HEADER IMMUNE SYSTEM 31-MAY-19 6RV6
TITLE STRUCTURE OF PROPERDIN LACKING TSR3 BASED ON ANOMALOUS DATA
CAVEAT 6RV6 FUC F 3 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROPERDIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: COMPLEMENT FACTOR P;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: TB-TSR1-TSR2 AND ADDITIONAL RESIDUES FROM EXPRESSION
COMPND 7 VECTOR;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PROPERDIN;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: COMPLEMENT FACTOR P;
COMPND 12 ENGINEERED: YES;
COMPND 13 OTHER_DETAILS: TSR4-5-6 WITH ADDIOTIONAL RESIDUES FROM EXPRESSION
COMPND 14 VECTOR
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CFP, PFC;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: HEL293F;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: CFP, PFC;
SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 16 EXPRESSION_SYSTEM_VARIANT: HEK293F
KEYWDS INNATE IMMUNITY, COMPLEMENT, PROTEASE, REGULATOR, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR D.V.PEDERSEN,G.R.ANDERSEN
REVDAT 3 29-JUL-20 6RV6 1 CAVEAT COMPND REMARK HETNAM
REVDAT 3 2 1 LINK SITE ATOM
REVDAT 2 25-SEP-19 6RV6 1 JRNL
REVDAT 1 21-AUG-19 6RV6 0
JRNL AUTH D.V.PEDERSEN,T.A.F.GADEBERG,C.THOMAS,Y.WANG,N.JORAM,
JRNL AUTH 2 R.K.JENSEN,S.M.M.MAZARAKIS,M.REVEL,C.EL SISSY,S.V.PETERSEN,
JRNL AUTH 3 K.LINDORFF-LARSEN,S.THIEL,N.S.LAURSEN,V.FREMEAUX-BACCHI,
JRNL AUTH 4 G.R.ANDERSEN
JRNL TITL STRUCTURAL BASIS FOR PROPERDIN OLIGOMERIZATION AND
JRNL TITL 2 CONVERTASE STIMULATION IN THE HUMAN COMPLEMENT SYSTEM.
JRNL REF FRONT IMMUNOL V. 10 2007 2019
JRNL REFN ESSN 1664-3224
JRNL PMID 31507604
JRNL DOI 10.3389/FIMMU.2019.02007
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.MOSS,V.SUBRAMANIAN,K.R.ACHARYA
REMARK 1 TITL CRYSTAL STRUCTURE OF PEPTIDE-BOUND NEPRILYSIN REVEALS KEY
REMARK 1 TITL 2 BINDING INTERACTIONS.
REMARK 1 REF FEBS LETT. 2019
REMARK 1 REFN ISSN 0014-5793
REMARK 1 PMID 31514225
REMARK 1 DOI 10.1002/1873-3468.13602
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.V.PEDERSEN,M.REVEL,T.A.F.GADEBERG,G.R.ANDERSEN
REMARK 1 TITL CRYSTALLIZATION AND X-RAY ANALYSIS OF MONODISPERSE HUMAN
REMARK 1 TITL 2 PROPERDIN.
REMARK 1 REF ACTA CRYSTALLOGR F STRUCT V. 75 0 2019
REMARK 1 REF 2 BIOL COMMUN
REMARK 1 REFN ESSN 2053-230X
REMARK 1 PMID 30713161
REMARK 1 DOI 10.1107/S2053230X18018150
REMARK 2
REMARK 2 RESOLUTION. 3.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.14_3260: ???)
