HEADER IMMUNE SYSTEM 22-OCT-18 6MUB
TITLE ANTI-HIV-1 FAB 2G12 + MAN5 RE-REFINEMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FAB 2G12, LIGHT CHAIN;
COMPND 3 CHAIN: L, K;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: FAB 2G12, HEAVY CHAIN;
COMPND 7 CHAIN: H, M;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 EXPRESSION_SYSTEM_ORGAN: OVARY;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 14 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 16 EXPRESSION_SYSTEM_ORGAN: OVARY
KEYWDS ANTIBODY, CARBOHYDRATE, HIV-1, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR I.A.WILSON,D.A.CALARESE,R.L.STANFIELD
REVDAT 5 11-OCT-23 6MUB 1 HETSYN LINK
REVDAT 4 29-JUL-20 6MUB 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 01-JAN-20 6MUB 1 REMARK
REVDAT 2 13-NOV-19 6MUB 1 JRNL
REVDAT 1 31-OCT-18 6MUB 0
SPRSDE 31-OCT-18 6MUB 1ZLU
JRNL AUTH D.A.CALARESE,H.K.LEE,C.Y.HUANG,M.D.BEST,R.D.ASTRONOMO,
JRNL AUTH 2 R.L.STANFIELD,H.KATINGER,D.R.BURTON,C.H.WONG,I.A.WILSON
JRNL TITL DISSECTION OF THE CARBOHYDRATE SPECIFICITY OF THE BROADLY
JRNL TITL 2 NEUTRALIZING ANTI-HIV-1 ANTIBODY 2G12.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 13372 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 16174734
JRNL DOI 10.1073/PNAS.0505763102
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12_2829)
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.5
REMARK 3 NUMBER OF REFLECTIONS : 31731
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.247
REMARK 3 R VALUE (WORKING SET) : 0.245
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 1570
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 43.4098 - 5.5625 0.97 3203 190 0.2134 0.2390
REMARK 3 2 5.5625 - 4.4165 0.98 3098 173 0.1858 0.2284
REMARK 3 3 4.4165 - 3.8586 0.99 3104 148 0.2101 0.2393
REMARK 3 4 3.8586 - 3.5060 0.99 3089 133 0.2523 0.2906
REMARK 3 5 3.5060 - 3.2548 0.99 3062 133 0.2787 0.3262
REMARK 3 6 3.2548 - 3.0629 0.98 2993 177 0.3035 0.3160
REMARK 3 7 3.0629 - 2.9096 0.98 2983 166 0.3275 0.3865
REMARK 3 8 2.9096 - 2.7829 0.95 2890 154 0.3320 0.3857
REMARK 3 9 2.7829 - 2.6758 0.80 2474 123 0.3469 0.4084
REMARK 3 10 2.6758 - 2.5835 0.60 1822 101 0.3325 0.3532
REMARK 3 11 2.5835 - 2.5027 0.48 1443 72 0.3401 0.3859
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) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.270
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 46.50
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 : 0.003 6866
REMARK 3 ANGLE : 0.621 9359
REMARK 3 CHIRALITY : 0.045 1096
REMARK 3 PLANARITY : 0.005 1168
REMARK 3 DIHEDRAL : 14.151 4132
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 6MUB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1000237606.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUL-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32006
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 89.3
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 50.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.37500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
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: 1OM3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M SODIUM/POTASSIUM PHOSPHATE, PH
REMARK 280 6.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 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
