HEADER IMMUNE SYSTEM, MEMBRANE PROTEIN 13-OCT-00 1G1S
TITLE P-SELECTIN LECTIN/EGF DOMAINS COMPLEXED WITH PSGL-1 PEPTIDE
CAVEAT 1G1S NGA E 1 HAS WRONG CHIRALITY AT ATOM C1 NGA F 1 HAS WRONG
CAVEAT 2 1G1S CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: P-SELECTIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LECTIN/EGF DOMAINS;
COMPND 5 SYNONYM: GRANULE MEMBRANE PROTEIN 140, GMP-140, PADGEM, CD62P,
COMPND 6 LEUKOCYTE-ENDOTHELIAL CELL ADHESION MOLECULE 3, LECAM3;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PSGL-1 PEPTIDE;
COMPND 10 CHAIN: C, D;
COMPND 11 SYNONYM: PSGL-1;
COMPND 12 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_CELL: CHO CELLS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 17 EXPRESSION_SYSTEM_CELL: CHO CELLS;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS SELECTIN, LECTIN, EGF, SULPHATED, SLEX, IMMUNE SYSTEM, MEMBRANE
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR W.S.SOMERS,R.T.CAMPHAUSEN
REVDAT 6 03-APR-24 1G1S 1 HETSYN
REVDAT 5 29-JUL-20 1G1S 1 CAVEAT COMPND REMARK SEQADV
REVDAT 5 2 1 HETNAM LINK SITE ATOM
REVDAT 4 13-JUL-11 1G1S 1 VERSN
REVDAT 3 24-FEB-09 1G1S 1 VERSN
REVDAT 2 01-APR-03 1G1S 1 JRNL
REVDAT 1 13-OCT-01 1G1S 0
JRNL AUTH W.S.SOMERS,J.TANG,G.D.SHAW,R.T.CAMPHAUSEN
JRNL TITL INSIGHTS INTO THE MOLECULAR BASIS OF LEUKOCYTE TETHERING AND
JRNL TITL 2 ROLLING REVEALED BY STRUCTURES OF P- AND E-SELECTIN BOUND TO
JRNL TITL 3 SLE(X) AND PSGL-1.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 103 467 2000
JRNL REFN ISSN 0092-8674
JRNL PMID 11081633
JRNL DOI 10.1016/S0092-8674(00)00138-0
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 44923
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2246
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2814
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 220
REMARK 3 SOLVENT ATOMS : 224
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.00
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.540
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1G1S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000012126.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99987
REMARK 200 MONOCHROMATOR : SYNCHROTRON
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44923
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 4.630
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.63
REMARK 200 R MERGE FOR SHELL (I) : 0.27400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: P-SELECTIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, 10 MM TRIS, 150 MN NACL,
REMARK 280 4 MM CACL2, 50 MM SRCL2, 5% PEG 6000, 33% MPD, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP AT 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 31.72250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.37800