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) : 3.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 77.71
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 27803
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.265
REMARK 3 R VALUE (WORKING SET) : 0.264
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.870
REMARK 3 FREE R VALUE TEST SET COUNT : 1354
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 77.7265 - 7.5534 1.00 2653 123 0.2157 0.2212
REMARK 3 2 7.5534 - 5.9961 1.00 2625 144 0.2727 0.3199
REMARK 3 3 5.9961 - 5.2383 1.00 2612 160 0.2565 0.2481
REMARK 3 4 5.2383 - 4.7594 1.00 2642 120 0.2413 0.3126
REMARK 3 5 4.7594 - 4.4183 1.00 2710 148 0.2536 0.2997
REMARK 3 6 4.4183 - 4.1579 1.00 2628 140 0.2757 0.3249
REMARK 3 7 4.1579 - 3.9496 1.00 2599 116 0.3299 0.2596
REMARK 3 8 3.9496 - 3.7777 1.00 2731 133 0.3246 0.2824
REMARK 3 9 3.7777 - 3.6323 1.00 2544 152 0.3496 0.4500
REMARK 3 10 3.6323 - 3.5070 0.99 2705 118 0.4514 0.4541
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.600
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.390
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 3321
REMARK 3 ANGLE : 1.384 4572
REMARK 3 CHIRALITY : 0.071 498
REMARK 3 PLANARITY : 0.008 559
REMARK 3 DIHEDRAL : 31.650 1460
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 6RV6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1292102658.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUN-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 2.47968
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27811
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.507
REMARK 200 RESOLUTION RANGE LOW (A) : 155.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 20.07
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.51
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.60
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: ELECTRON DENSITY FOR TB-TSR1-TSR5-TSR6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 81.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M LITHIUM SULFATE, 0.1 M SODIUM
REMARK 280 ACETATE PH 4.0, 0.1 M BARIUM CHLORIDE, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y,Z
REMARK 290 7555 -Y+1/2,X,Z+3/4
REMARK 290 8555 Y,-X+1/2,Z+1/4
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 109.89500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 109.89500
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 23.72000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 109.89500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 11.86000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 109.89500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 35.58000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 109.89500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 109.89500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 23.72000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 109.89500
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 35.58000
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 109.89500
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 11.86000
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: 7150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 ASN A 193
REMARK 465 LEU A 194
REMARK 465 TYR A 195
REMARK 465 PHE A 196
REMARK 465 GLN A 197
REMARK 465 GLN B 475
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 CYS A 132 CA - CB - SG ANGL. DEV. = 8.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 39 -30.24 76.75
REMARK 500 ARG A 67 -5.24 55.86