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 22.44300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.13650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.89350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.13650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.44300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.89350
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, K, M, A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 GLU L 213
REMARK 465 CYS H 230
REMARK 465 SER M 130
REMARK 465 LYS M 131
REMARK 465 SER M 132
REMARK 465 THR M 133
REMARK 465 SER M 134
REMARK 465 GLY M 135
REMARK 465 CYS M 230
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 SER M 127 OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU L 30 -118.45 54.16
REMARK 500 ALA L 51 -42.50 66.46
REMARK 500 ASN L 138 76.43 55.85
REMARK 500 PRO L 141 -169.29 -77.48
REMARK 500 ARG L 211 106.62 -58.97
REMARK 500 SER H 53 15.48 59.48
REMARK 500 SER H 97 -169.98 -162.54
REMARK 500 ASN H 100C 94.09 -162.81
REMARK 500 ASP H 146 68.28 63.90
REMARK 500 THR H 200 -61.22 -100.18
REMARK 500 GLU K 30 -114.69 50.87
REMARK 500 ALA K 51 -43.60 67.30
REMARK 500 ASN K 138 76.44 55.94
REMARK 500 PRO K 141 -169.94 -77.55
REMARK 500 ARG K 211 109.91 -58.80
REMARK 500 ASN M 100C 94.36 -163.53
REMARK 500 ASP M 146 70.07 63.01
REMARK 500 LYS M 228 164.33 70.14
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6MUB L 1 109 PDB 6MUB 6MUB 1 109
DBREF 6MUB L 110 213 UNP P0DOX7 IGK_HUMAN 110 213
DBREF 6MUB H 1 113 PDB 6MUB 6MUB 1 113
DBREF 6MUB H 114 230 UNP P0DOX5 IGG1_HUMAN 120 222
DBREF 6MUB K 1 109 PDB 6MUB 6MUB 1 109
DBREF 6MUB K 110 213 UNP P0DOX7 IGK_HUMAN 110 213
DBREF 6MUB M 1 113 PDB 6MUB 6MUB 1 113
DBREF 6MUB M 114 230 UNP P0DOX5 IGG1_HUMAN 120 222
SEQRES 1 L 213 ASP VAL VAL MET THR GLN SER PRO SER THR LEU SER ALA
SEQRES 2 L 213 SER VAL GLY ASP THR ILE THR ILE THR CYS ARG ALA SER
SEQRES 3 L 213 GLN SER ILE GLU THR TRP LEU ALA TRP TYR GLN GLN LYS
SEQRES 4 L 213 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR LYS ALA SER
SEQRES 5 L 213 THR LEU LYS THR GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 L 213 GLY SER GLY THR GLU PHE THR LEU THR ILE SER GLY LEU
SEQRES 7 L 213 GLN PHE ASP ASP PHE ALA THR TYR HIS CYS GLN HIS TYR
SEQRES 8 L 213 ALA GLY TYR SER ALA THR PHE GLY GLN GLY THR ARG VAL
SEQRES 9 L 213 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 L 213 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 L 213 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 L 213 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 L 213 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 L 213 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 L 213 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 L 213 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 L 213 PHE ASN ARG GLY GLU
SEQRES 1 H 226 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS
SEQRES 2 H 226 ALA GLY GLY SER LEU ILE LEU SER CYS GLY VAL SER ASN
SEQRES 3 H 226 PHE ARG ILE SER ALA HIS THR MET ASN TRP VAL ARG ARG
SEQRES 4 H 226 VAL PRO GLY GLY GLY LEU GLU TRP VAL ALA SER ILE SER
SEQRES 5 H 226 THR SER SER THR TYR ARG ASP TYR ALA ASP ALA VAL LYS
SEQRES 6 H 226 GLY ARG PHE THR VAL SER ARG ASP ASP LEU GLU ASP PHE
