEQ 5:91)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.1523 -60.1726 -8.1799
REMARK 3 T TENSOR
REMARK 3 T11: 0.3739 T22: 0.9965
REMARK 3 T33: 0.5401 T12: -0.0463
REMARK 3 T13: 0.0232 T23: -0.0950
REMARK 3 L TENSOR
REMARK 3 L11: 7.2190 L22: 3.6265
REMARK 3 L33: 4.7821 L12: -1.7727
REMARK 3 L13: 2.0239 L23: -1.1765
REMARK 3 S TENSOR
REMARK 3 S11: -0.0828 S12: 1.0343 S13: -0.3626
REMARK 3 S21: -0.2616 S22: -0.1147 S23: 0.0134
REMARK 3 S31: -0.3871 S32: 0.0919 S33: 0.1687
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'L' AND (RESSEQ 92:130)
REMARK 3 ORIGIN FOR THE GROUP (A): -23.6934 -59.1450 -7.1496
REMARK 3 T TENSOR
REMARK 3 T11: 0.3962 T22: 0.5455
REMARK 3 T33: 0.4678 T12: 0.1401
REMARK 3 T13: -0.0044 T23: -0.0709
REMARK 3 L TENSOR
REMARK 3 L11: 4.1407 L22: 0.5920
REMARK 3 L33: 1.5968 L12: 0.9936
REMARK 3 L13: 2.0459 L23: 0.0403
REMARK 3 S TENSOR
REMARK 3 S11: 0.0329 S12: 0.4048 S13: 0.1164
REMARK 3 S21: 0.0824 S22: 0.0719 S23: -0.1701
REMARK 3 S31: -0.1712 S32: 0.4125 S33: -0.0692
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'L' AND (RESSEQ 131:211)
REMARK 3 ORIGIN FOR THE GROUP (A): -38.4871 -56.5726 -12.8195
REMARK 3 T TENSOR
REMARK 3 T11: 0.3473 T22: 0.4461
REMARK 3 T33: 0.3125 T12: 0.1541
REMARK 3 T13: -0.0322 T23: -0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 1.5241 L22: 3.0099
REMARK 3 L33: 5.3079 L12: 1.2117
REMARK 3 L13: 0.1918 L23: -0.1383
REMARK 3 S TENSOR
REMARK 3 S11: 0.0034 S12: 0.0244 S13: 0.1983
REMARK 3 S21: -0.0358 S22: 0.0396 S23: -0.0076
REMARK 3 S31: -0.5621 S32: -0.0905 S33: -0.0160
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'H' AND (RESSEQ 2:52)
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9097 -60.5973 13.1263
REMARK 3 T TENSOR
REMARK 3 T11: 0.3838 T22: 0.9217
REMARK 3 T33: 0.5582 T12: -0.0186
REMARK 3 T13: 0.0033 T23: 0.0923
REMARK 3 L TENSOR
REMARK 3 L11: 5.9559 L22: 3.8128
REMARK 3 L33: 2.9728 L12: -1.7470
REMARK 3 L13: -0.2036 L23: 0.0521
REMARK 3 S TENSOR
REMARK 3 S11: -0.0795 S12: -0.7106 S13: -0.3935
REMARK 3 S21: 0.0814 S22: -0.2175 S23: -0.0759
REMARK 3 S31: -0.1529 S32: 0.5228 S33: 0.2813
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'H' AND (RESSEQ 53:121)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.9833 -59.1028 14.1752
REMARK 3 T TENSOR
REMARK 3 T11: 0.4281 T22: 1.0027
REMARK 3 T33: 0.5252 T12: -0.0526
REMARK 3 T13: -0.0321 T23: 0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 7.0407 L22: 1.1232
REMARK 3 L33: 0.6278 L12: -1.9199
REMARK 3 L13: -0.4631 L23: 0.3035
REMARK 3 S TENSOR
REMARK 3 S11: -0.1234 S12: -1.2828 S13: -0.0037
REMARK 3 S21: 0.2804 S22: 0.1328 S23: -0.2061
REMARK 3 S31: -0.2876 S32: 0.5687 S33: 0.0139
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'H' AND (RESSEQ 122:187)
REMARK 3 ORIGIN FOR THE GROUP (A): -33.9979 -64.3803 -0.1957
REMARK 3 T TENSOR
REMARK 3 T11: 0.3263 T22: 0.4610
