HEADER BLOOD CLOTTING 18-JUL-01 1JMJ
TITLE CRYSTAL STRUCTURE OF NATIVE HEPARIN COFACTOR II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPARIN COFACTOR II;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HC-II; PROTEASE INHIBITOR LEUSERPIN 2; HLS2; SERINE (OR
COMPND 5 CYSTEINE) PROTEINASE INHIBITOR, CLADE D (HEPARIN COFACTOR), MEMBER 1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS SERPIN, THROMBIN INHIBITOR, HEPARIN, BLOOD CLOTTING
EXPDTA X-RAY DIFFRACTION
AUTHOR T.P.BAGLIN,R.W.CARRELL,F.C.CHURCH,J.A.HUNTINGTON
REVDAT 5 03-APR-24 1JMJ 1 REMARK HETSYN
REVDAT 4 29-JUL-20 1JMJ 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 13-JUL-11 1JMJ 1 VERSN
REVDAT 2 24-FEB-09 1JMJ 1 VERSN
REVDAT 1 30-AUG-02 1JMJ 0
JRNL AUTH T.P.BAGLIN,R.W.CARRELL,F.C.CHURCH,C.T.ESMON,J.A.HUNTINGTON
JRNL TITL CRYSTAL STRUCTURES OF NATIVE AND THROMBIN-COMPLEXED HEPARIN
JRNL TITL 2 COFACTOR II REVEAL A MULTISTEP ALLOSTERIC MECHANISM.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 99 11079 2002
JRNL REFN ISSN 0027-8424
JRNL PMID 12169660
JRNL DOI 10.1073/PNAS.162232399
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
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) (%) : 88.0
REMARK 3 NUMBER OF REFLECTIONS : 39156
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) : 0.208
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.500
REMARK 3 FREE R VALUE TEST SET COUNT : 994
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) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.50
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3150
REMARK 3 BIN FREE R VALUE : 0.3870
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 142
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.032
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6372
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 297
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.39
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 13.95000
REMARK 3 B22 (A**2) : -9.52000
REMARK 3 B33 (A**2) : -4.43000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 12.10000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.38
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.42
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.297 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.182 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.229 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.429 ; 2.500
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 1JMJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-01.
REMARK 100 THE DEPOSITION ID IS D_1000013938.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-NOV-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.4880
REMARK 200 MONOCHROMATOR : LIQUID GALLIUM
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40150
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 66.0
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : 0.14000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.60
REMARK 200 R MERGE FOR SHELL (I) : 0.45000
REMARK 200 R SYM FOR SHELL (I) : 0.35000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