SEQRES 7 H 226 VAL TYR LEU GLN MET HIS LYS MET ARG VAL GLU ASP THR
SEQRES 8 H 226 ALA ILE TYR TYR CYS ALA ARG LYS GLY SER ASP ARG LEU
SEQRES 9 H 226 SER ASP ASN ASP PRO PHE ASP ALA TRP GLY PRO GLY THR
SEQRES 10 H 226 VAL VAL THR VAL SER PRO ALA SER 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 LYS VAL
SEQRES 18 H 226 GLU PRO LYS SER CYS
SEQRES 1 K 213 ASP VAL VAL MET THR GLN SER PRO SER THR LEU SER ALA
SEQRES 2 K 213 SER VAL GLY ASP THR ILE THR ILE THR CYS ARG ALA SER
SEQRES 3 K 213 GLN SER ILE GLU THR TRP LEU ALA TRP TYR GLN GLN LYS
SEQRES 4 K 213 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR LYS ALA SER
SEQRES 5 K 213 THR LEU LYS THR GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 K 213 GLY SER GLY THR GLU PHE THR LEU THR ILE SER GLY LEU
SEQRES 7 K 213 GLN PHE ASP ASP PHE ALA THR TYR HIS CYS GLN HIS TYR
SEQRES 8 K 213 ALA GLY TYR SER ALA THR PHE GLY GLN GLY THR ARG VAL
SEQRES 9 K 213 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 K 213 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 K 213 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 K 213 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 K 213 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 K 213 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 K 213 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 K 213 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 K 213 PHE ASN ARG GLY GLU
SEQRES 1 M 226 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS
SEQRES 2 M 226 ALA GLY GLY SER LEU ILE LEU SER CYS GLY VAL SER ASN
SEQRES 3 M 226 PHE ARG ILE SER ALA HIS THR MET ASN TRP VAL ARG ARG
SEQRES 4 M 226 VAL PRO GLY GLY GLY LEU GLU TRP VAL ALA SER ILE SER
SEQRES 5 M 226 THR SER SER THR TYR ARG ASP TYR ALA ASP ALA VAL LYS
SEQRES 6 M 226 GLY ARG PHE THR VAL SER ARG ASP ASP LEU GLU ASP PHE
SEQRES 7 M 226 VAL TYR LEU GLN MET HIS LYS MET ARG VAL GLU ASP THR
SEQRES 8 M 226 ALA ILE TYR TYR CYS ALA ARG LYS GLY SER ASP ARG LEU
SEQRES 9 M 226 SER ASP ASN ASP PRO PHE ASP ALA TRP GLY PRO GLY THR
SEQRES 10 M 226 VAL VAL THR VAL SER PRO ALA SER THR LYS GLY PRO SER
SEQRES 11 M 226 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY
SEQRES 12 M 226 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE
SEQRES 13 M 226 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU
SEQRES 14 M 226 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER
SEQRES 15 M 226 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO
SEQRES 16 M 226 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL
SEQRES 17 M 226 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL
SEQRES 18 M 226 GLU PRO LYS SER CYS
HET BMA A 1 12
HET MAN A 2 11
HET MAN A 3 11
HET MAN A 4 11
HET MAN A 5 11
HET BMA B 1 12
HET MAN B 2 11
HET MAN B 3 11
HET MAN B 4 11
HET MAN B 5 11
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 5 BMA 2(C6 H12 O6)
FORMUL 5 MAN 8(C6 H12 O6)
FORMUL 7 HOH *6(H2 O)
HELIX 1 AA1 GLN L 79 PHE L 83 5 5
HELIX 2 AA2 SER L 121 SER L 127 1 7
HELIX 3 AA3 LYS L 183 LYS L 188 1 6
HELIX 4 AA4 THR H 52A THR H 55 5 4
HELIX 5 AA5 ARG H 83 THR H 87 5 5
HELIX 6 AA6 SER H 163 ALA H 165 5 3
HELIX 7 AA7 SER H 196 GLY H 199 5 4
HELIX 8 AA8 LYS H 213 ASN H 216 5 4
HELIX 9 AA9 GLN K 79 PHE K 83 5 5
HELIX 10 AB1 SER K 121 SER K 127 1 7
HELIX 11 AB2 LYS K 183 LYS K 188 1 6