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 93.64450
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 31.72250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.37800
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 93.64450
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 31.72250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 48.37800
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 93.64450
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 31.72250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 48.37800
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 93.64450
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 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 ASP A 159
REMARK 465 ASP A 160
REMARK 465 ASP A 161
REMARK 465 LYS A 162
REMARK 465 ASP B 158
REMARK 465 ASP B 159
REMARK 465 ASP B 160
REMARK 465 ASP B 161
REMARK 465 LYS B 162
REMARK 465 GLN C 601
REMARK 465 ALA C 602
REMARK 465 THR C 603
REMARK 465 GLU C 604
REMARK 465 TYS C 605
REMARK 465 PRO C 619
REMARK 465 ARG C 620
REMARK 465 PRO C 621
REMARK 465 MET C 622
REMARK 465 MET C 623
REMARK 465 ASP C 624
REMARK 465 ASP C 625
REMARK 465 ASP C 626
REMARK 465 ASP C 627
REMARK 465 LYS C 628
REMARK 465 GLN D 601
REMARK 465 ALA D 602
REMARK 465 THR D 603
REMARK 465 GLU D 604
REMARK 465 PRO D 619
REMARK 465 ARG D 620
REMARK 465 PRO D 621
REMARK 465 MET D 622
REMARK 465 MET D 623
REMARK 465 ASP D 624
REMARK 465 ASP D 625
REMARK 465 ASP D 626
REMARK 465 ASP D 627
REMARK 465 LYS D 628
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 LYS A 32 CG CD CE NZ
REMARK 470 ASN A 57 CG OD1 ND2
REMARK 470 LYS A 58 CG CD CE NZ
REMARK 470 ASN A 71 CG OD1 ND2
REMARK 470 ASP A 158 CG OD1 OD2
REMARK 470 ARG B 22 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 57 CG OD1 ND2
REMARK 470 LYS B 58 CG CD CE NZ
REMARK 470 GLU B 72 CG CD OE1 OE2
REMARK 470 MET B 125 CG SD CE
REMARK 470 ARG B 157 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 606 CG CD OE1 OE2
REMARK 470 TYS D 605 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYS D 605 S O1 O2 O3
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 950 O HOH B 950 4576 1.88
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 TYR A 23 -137.03 -129.66
REMARK 500 ALA A 28 75.29 -112.92
REMARK 500 ILE A 29 91.88 -41.86
REMARK 500 TYR A 48 -158.45 61.79
REMARK 500 ASN A 57 -92.65 67.21
REMARK 500 ASN A 83 47.43 36.22
REMARK 500 ASN A 86 150.48 80.77
REMARK 500 ALA A 100 56.85 -145.95
REMARK 500 ASN A 139 -139.20 -163.07
REMARK 500 TYR B 23 -137.34 -128.54
REMARK 500 TYR B 48 -160.90 62.87
REMARK 500 ASN B 57 -111.45 72.64
REMARK 500 GLU B 74 132.04 -27.69
REMARK 500 ASN B 75 38.39 -144.65
REMARK 500 ASN B 83 45.82 33.69
REMARK 500 ASN B 86 148.71 77.14
REMARK 500 ALA B 100 59.94 -145.15
REMARK 500 SER B 128 25.35 49.26