REMARK 3 T33: 0.3622 T12: 0.1342
REMARK 3 T13: -0.0118 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 3.3095 L22: 1.9628
REMARK 3 L33: 4.5590 L12: 1.2891
REMARK 3 L13: 2.0560 L23: 1.3812
REMARK 3 S TENSOR
REMARK 3 S11: -0.0868 S12: 0.1944 S13: 0.2327
REMARK 3 S21: -0.1862 S22: -0.0837 S23: 0.1661
REMARK 3 S31: -0.1749 S32: 0.1691 S33: 0.1888
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'H' AND (RESSEQ 188:223)
REMARK 3 ORIGIN FOR THE GROUP (A): -35.8621 -73.1688 1.0375
REMARK 3 T TENSOR
REMARK 3 T11: 0.3853 T22: 0.4425
REMARK 3 T33: 0.3935 T12: 0.1372
REMARK 3 T13: 0.0016 T23: -0.0223
REMARK 3 L TENSOR
REMARK 3 L11: 3.8701 L22: 1.5924
REMARK 3 L33: 4.1827 L12: 0.4682
REMARK 3 L13: 1.7061 L23: 0.4203
REMARK 3 S TENSOR
REMARK 3 S11: 0.1827 S12: -0.1115 S13: -0.4689
REMARK 3 S21: 0.2425 S22: -0.2228 S23: 0.2381
REMARK 3 S31: 0.7444 S32: -0.1383 S33: -0.0246
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 4GSD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-SEP-12.
REMARK 100 THE DEPOSITION ID IS D_1000074575.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43198
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.57100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1FGW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG 1500 AND 20% GLYCEROL, 21
REMARK 280 MG/ML PROTEIN, PH 7.5, VAPOR DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 23.50567
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 47.01133
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 35.25850
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 58.76417
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 11.75283
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER L 2
REMARK 465 TYR L 3
REMARK 465 GLU L 4
REMARK 465 CYS L 212
REMARK 465 SER L 213
REMARK 465 GLU H 1
REMARK 465 LYS H 224
REMARK 465 SER H 225
REMARK 465 CYS H 226
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 HOH L 382 O HOH H 384 1.86
REMARK 500 O HOH H 383 O HOH H 386 1.93
REMARK 500 O HOH L 377 O HOH H 386 1.95
REMARK 500 O HOH L 337 O HOH L 338 1.96
REMARK 500 OD1 ASP H 111 O HOH H 372 2.04
REMARK 500 O HOH L 368 O HOH L 371 2.05
REMARK 500 OG SER H 198 O HOH H 336 2.05
REMARK 500 NZ LYS H 127 O HOH H 342 2.10
REMARK 500 O HOH L 352 O HOH L 384 2.11
REMARK 500 OG SER L 65 O HOH L 351 2.16
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 ASP L 51 -38.07 70.60
REMARK 500 ARG L 108 36.85 -86.09
REMARK 500 SER H 15 -3.28 73.45
REMARK 500 SER H 30 2.92 -69.51
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4GSD L 2 213 PDB 4GSD 4GSD 2 213
DBREF 4GSD H 1 226 PDB 4GSD 4GSD 1 226
SEQRES 1 L 212 SER TYR GLU LEU THR GLN PRO PRO SER VAL SER VAL SER
SEQRES 2 L 212 PRO GLY GLN THR VAL ASN ILE THR CYS SER GLY ASP THR
SEQRES 3 L 212 LEU GLY ASP LYS TYR VAL CYS TRP TYR GLN GLN LYS PRO