REMARK 500 LEU A 71 74.98 56.34
REMARK 500 SER A 94 -161.14 57.12
REMARK 500 ASN A 108 80.30 61.04
REMARK 500 SER A 153 -143.16 59.79
REMARK 500 ASN A 164 41.85 -148.77
REMARK 500 HIS A 165 73.36 -156.61
REMARK 500 CYS A 170 -98.10 57.44
REMARK 500 PRO A 191 84.93 -58.25
REMARK 500 CYS B 284 54.55 -107.87
REMARK 500 LYS B 333 -154.45 65.30
REMARK 500 CYS B 395 -15.40 94.61
REMARK 500 ASN B 398 75.35 49.89
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6RV6 A 28 191 UNP P27918 PROP_HUMAN 28 191
DBREF 6RV6 B 256 469 UNP P27918 PROP_HUMAN 256 469
SEQADV 6RV6 GLU A 192 UNP P27918 EXPRESSION TAG
SEQADV 6RV6 ASN A 193 UNP P27918 EXPRESSION TAG
SEQADV 6RV6 LEU A 194 UNP P27918 EXPRESSION TAG
SEQADV 6RV6 TYR A 195 UNP P27918 EXPRESSION TAG
SEQADV 6RV6 PHE A 196 UNP P27918 EXPRESSION TAG
SEQADV 6RV6 GLN A 197 UNP P27918 EXPRESSION TAG
SEQADV 6RV6 GLY B 255 UNP P27918 EXPRESSION TAG
SEQADV 6RV6 GLU B 470 UNP P27918 EXPRESSION TAG
SEQADV 6RV6 ASN B 471 UNP P27918 EXPRESSION TAG
SEQADV 6RV6 LEU B 472 UNP P27918 EXPRESSION TAG
SEQADV 6RV6 TYR B 473 UNP P27918 EXPRESSION TAG
SEQADV 6RV6 PHE B 474 UNP P27918 EXPRESSION TAG
SEQADV 6RV6 GLN B 475 UNP P27918 EXPRESSION TAG
SEQRES 1 A 170 ASP PRO VAL LEU CYS PHE THR GLN TYR GLU GLU SER SER
SEQRES 2 A 170 GLY LYS CYS LYS GLY LEU LEU GLY GLY GLY VAL SER VAL
SEQRES 3 A 170 GLU ASP CYS CYS LEU ASN THR ALA PHE ALA TYR GLN LYS
SEQRES 4 A 170 ARG SER GLY GLY LEU CYS GLN PRO CYS ARG SER PRO ARG
SEQRES 5 A 170 TRP SER LEU TRP SER THR TRP ALA PRO CYS SER VAL THR
SEQRES 6 A 170 CYS SER GLU GLY SER GLN LEU ARG TYR ARG ARG CYS VAL
SEQRES 7 A 170 GLY TRP ASN GLY GLN CYS SER GLY LYS VAL ALA PRO GLY
SEQRES 8 A 170 THR LEU GLU TRP GLN LEU GLN ALA CYS GLU ASP GLN GLN
SEQRES 9 A 170 CYS CYS PRO GLU MET GLY GLY TRP SER GLY TRP GLY PRO
SEQRES 10 A 170 TRP GLU PRO CYS SER VAL THR CYS SER LYS GLY THR ARG
SEQRES 11 A 170 THR ARG ARG ARG ALA CYS ASN HIS PRO ALA PRO LYS CYS
SEQRES 12 A 170 GLY GLY HIS CYS PRO GLY GLN ALA GLN GLU SER GLU ALA
SEQRES 13 A 170 CYS ASP THR GLN GLN VAL CYS PRO GLU ASN LEU TYR PHE
SEQRES 14 A 170 GLN
SEQRES 1 B 221 GLY VAL ALA GLY GLY TRP GLY PRO TRP GLY PRO VAL SER
SEQRES 2 B 221 PRO CYS PRO VAL THR CYS GLY LEU GLY GLN THR MET GLU
SEQRES 3 B 221 GLN ARG THR CYS ASN HIS PRO VAL PRO GLN HIS GLY GLY
SEQRES 4 B 221 PRO PHE CYS ALA GLY ASP ALA THR ARG THR HIS ILE CYS
SEQRES 5 B 221 ASN THR ALA VAL PRO CYS PRO VAL ASP GLY GLU TRP ASP
SEQRES 6 B 221 SER TRP GLY GLU TRP SER PRO CYS ILE ARG ARG ASN MET
SEQRES 7 B 221 LYS SER ILE SER CYS GLN GLU ILE PRO GLY GLN GLN SER
SEQRES 8 B 221 ARG GLY ARG THR CYS ARG GLY ARG LYS PHE ASP GLY HIS
SEQRES 9 B 221 ARG CYS ALA GLY GLN GLN GLN ASP ILE ARG HIS CYS TYR
SEQRES 10 B 221 SER ILE GLN HIS CYS PRO LEU LYS GLY SER TRP SER GLU
SEQRES 11 B 221 TRP SER THR TRP GLY LEU CYS MET PRO PRO CYS GLY PRO
SEQRES 12 B 221 ASN PRO THR ARG ALA ARG GLN ARG LEU CYS THR PRO LEU
SEQRES 13 B 221 LEU PRO LYS TYR PRO PRO THR VAL SER MET VAL GLU GLY
SEQRES 14 B 221 GLN GLY GLU LYS ASN VAL THR PHE TRP GLY ARG PRO LEU
SEQRES 15 B 221 PRO ARG CYS GLU GLU LEU GLN GLY GLN LYS LEU VAL VAL
SEQRES 16 B 221 GLU GLU LYS ARG PRO CYS LEU HIS VAL PRO ALA CYS LYS
SEQRES 17 B 221 ASP PRO GLU GLU GLU GLU LEU GLU ASN LEU TYR PHE GLN
HET FUC C 1 10
HET BGC C 2 11
HET FUC D 1 10
HET BGC D 2 11
HET FUC E 1 10
HET BGC E 2 11
HET NAG F 1 14
HET NAG F 2 14
HET FUC F 3 10
HET MAN A 203 11
HET MAN A 204 11
HET MAN A 207 11
HET MAN A 208 11
HET MAN A 209 11
HET MAN B 503 11
HET MAN B 504 11
HET MAN B 505 11
HET MAN B 509 11
HET MAN B 510 11
HET MAN B 511 11
HET MAN B 512 11