REMARK 500 ASN B 139 -150.60 -161.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SR A 901 SR
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 80 OE1
REMARK 620 2 ASN A 82 OD1 71.6
REMARK 620 3 GLU A 88 OE1 135.8 73.1
REMARK 620 4 ASN A 105 OD1 66.9 136.8 149.0
REMARK 620 5 ASP A 106 O 132.1 144.6 72.6 76.5
REMARK 620 6 ASP A 106 OD1 74.1 97.0 84.7 83.3 71.8
REMARK 620 7 FUC F 5 O3 130.6 115.6 88.7 84.1 71.7 143.2
REMARK 620 8 FUC F 5 O4 74.6 76.6 121.3 81.1 129.8 148.5 61.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SR B 902 SR
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 80 OE1
REMARK 620 2 ASN B 82 OD1 73.1
REMARK 620 3 GLU B 88 OE1 138.6 72.5
REMARK 620 4 ASN B 105 OD1 67.1 138.3 148.8
REMARK 620 5 ASP B 106 O 131.5 141.9 71.4 77.6
REMARK 620 6 ASP B 106 OD1 74.8 92.2 84.1 89.2 72.4
REMARK 620 7 FUC E 5 O3 131.5 117.3 85.3 82.3 71.3 143.7
REMARK 620 8 FUC E 5 O4 75.9 80.6 119.7 78.2 128.8 150.7 61.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 903 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 954 O
REMARK 620 2 HOH D 201 O 86.2
REMARK 620 3 HOH D 202 O 86.7 169.3
REMARK 620 4 HOH D 203 O 75.9 86.2 84.4
REMARK 620 5 ASP D 609 OD1 155.4 72.4 116.1 113.5
REMARK 620 6 ASP D 609 OD2 149.2 104.7 77.8 76.2 52.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 904 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 55 O
REMARK 620 2 HOH C 185 O 86.1
REMARK 620 3 HOH C 199 O 171.5 87.1
REMARK 620 4 HOH C 200 O 89.2 81.9 84.9
REMARK 620 5 ASP C 609 OD1 115.6 148.8 72.7 118.5
REMARK 620 6 ASP C 609 OD2 75.6 157.2 109.8 84.4 53.9
REMARK 620 7 ASP C 611 OD2 94.7 65.9 87.1 147.2 89.0 128.1
REMARK 620 N 1 2 3 4 5 6
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G1Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF P-SELECTIN LECTIN/EGF DOMAINS
REMARK 900 RELATED ID: 1G1R RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF P-SELECTIN LECTIN/EGF DOMAINS COMPLEXED WITH
REMARK 900 SLEX
REMARK 900 RELATED ID: 1G1T RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E-SELECTIN
DBREF 1G1S A 1 158 UNP P16109 LEM3_HUMAN 42 199
DBREF 1G1S B 1 158 UNP P16109 LEM3_HUMAN 42 199
DBREF 1G1S C 601 619 UNP Q14242 SEPL_HUMAN 42 60
DBREF 1G1S D 601 619 UNP Q14242 SEPL_HUMAN 42 60
SEQADV 1G1S ASP A 158 UNP P16109 GLU 199 CONFLICT
SEQADV 1G1S ASP A 159 UNP P16109 CLONING ARTIFACT
SEQADV 1G1S ASP A 160 UNP P16109 CLONING ARTIFACT
SEQADV 1G1S ASP A 161 UNP P16109 CLONING ARTIFACT
SEQADV 1G1S LYS A 162 UNP P16109 CLONING ARTIFACT
SEQADV 1G1S ASP B 158 UNP P16109 GLU 199 CONFLICT
SEQADV 1G1S ASP B 159 UNP P16109 CLONING ARTIFACT
SEQADV 1G1S ASP B 160 UNP P16109 CLONING ARTIFACT
SEQADV 1G1S ASP B 161 UNP P16109 CLONING ARTIFACT
SEQADV 1G1S LYS B 162 UNP P16109 CLONING ARTIFACT
SEQADV 1G1S TYS C 605 UNP Q14242 TYR 46 MODIFIED RESIDUE