HELIX 12 AB3 THR M 52A THR M 55 5 4
HELIX 13 AB4 ARG M 83 THR M 87 5 5
HELIX 14 AB5 SER M 163 ALA M 165 5 3
HELIX 15 AB6 SER M 196 GLY M 199 5 4
HELIX 16 AB7 LYS M 213 ASN M 216 5 4
SHEET 1 AA1 4 MET L 4 SER L 7 0
SHEET 2 AA1 4 THR L 18 ALA L 25 -1 O THR L 22 N SER L 7
SHEET 3 AA1 4 GLU L 70 SER L 76 -1 O PHE L 71 N CYS L 23
SHEET 4 AA1 4 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72
SHEET 1 AA2 6 THR L 10 ALA L 13 0
SHEET 2 AA2 6 THR L 102 ILE L 106 1 O ARG L 103 N LEU L 11
SHEET 3 AA2 6 THR L 85 TYR L 91 -1 N TYR L 86 O THR L 102
SHEET 4 AA2 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85
SHEET 5 AA2 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37
SHEET 6 AA2 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49
SHEET 1 AA3 4 THR L 10 ALA L 13 0
SHEET 2 AA3 4 THR L 102 ILE L 106 1 O ARG L 103 N LEU L 11
SHEET 3 AA3 4 THR L 85 TYR L 91 -1 N TYR L 86 O THR L 102
SHEET 4 AA3 4 ALA L 96 PHE L 98 -1 O THR L 97 N HIS L 90
SHEET 1 AA4 4 SER L 114 PHE L 118 0
SHEET 2 AA4 4 THR L 129 PHE L 139 -1 O VAL L 133 N PHE L 118
SHEET 3 AA4 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132
SHEET 4 AA4 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178
SHEET 1 AA5 4 ALA L 153 LEU L 154 0
SHEET 2 AA5 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153
SHEET 3 AA5 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147
SHEET 4 AA5 4 VAL L 205 ASN L 210 -1 O PHE L 209 N TYR L 192
SHEET 1 AA6 4 GLN H 3 SER H 7 0
SHEET 2 AA6 4 LEU H 18 SER H 25 -1 O GLY H 23 N VAL H 5
SHEET 3 AA6 4 PHE H 77 MET H 82 -1 O LEU H 80 N LEU H 20
SHEET 4 AA6 4 PHE H 67 ASP H 72 -1 N SER H 70 O TYR H 79
SHEET 1 AA7 6 GLY H 10 LYS H 13 0
SHEET 2 AA7 6 THR H 107 SER H 112 1 O SER H 112 N VAL H 12
SHEET 3 AA7 6 ALA H 88 LYS H 95 -1 N TYR H 90 O THR H 107
SHEET 4 AA7 6 THR H 33 ARG H 39 -1 N VAL H 37 O TYR H 91
SHEET 5 AA7 6 LEU H 45 ILE H 51 -1 O ILE H 51 N MET H 34
SHEET 6 AA7 6 ARG H 57 TYR H 59 -1 O ASP H 58 N SER H 50
SHEET 1 AA8 4 GLY H 10 LYS H 13 0
SHEET 2 AA8 4 THR H 107 SER H 112 1 O SER H 112 N VAL H 12
SHEET 3 AA8 4 ALA H 88 LYS H 95 -1 N TYR H 90 O THR H 107
SHEET 4 AA8 4 PHE H 100F TRP H 103 -1 O ALA H 102 N ARG H 94
SHEET 1 AA9 4 SER H 120 LEU H 124 0
SHEET 2 AA9 4 THR H 137 TYR H 147 -1 O GLY H 141 N LEU H 124
SHEET 3 AA9 4 TYR H 185 PRO H 194 -1 O TYR H 185 N TYR H 147
SHEET 4 AA9 4 VAL H 171 THR H 173 -1 N HIS H 172 O VAL H 190
SHEET 1 AB1 4 THR H 133 SER H 134 0
SHEET 2 AB1 4 THR H 137 TYR H 147 -1 O THR H 137 N SER H 134
SHEET 3 AB1 4 TYR H 185 PRO H 194 -1 O TYR H 185 N TYR H 147
SHEET 4 AB1 4 VAL H 177 LEU H 178 -1 N VAL H 177 O SER H 186
SHEET 1 AB2 3 THR H 153 TRP H 157 0
SHEET 2 AB2 3 ILE H 207 HIS H 212 -1 O ASN H 211 N THR H 153
SHEET 3 AB2 3 THR H 217 LYS H 222 -1 O VAL H 219 N VAL H 210
SHEET 1 AB3 4 MET K 4 SER K 7 0
SHEET 2 AB3 4 THR K 18 ALA K 25 -1 O ARG K 24 N THR K 5
SHEET 3 AB3 4 GLU K 70 SER K 76 -1 O PHE K 71 N CYS K 23
SHEET 4 AB3 4 PHE K 62 SER K 67 -1 N SER K 65 O THR K 72
SHEET 1 AB4 6 THR K 10 ALA K 13 0
SHEET 2 AB4 6 THR K 102 ILE K 106 1 O ARG K 103 N LEU K 11
SHEET 3 AB4 6 THR K 85 TYR K 91 -1 N TYR K 86 O THR K 102
SHEET 4 AB4 6 ALA K 34 GLN K 38 -1 N GLN K 38 O THR K 85
SHEET 5 AB4 6 LYS K 45 TYR K 49 -1 O LYS K 45 N GLN K 37
SHEET 6 AB4 6 THR K 53 LEU K 54 -1 O THR K 53 N TYR K 49