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM BGC BETA-D-GLUCOPYRANOSE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
FORMUL 3 FUC 4(C6 H12 O5)
FORMUL 3 BGC 3(C6 H12 O6)
FORMUL 6 NAG 2(C8 H15 N O6)
FORMUL 7 MAN 12(C6 H12 O6)
HELIX 1 AA1 VAL A 53 CYS A 57 1 5
HELIX 2 AA2 ASP B 463 PHE B 474 1 12
SHEET 1 AA1 4 CYS A 43 SER A 52 0
SHEET 2 AA1 4 PRO A 29 TYR A 36 -1 N THR A 34 O GLY A 45
SHEET 3 AA1 4 ALA A 63 GLN A 65 -1 O ALA A 63 N PHE A 33
SHEET 4 AA1 4 GLN A 73 PRO A 74 -1 O GLN A 73 N TYR A 64
SHEET 1 AA2 3 ARG A 79 TRP A 80 0
SHEET 2 AA2 3 GLN A 98 VAL A 105 -1 O VAL A 105 N ARG A 79
SHEET 3 AA2 3 LEU A 120 GLN A 125 -1 O GLN A 125 N GLN A 98
SHEET 1 AA3 2 LYS A 154 ARG A 160 0
SHEET 2 AA3 2 GLN A 179 ASP A 185 -1 O GLU A 182 N ARG A 157
SHEET 1 AA4 2 LEU B 275 GLN B 281 0
SHEET 2 AA4 2 THR B 301 ASN B 307 -1 O HIS B 304 N THR B 278
SHEET 1 AA5 2 GLU B 317 TRP B 318 0
SHEET 2 AA5 2 CYS B 350 ARG B 351 -1 O ARG B 351 N GLU B 317
SHEET 1 AA6 4 GLY B 342 GLY B 347 0
SHEET 2 AA6 4 GLN B 365 SER B 372 -1 O CYS B 370 N GLY B 342
SHEET 3 AA6 4 GLY B 425 TRP B 432 1 O THR B 430 N TYR B 371
SHEET 4 AA6 4 THR B 417 MET B 420 -1 N MET B 420 O GLY B 425
SHEET 1 AA7 4 LEU B 436 ARG B 438 0
SHEET 2 AA7 4 PRO B 377 TRP B 382 1 N LEU B 378 O ARG B 438
SHEET 3 AA7 4 THR B 400 PRO B 409 -1 O THR B 408 N SER B 381
SHEET 4 AA7 4 VAL B 448 PRO B 454 -1 O ARG B 453 N ARG B 401
SSBOND 1 CYS A 32 CYS A 56 1555 1555 2.04
SSBOND 2 CYS A 43 CYS A 72 1555 1555 2.03
SSBOND 3 CYS A 57 CYS A 75 1555 1555 2.03
SSBOND 4 CYS A 89 CYS A 127 1555 1555 2.03
SSBOND 5 CYS A 93 CYS A 133 1555 1555 2.01
SSBOND 6 CYS A 104 CYS A 111 1555 1555 2.03
SSBOND 7 CYS A 132 CYS A 170 1555 1555 2.06
SSBOND 8 CYS A 148 CYS A 184 1555 1555 2.04
SSBOND 9 CYS A 152 CYS A 190 1555 1555 2.03
SSBOND 10 CYS A 163 CYS A 174 1555 1555 2.04
SSBOND 11 CYS B 269 CYS B 306 1555 1555 2.04
SSBOND 12 CYS B 273 CYS B 312 1555 1555 2.02
SSBOND 13 CYS B 284 CYS B 296 1555 1555 2.03
SSBOND 14 CYS B 327 CYS B 370 1555 1555 2.03
SSBOND 15 CYS B 337 CYS B 376 1555 1555 2.02
SSBOND 16 CYS B 350 CYS B 360 1555 1555 2.03
SSBOND 17 CYS B 391 CYS B 455 1555 1555 2.03
SSBOND 18 CYS B 395 CYS B 461 1555 1555 2.02
SSBOND 19 CYS B 407 CYS B 439 1555 1555 2.03
LINK CD1 TRP A 83 C1 MAN A 203 1555 1555 1.52
LINK CD1 TRP A 86 C1 MAN A 204 1555 1555 1.53
LINK OG1 THR A 92 C1 FUC D 1 1555 1555 1.44
LINK CD1 TRP A 139 C1 MAN A 207 1555 1555 1.52
LINK CD1 TRP A 142 C1 MAN A 208 1555 1555 1.52
LINK CD1 TRP A 145 C1 MAN A 209 1555 1555 1.52
LINK OG1 THR A 151 C1 FUC C 1 1555 1555 1.43
LINK CD1 TRP B 260 C1 MAN B 511 1555 1555 1.52
LINK CD1 TRP B 263 C1 MAN B 512 1555 1555 1.52
LINK OG1 THR B 272 C1 FUC E 1 1555 1555 1.44
LINK CD1 TRP B 321 C1 MAN B 503 1555 1555 1.52
LINK CD1 TRP B 324 C1 MAN B 504 1555 1555 1.52
LINK CD1 TRP B 382 C1 MAN B 505 1555 1555 1.53
LINK CD1 TRP B 385 C1 MAN B 510 1555 1555 1.52
LINK CD1 TRP B 388 C1 MAN B 509 1555 1555 1.52
LINK ND2 ASN B 428 C1 NAG F 1 1555 1555 1.44
LINK O3 FUC C 1 C1 BGC C 2 1555 1555 1.44
LINK O3 FUC D 1 C1 BGC D 2 1555 1555 1.46
LINK O3 FUC E 1 C1 BGC E 2 1555 1555 1.44
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.46
LINK O6 NAG F 1 C1 FUC F 3 1555 1555 1.47
CISPEP 1 HIS A 165 PRO A 166 0 -3.00
CISPEP 2 MET B 392 PRO B 393 0 -3.65
CRYST1 219.790 219.790 47.440 90.00 90.00 90.00 I 41 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 0.004550 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004550 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021079 0.00000
(ATOM LINES ARE NOT SHOWN.)
END