SEQADV 1G1S TYS C 607 UNP Q14242 TYR 48 MODIFIED RESIDUE
SEQADV 1G1S TYS C 610 UNP Q14242 TYR 51 MODIFIED RESIDUE
SEQADV 1G1S ARG C 620 UNP Q14242 CLONING ARTIFACT
SEQADV 1G1S PRO C 621 UNP Q14242 CLONING ARTIFACT
SEQADV 1G1S MET C 622 UNP Q14242 CLONING ARTIFACT
SEQADV 1G1S MET C 623 UNP Q14242 CLONING ARTIFACT
SEQADV 1G1S ASP C 624 UNP Q14242 CLONING ARTIFACT
SEQADV 1G1S ASP C 625 UNP Q14242 CLONING ARTIFACT
SEQADV 1G1S ASP C 626 UNP Q14242 CLONING ARTIFACT
SEQADV 1G1S ASP C 627 UNP Q14242 CLONING ARTIFACT
SEQADV 1G1S LYS C 628 UNP Q14242 CLONING ARTIFACT
SEQADV 1G1S TYS D 605 UNP Q14242 TYR 46 MODIFIED RESIDUE
SEQADV 1G1S TYS D 607 UNP Q14242 TYR 48 MODIFIED RESIDUE
SEQADV 1G1S TYS D 610 UNP Q14242 TYR 51 MODIFIED RESIDUE
SEQADV 1G1S ARG D 620 UNP Q14242 CLONING ARTIFACT
SEQADV 1G1S PRO D 621 UNP Q14242 CLONING ARTIFACT
SEQADV 1G1S MET D 622 UNP Q14242 CLONING ARTIFACT
SEQADV 1G1S MET D 623 UNP Q14242 CLONING ARTIFACT
SEQADV 1G1S ASP D 624 UNP Q14242 CLONING ARTIFACT
SEQADV 1G1S ASP D 625 UNP Q14242 CLONING ARTIFACT
SEQADV 1G1S ASP D 626 UNP Q14242 CLONING ARTIFACT
SEQADV 1G1S ASP D 627 UNP Q14242 CLONING ARTIFACT
SEQADV 1G1S LYS D 628 UNP Q14242 CLONING ARTIFACT
SEQRES 1 A 162 TRP THR TYR HIS TYR SER THR LYS ALA TYR SER TRP ASN
SEQRES 2 A 162 ILE SER ARG LYS TYR CYS GLN ASN ARG TYR THR ASP LEU
SEQRES 3 A 162 VAL ALA ILE GLN ASN LYS ASN GLU ILE ASP TYR LEU ASN
SEQRES 4 A 162 LYS VAL LEU PRO TYR TYR SER SER TYR TYR TRP ILE GLY
SEQRES 5 A 162 ILE ARG LYS ASN ASN LYS THR TRP THR TRP VAL GLY THR
SEQRES 6 A 162 LYS LYS ALA LEU THR ASN GLU ALA GLU ASN TRP ALA ASP
SEQRES 7 A 162 ASN GLU PRO ASN ASN LYS ARG ASN ASN GLU ASP CYS VAL
SEQRES 8 A 162 GLU ILE TYR ILE LYS SER PRO SER ALA PRO GLY LYS TRP
SEQRES 9 A 162 ASN ASP GLU HIS CYS LEU LYS LYS LYS HIS ALA LEU CYS
SEQRES 10 A 162 TYR THR ALA SER CYS GLN ASP MET SER CYS SER LYS GLN
SEQRES 11 A 162 GLY GLU CYS LEU GLU THR ILE GLY ASN TYR THR CYS SER
SEQRES 12 A 162 CYS TYR PRO GLY PHE TYR GLY PRO GLU CYS GLU TYR VAL
SEQRES 13 A 162 ARG ASP ASP ASP ASP LYS
SEQRES 1 B 162 TRP THR TYR HIS TYR SER THR LYS ALA TYR SER TRP ASN
SEQRES 2 B 162 ILE SER ARG LYS TYR CYS GLN ASN ARG TYR THR ASP LEU
SEQRES 3 B 162 VAL ALA ILE GLN ASN LYS ASN GLU ILE ASP TYR LEU ASN
SEQRES 4 B 162 LYS VAL LEU PRO TYR TYR SER SER TYR TYR TRP ILE GLY
SEQRES 5 B 162 ILE ARG LYS ASN ASN LYS THR TRP THR TRP VAL GLY THR
SEQRES 6 B 162 LYS LYS ALA LEU THR ASN GLU ALA GLU ASN TRP ALA ASP
SEQRES 7 B 162 ASN GLU PRO ASN ASN LYS ARG ASN ASN GLU ASP CYS VAL
SEQRES 8 B 162 GLU ILE TYR ILE LYS SER PRO SER ALA PRO GLY LYS TRP
SEQRES 9 B 162 ASN ASP GLU HIS CYS LEU LYS LYS LYS HIS ALA LEU CYS
SEQRES 10 B 162 TYR THR ALA SER CYS GLN ASP MET SER CYS SER LYS GLN
SEQRES 11 B 162 GLY GLU CYS LEU GLU THR ILE GLY ASN TYR THR CYS SER
SEQRES 12 B 162 CYS TYR PRO GLY PHE TYR GLY PRO GLU CYS GLU TYR VAL