SHEET 1 AB5 4 THR K 10 ALA K 13 0
SHEET 2 AB5 4 THR K 102 ILE K 106 1 O ARG K 103 N LEU K 11
SHEET 3 AB5 4 THR K 85 TYR K 91 -1 N TYR K 86 O THR K 102
SHEET 4 AB5 4 ALA K 96 PHE K 98 -1 O THR K 97 N HIS K 90
SHEET 1 AB6 4 SER K 114 PHE K 118 0
SHEET 2 AB6 4 THR K 129 PHE K 139 -1 O VAL K 133 N PHE K 118
SHEET 3 AB6 4 TYR K 173 SER K 182 -1 O LEU K 179 N VAL K 132
SHEET 4 AB6 4 SER K 159 VAL K 163 -1 N GLN K 160 O THR K 178
SHEET 1 AB7 4 ALA K 153 LEU K 154 0
SHEET 2 AB7 4 LYS K 145 VAL K 150 -1 N VAL K 150 O ALA K 153
SHEET 3 AB7 4 VAL K 191 THR K 197 -1 O GLU K 195 N GLN K 147
SHEET 4 AB7 4 VAL K 205 ASN K 210 -1 O LYS K 207 N CYS K 194
SHEET 1 AB8 4 GLN M 3 SER M 7 0
SHEET 2 AB8 4 LEU M 18 SER M 25 -1 O GLY M 23 N VAL M 5
SHEET 3 AB8 4 PHE M 77 MET M 82 -1 O LEU M 80 N LEU M 20
SHEET 4 AB8 4 PHE M 67 ASP M 72 -1 N SER M 70 O TYR M 79
SHEET 1 AB9 6 GLY M 10 LYS M 13 0
SHEET 2 AB9 6 THR M 107 SER M 112 1 O SER M 112 N VAL M 12
SHEET 3 AB9 6 ALA M 88 LYS M 95 -1 N TYR M 90 O THR M 107
SHEET 4 AB9 6 MET M 34 ARG M 39 -1 N VAL M 37 O TYR M 91
SHEET 5 AB9 6 LEU M 45 ILE M 51 -1 O GLU M 46 N ARG M 38
SHEET 6 AB9 6 ARG M 57 TYR M 59 -1 O ASP M 58 N SER M 50
SHEET 1 AC1 4 GLY M 10 LYS M 13 0
SHEET 2 AC1 4 THR M 107 SER M 112 1 O SER M 112 N VAL M 12
SHEET 3 AC1 4 ALA M 88 LYS M 95 -1 N TYR M 90 O THR M 107
SHEET 4 AC1 4 PHE M 100F TRP M 103 -1 O ALA M 102 N ARG M 94
SHEET 1 AC2 4 SER M 120 LEU M 124 0
SHEET 2 AC2 4 THR M 137 TYR M 147 -1 O LYS M 145 N SER M 120
SHEET 3 AC2 4 TYR M 185 PRO M 194 -1 O TYR M 185 N TYR M 147
SHEET 4 AC2 4 VAL M 171 THR M 173 -1 N HIS M 172 O VAL M 190
SHEET 1 AC3 4 SER M 120 LEU M 124 0
SHEET 2 AC3 4 THR M 137 TYR M 147 -1 O LYS M 145 N SER M 120
SHEET 3 AC3 4 TYR M 185 PRO M 194 -1 O TYR M 185 N TYR M 147
SHEET 4 AC3 4 VAL M 177 LEU M 178 -1 N VAL M 177 O SER M 186
SHEET 1 AC4 3 THR M 153 TRP M 157 0
SHEET 2 AC4 3 ILE M 207 HIS M 212 -1 O ASN M 211 N THR M 153
SHEET 3 AC4 3 THR M 217 LYS M 222 -1 O VAL M 219 N VAL M 210
SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.04
SSBOND 2 CYS L 134 CYS L 194 1555 1555 2.04
SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.04
SSBOND 4 CYS H 142 CYS H 208 1555 1555 2.04
SSBOND 5 CYS K 23 CYS K 88 1555 1555 2.04
SSBOND 6 CYS K 134 CYS K 194 1555 1555 2.04
SSBOND 7 CYS M 22 CYS M 92 1555 1555 2.04
SSBOND 8 CYS M 142 CYS M 208 1555 1555 2.04
LINK O3 BMA A 1 C1 MAN A 2 1555 1555 1.45
LINK O6 BMA A 1 C1 MAN A 4 1555 1555 1.44
LINK O2 MAN A 2 C1 MAN A 3 1555 1555 1.45
LINK O2 MAN A 4 C1 MAN A 5 1555 1555 1.45
LINK O3 BMA B 1 C1 MAN B 2 1555 1555 1.45
LINK O6 BMA B 1 C1 MAN B 4 1555 1555 1.44
LINK O2 MAN B 2 C1 MAN B 3 1555 1555 1.45
LINK O2 MAN B 4 C1 MAN B 5 1555 1555 1.45
CISPEP 1 SER L 7 PRO L 8 0 -3.75
CISPEP 2 TYR L 140 PRO L 141 0 6.29
CISPEP 3 PHE H 148 PRO H 149 0 -4.95
CISPEP 4 GLU H 150 PRO H 151 0 -0.36
CISPEP 5 SER K 7 PRO K 8 0 -3.48
CISPEP 6 TYR K 140 PRO K 141 0 6.38
CISPEP 7 PHE M 148 PRO M 149 0 -4.77
CISPEP 8 GLU M 150 PRO M 151 0 -0.05
CRYST1 44.886 131.787 170.273 90.00 90.00 90.00 P 21 21 21 8
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 0.022279 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007588 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005873 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