SEQRES 4 L 212 GLY GLN SER PRO VAL LEU VAL ILE TYR GLN ASP THR LYS
SEQRES 5 L 212 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER ASN
SEQRES 6 L 212 SER GLY ASP THR ALA THR LEU THR VAL SER GLY THR GLN
SEQRES 7 L 212 ALA MET ASP GLU ALA ASP TYR TYR CYS GLN ALA TRP ASP
SEQRES 8 L 212 SER SER SER PHE VAL PHE GLY THR GLY THR LYS VAL THR
SEQRES 9 L 212 VAL LEU ARG GLN PRO LYS ALA ASN PRO THR VAL THR LEU
SEQRES 10 L 212 PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA
SEQRES 11 L 212 THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA
SEQRES 12 L 212 VAL THR VAL ALA TRP LYS ALA ASP GLY SER PRO VAL LYS
SEQRES 13 L 212 ALA GLY VAL GLU THR THR LYS PRO SER LYS GLN SER ASN
SEQRES 14 L 212 ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU THR PRO
SEQRES 15 L 212 GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS GLN VAL
SEQRES 16 L 212 THR HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO
SEQRES 17 L 212 THR GLU CYS SER
SEQRES 1 H 226 GLU VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS
SEQRES 2 H 226 PRO SER GLY THR VAL SER LEU THR CYS ALA VAL SER GLY
SEQRES 3 H 226 GLY SER ILE SER SER SER TYR TRP TRP SER TRP VAL ARG
SEQRES 4 H 226 GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY GLU ILE
SEQRES 5 H 226 TYR HIS SER GLY ASN THR ASN TYR ASN PRO SER LEU LYS
SEQRES 6 H 226 SER ARG VAL THR ILE SER VAL ASP LYS SER LYS ASN LEU
SEQRES 7 H 226 PHE SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR
SEQRES 8 H 226 ALA VAL TYR TYR CYS ALA ARG VAL ALA LEU PHE ASP ILE
SEQRES 9 H 226 LEU THR GLY GLY TRP PHE ASP PRO TRP GLY GLN GLY THR
SEQRES 10 H 226 LEU VAL THR VAL SER SER ALA GLY THR LYS GLY PRO SER
SEQRES 11 H 226 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY
SEQRES 12 H 226 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE
SEQRES 13 H 226 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU
SEQRES 14 H 226 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER
SEQRES 15 H 226 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO
SEQRES 16 H 226 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL
SEQRES 17 H 226 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL
SEQRES 18 H 226 GLU PRO LYS SER CYS
FORMUL 3 HOH *188(H2 O)
HELIX 1 1 THR L 27 LYS L 31 5 5
HELIX 2 2 GLN L 79 GLU L 83 5 5
HELIX 3 3 SER L 122 ALA L 128 1 7
HELIX 4 4 THR L 182 SER L 188 1 7
HELIX 5 5 LYS H 74 LYS H 76 5 3
HELIX 6 6 THR H 87 THR H 91 5 5
HELIX 7 7 SER H 137 LYS H 139 5 3
HELIX 8 8 SER H 166 ALA H 168 5 3
HELIX 9 9 SER H 197 LEU H 199 5 3
HELIX 10 10 LYS H 211 ASN H 214 5 4
SHEET 1 A 5 SER L 10 VAL L 13 0
SHEET 2 A 5 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11
SHEET 3 A 5 ASP L 85 TRP L 91 -1 N TYR L 86 O THR L 102
SHEET 4 A 5 TYR L 32 GLN L 38 -1 N CYS L 34 O GLN L 89
SHEET 5 A 5 VAL L 45 ILE L 48 -1 O VAL L 47 N TRP L 35
SHEET 1 B 4 SER L 10 VAL L 13 0