SEQRES 13 B 162 ARG ASP ASP ASP ASP LYS
SEQRES 1 C 28 GLN ALA THR GLU TYS GLU TYS LEU ASP TYS ASP PHE LEU
SEQRES 2 C 28 PRO GLU THR GLU PRO PRO ARG PRO MET MET ASP ASP ASP
SEQRES 3 C 28 ASP LYS
SEQRES 1 D 28 GLN ALA THR GLU TYS GLU TYS LEU ASP TYS ASP PHE LEU
SEQRES 2 D 28 PRO GLU THR GLU PRO PRO ARG PRO MET MET ASP ASP ASP
SEQRES 3 D 28 ASP LYS
MODRES 1G1S THR D 616 THR GLYCOSYLATION SITE
MODRES 1G1S THR C 616 THR GLYCOSYLATION SITE
MODRES 1G1S TYS C 607 TYR O-SULFO-L-TYROSINE
MODRES 1G1S TYS C 610 TYR O-SULFO-L-TYROSINE
MODRES 1G1S TYS D 605 TYR O-SULFO-L-TYROSINE
MODRES 1G1S TYS D 607 TYR O-SULFO-L-TYROSINE
MODRES 1G1S TYS D 610 TYR O-SULFO-L-TYROSINE
HET TYS C 607 16
HET TYS C 610 16
HET TYS D 605 5
HET TYS D 607 16
HET TYS D 610 16
HET NGA E 1 14
HET NAG E 2 14
HET GAL E 3 11
HET SIA E 4 20
HET FUC E 5 10
HET GAL E 6 11
HET NGA F 1 14
HET NAG F 2 14
HET GAL F 3 11
HET SIA F 4 20
HET FUC F 5 10
HET GAL F 6 11
HET SR A 901 1
HET MRD A 807 8
HET MRD A 811 8
HET SR B 902 1
HET NA B 903 1
HET MRD B 805 8
HET MRD B 806 8
HET MRD B 808 8
HET MRD B 809 8
HET MRD B 810 8
HET NA C 904 1
HETNAM TYS O-SULFO-L-TYROSINE
HETNAM NGA 2-ACETAMIDO-2-DEOXY-BETA-D-GALACTOPYRANOSE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETNAM SIA N-ACETYL-ALPHA-NEURAMINIC ACID
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM SR STRONTIUM ION
HETNAM MRD (4R)-2-METHYLPENTANE-2,4-DIOL
HETNAM NA SODIUM ION
HETSYN NGA N-ACETYL-BETA-D-GALACTOSAMINE; 2-ACETAMIDO-2-DEOXY-
HETSYN 2 NGA BETA-D-GALACTOSE; 2-ACETAMIDO-2-DEOXY-D-GALACTOSE; 2-
HETSYN 3 NGA ACETAMIDO-2-DEOXY-GALACTOSE; N-ACETYL-D-GALACTOSAMINE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE
HETSYN SIA N-ACETYLNEURAMINIC ACID; SIALIC ACID; ALPHA-SIALIC
HETSYN 2 SIA ACID; O-SIALIC ACID
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
FORMUL 3 TYS 5(C9 H11 N O6 S)
FORMUL 5 NGA 2(C8 H15 N O6)
FORMUL 5 NAG 2(C8 H15 N O6)
FORMUL 5 GAL 4(C6 H12 O6)
FORMUL 5 SIA 2(C11 H19 N O9)
FORMUL 5 FUC 2(C6 H12 O5)
FORMUL 7 SR 2(SR 2+)
FORMUL 8 MRD 7(C6 H14 O2)
FORMUL 11 NA 2(NA 1+)
FORMUL 18 HOH *224(H2 O)
HELIX 1 1 SER A 11 TYR A 23 1 13
HELIX 2 2 ASN A 31 LEU A 42 1 12
HELIX 3 3 MET A 125 LYS A 129 5 5
HELIX 4 4 SER B 11 TYR B 23 1 13
HELIX 5 5 ASN B 31 LEU B 42 1 12
SHEET 1 A 2 GLY A 131 GLU A 135 0
SHEET 2 A 2 TYR A 140 CYS A 144 -1 O THR A 141 N LEU A 134
SHEET 1 B 2 PHE A 148 TYR A 149 0
SHEET 2 B 2 TYR A 155 VAL A 156 -1 N TYR A 155 O TYR A 149
SHEET 1 C 2 GLY B 131 THR B 136 0
SHEET 2 C 2 ASN B 139 CYS B 144 -1 O ASN B 139 N THR B 136
SHEET 1 D 2 PHE B 148 TYR B 149 0
SHEET 2 D 2 TYR B 155 VAL B 156 -1 N TYR B 155 O TYR B 149
SSBOND 1 CYS A 19 CYS A 117 1555 1555 2.06
SSBOND 2 CYS A 90 CYS A 109 1555 1555 2.04
SSBOND 3 CYS A 122 CYS A 133 1555 1555 2.06
SSBOND 4 CYS A 127 CYS A 142 1555 1555 2.06
SSBOND 5 CYS A 144 CYS A 153 1555 1555 2.09
SSBOND 6 CYS B 19 CYS B 117 1555 1555 2.07
SSBOND 7 CYS B 90 CYS B 109 1555 1555 2.05
SSBOND 8 CYS B 122 CYS B 133 1555 1555 2.05
SSBOND 9 CYS B 127 CYS B 142 1555 1555 2.05
SSBOND 10 CYS B 144 CYS B 153 1555 1555 2.08
LINK C GLU C 606 N TYS C 607 1555 1555 1.33
LINK C TYS C 607 N LEU C 608 1555 1555 1.33
LINK C ASP C 609 N TYS C 610 1555 1555 1.33
LINK C TYS C 610 N ASP C 611 1555 1555 1.32
LINK OG1 THR C 616 C1 NGA E 1 1555 1555 1.43
LINK C TYS D 605 N GLU D 606 1555 1555 1.33
LINK C GLU D 606 N TYS D 607 1555 1555 1.32
LINK C TYS D 607 N LEU D 608 1555 1555 1.33
LINK C ASP D 609 N TYS D 610 1555 1555 1.33
LINK C TYS D 610 N ASP D 611 1555 1555 1.33
LINK OG1 THR D 616 C1 NGA F 1 1555 1555 1.43
LINK O6 NGA E 1 C1 NAG E 2 1555 1555 1.40
LINK O3 NGA E 1 C1 GAL E 6 1555 1555 1.41
LINK O4 NAG E 2 C1 GAL E 3 1555 1555 1.39
LINK O3 NAG E 2 C1 FUC E 5 1555 1555 1.42
LINK O3 GAL E 3 C2 SIA E 4 1555 1555 1.44
LINK O6 NGA F 1 C1 NAG F 2 1555 1555 1.38
LINK O3 NGA F 1 C1 GAL F 6 1555 1555 1.40
LINK O4 NAG F 2 C1 GAL F 3 1555 1555 1.39
LINK O3 NAG F 2 C1 FUC F 5 1555 1555 1.40
LINK O3 GAL F 3 C2 SIA F 4 1555 1555 1.45
LINK OE1 GLU A 80 SR SR A 901 1555 1555 2.85
LINK OD1 ASN A 82 SR SR A 901 1555 1555 2.58
LINK OE1 GLU A 88 SR SR A 901 1555 1555 2.60
LINK OD1 ASN A 105 SR SR A 901 1555 1555 2.54
LINK O ASP A 106 SR SR A 901 1555 1555 2.54
LINK OD1 ASP A 106 SR SR A 901 1555 1555 2.33
LINK SR SR A 901 O3 FUC F 5 1555 1555 2.51
LINK SR SR A 901 O4 FUC F 5 1555 1555 2.76
LINK OE1 GLU B 80 SR SR B 902 1555 1555 2.65
LINK OD1 ASN B 82 SR SR B 902 1555 1555 2.60
LINK OE1 GLU B 88 SR SR B 902 1555 1555 2.58
LINK OD1 ASN B 105 SR SR B 902 1555 1555 2.54
LINK O ASP B 106 SR SR B 902 1555 1555 2.55
LINK OD1 ASP B 106 SR SR B 902 1555 1555 2.22
LINK SR SR B 902 O3 FUC E 5 1555 1555 2.56
LINK SR SR B 902 O4 FUC E 5 1555 1555 2.73
LINK NA NA B 903 O HOH B 954 1555 1555 2.36
LINK NA NA B 903 O HOH D 201 1555 7645 2.28
LINK NA NA B 903 O HOH D 202 1555 7645 2.19
LINK NA NA B 903 O HOH D 203 1555 7645 2.49
LINK NA NA B 903 OD1 ASP D 609 1555 7645 2.54
LINK NA NA B 903 OD2 ASP D 609 1555 7645 2.48
LINK O HOH C 55 NA NA C 904 1555 1555 2.22
LINK O HOH C 185 NA NA C 904 1555 1555 2.41
LINK O HOH C 199 NA NA C 904 1555 1555 2.18
LINK O HOH C 200 NA NA C 904 1555 1555 2.48
LINK OD1 ASP C 609 NA NA C 904 1555 1555 2.46
LINK OD2 ASP C 609 NA NA C 904 1555 1555 2.39
LINK OD2 ASP C 611 NA NA C 904 1555 1555 2.71
CISPEP 1 GLU A 80 PRO A 81 0 0.05
CISPEP 2 GLU B 80 PRO B 81 0 -0.49
CRYST1 63.445 96.756 187.289 90.00 90.00 90.00 I 2 2 2 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015762 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010335 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005339 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