SHEET 2 B 4 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11
SHEET 3 B 4 ASP L 85 TRP L 91 -1 N TYR L 86 O THR L 102
SHEET 4 B 4 PHE L 96 PHE L 98 -1 O VAL L 97 N ALA L 90
SHEET 1 C 3 VAL L 19 SER L 24 0
SHEET 2 C 3 THR L 70 VAL L 75 -1 O ALA L 71 N CYS L 23
SHEET 3 C 3 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74
SHEET 1 D 4 THR L 115 PHE L 119 0
SHEET 2 D 4 ALA L 131 PHE L 140 -1 O LEU L 136 N THR L 117
SHEET 3 D 4 TYR L 173 LEU L 181 -1 O LEU L 181 N ALA L 131
SHEET 4 D 4 VAL L 160 THR L 162 -1 N GLU L 161 O TYR L 178
SHEET 1 E 4 THR L 115 PHE L 119 0
SHEET 2 E 4 ALA L 131 PHE L 140 -1 O LEU L 136 N THR L 117
SHEET 3 E 4 TYR L 173 LEU L 181 -1 O LEU L 181 N ALA L 131
SHEET 4 E 4 SER L 166 LYS L 167 -1 N SER L 166 O ALA L 174
SHEET 1 F 4 SER L 154 PRO L 155 0
SHEET 2 F 4 THR L 146 ALA L 151 -1 N ALA L 151 O SER L 154
SHEET 3 F 4 TYR L 192 HIS L 198 -1 O GLN L 195 N ALA L 148
SHEET 4 F 4 SER L 201 VAL L 207 -1 O VAL L 203 N VAL L 196
SHEET 1 G 4 GLN H 3 GLU H 6 0
SHEET 2 G 4 VAL H 18 SER H 25 -1 O ALA H 23 N GLN H 5
SHEET 3 G 4 LEU H 78 LEU H 83 -1 O LEU H 81 N LEU H 20
SHEET 4 G 4 VAL H 68 ASP H 73 -1 N THR H 69 O LYS H 82
SHEET 1 H 6 GLY H 10 VAL H 12 0
SHEET 2 H 6 THR H 117 VAL H 121 1 O THR H 120 N VAL H 12
SHEET 3 H 6 ALA H 92 ALA H 100 -1 N TYR H 94 O THR H 117
SHEET 4 H 6 TYR H 33 GLN H 40 -1 N VAL H 38 O TYR H 95
SHEET 5 H 6 GLU H 47 ILE H 52 -1 O ILE H 49 N TRP H 37
SHEET 6 H 6 THR H 58 TYR H 60 -1 O ASN H 59 N GLU H 51
SHEET 1 I 4 GLY H 10 VAL H 12 0
SHEET 2 I 4 THR H 117 VAL H 121 1 O THR H 120 N VAL H 12
SHEET 3 I 4 ALA H 92 ALA H 100 -1 N TYR H 94 O THR H 117
SHEET 4 I 4 PHE H 110 TRP H 113 -1 O ASP H 111 N ARG H 98
SHEET 1 J 4 SER H 130 LEU H 134 0
SHEET 2 J 4 THR H 145 TYR H 155 -1 O LYS H 153 N SER H 130
SHEET 3 J 4 TYR H 186 PRO H 195 -1 O VAL H 192 N LEU H 148
SHEET 4 J 4 VAL H 173 THR H 175 -1 N HIS H 174 O VAL H 191
SHEET 1 K 4 THR H 141 SER H 142 0
SHEET 2 K 4 THR H 145 TYR H 155 -1 O THR H 145 N SER H 142
SHEET 3 K 4 TYR H 186 PRO H 195 -1 O VAL H 192 N LEU H 148
SHEET 4 K 4 VAL H 179 LEU H 180 -1 N VAL H 179 O SER H 187
SHEET 1 L 3 THR H 161 TRP H 164 0
SHEET 2 L 3 ILE H 205 HIS H 210 -1 O ASN H 209 N THR H 161
SHEET 3 L 3 THR H 215 ARG H 220 -1 O THR H 215 N HIS H 210
SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.04
SSBOND 2 CYS L 135 CYS L 194 1555 1555 2.04
SSBOND 3 CYS H 22 CYS H 96 1555 1555 2.13
SSBOND 4 CYS H 150 CYS H 206 1555 1555 2.05
CISPEP 1 TYR L 141 PRO L 142 0 0.53
CISPEP 2 ASP H 111 PRO H 112 0 -7.15
CISPEP 3 PHE H 156 PRO H 157 0 -5.69
CISPEP 4 GLU H 158 PRO H 159 0 4.46
CRYST1 150.430 150.430 70.517 90.00 90.00 120.00 P 61 6
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006648 0.003838 0.000000 0.00000
SCALE2 0.000000 0.007676 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014181 0.00000
(ATOM LINES ARE NOT SHOWN.)
END