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: SEVERAL SERPINS WERE TRIED BEST SOLUTION WITH
REMARK 200 NATIVE ANTITHROMBIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MGCL2, TRIS, PEG 4000, GLYCEROL, PH
REMARK 280 8.5, VAPOR DIFFUSION, HANGING DROP AT 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 40.00000
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 GLY A 1
REMARK 465 SER A 2
REMARK 465 LYS A 3
REMARK 465 GLY A 4
REMARK 465 PRO A 5
REMARK 465 LEU A 6
REMARK 465 ASP A 7
REMARK 465 GLN A 8
REMARK 465 LEU A 9
REMARK 465 GLU A 10
REMARK 465 LYS A 11
REMARK 465 GLY A 12
REMARK 465 GLY A 13
REMARK 465 GLU A 14
REMARK 465 THR A 15
REMARK 465 ALA A 16
REMARK 465 GLN A 17
REMARK 465 SER A 18
REMARK 465 ALA A 19
REMARK 465 ASP A 20
REMARK 465 PRO A 21
REMARK 465 GLN A 22
REMARK 465 TRP A 23
REMARK 465 GLU A 24
REMARK 465 GLN A 25
REMARK 465 LEU A 26
REMARK 465 ASN A 27
REMARK 465 ASN A 28
REMARK 465 LYS A 29
REMARK 465 ASN A 30
REMARK 465 LEU A 31
REMARK 465 SER A 32
REMARK 465 MET A 33
REMARK 465 PRO A 34
REMARK 465 LEU A 35
REMARK 465 LEU A 36
REMARK 465 PRO A 37
REMARK 465 ALA A 38
REMARK 465 ASP A 39
REMARK 465 PHE A 40
REMARK 465 HIS A 41
REMARK 465 LYS A 42
REMARK 465 GLU A 43
REMARK 465 ASN A 44
REMARK 465 THR A 45
REMARK 465 VAL A 46
REMARK 465 THR A 47
REMARK 465 ASN A 48
REMARK 465 ASP A 49
REMARK 465 TRP A 50
REMARK 465 ILE A 51
REMARK 465 PRO A 52
REMARK 465 GLU A 53
REMARK 465 GLY A 54
REMARK 465 GLU A 55
REMARK 465 GLU A 56
REMARK 465 ASP A 57
REMARK 465 ASP A 58
REMARK 465 ASP A 59
REMARK 465 TYR A 60
REMARK 465 ASP A 72
REMARK 465 TYR A 73
REMARK 465 ILE A 74
REMARK 465 ASP A 75
REMARK 465 ILE A 76
REMARK 465 VAL A 77
REMARK 465 ASP A 78
REMARK 465 SER A 79
REMARK 465 LEU A 80
REMARK 465 SER A 81
REMARK 465 VAL A 82
REMARK 465 SER A 83
REMARK 465 PRO A 84
REMARK 465 THR A 85
REMARK 465 ASP A 86
REMARK 465 SER A 87
REMARK 465 ASP A 88
REMARK 465 VAL A 89
REMARK 465 SER A 90
REMARK 465 ALA A 91
REMARK 465 GLY A 92
REMARK 465 ASN A 93
REMARK 465 ILE A 94
REMARK 465 GLY B 1
REMARK 465 SER B 2
REMARK 465 LYS B 3
REMARK 465 GLY B 4
REMARK 465 PRO B 5
REMARK 465 LEU B 6
REMARK 465 ASP B 7
REMARK 465 GLN B 8
REMARK 465 LEU B 9
REMARK 465 GLU B 10
REMARK 465 LYS B 11
REMARK 465 GLY B 12
REMARK 465 GLY B 13
REMARK 465 GLU B 14
REMARK 465 THR B 15
REMARK 465 ALA B 16
REMARK 465 GLN B 17
REMARK 465 SER B 18
REMARK 465 ALA B 19
REMARK 465 ASP B 20
REMARK 465 PRO B 21
REMARK 465 GLN B 22
REMARK 465 TRP B 23
REMARK 465 GLU B 24
REMARK 465 GLN B 25
REMARK 465 LEU B 26
REMARK 465 ASN B 27
REMARK 465 ASN B 28
REMARK 465 LYS B 29
REMARK 465 ASN B 30
REMARK 465 LEU B 31
REMARK 465 SER B 32
REMARK 465 MET B 33
REMARK 465 PRO B 34
REMARK 465 LEU B 35
REMARK 465 LEU B 36
REMARK 465 PRO B 37
REMARK 465 ALA B 38
REMARK 465 ASP B 39
REMARK 465 PHE B 40
REMARK 465 HIS B 41
REMARK 465 LYS B 42
REMARK 465 GLU B 43
REMARK 465 ASN B 44
REMARK 465 THR B 45
REMARK 465 VAL B 46
REMARK 465 THR B 47
REMARK 465 ASN B 48
REMARK 465 ASP B 49
REMARK 465 TRP B 50
REMARK 465 ILE B 51
REMARK 465 PRO B 52
REMARK 465 GLU B 53
REMARK 465 GLY B 54
REMARK 465 GLU B 55
REMARK 465 GLU B 56
REMARK 465 ASP B 57
REMARK 465 ASP B 58
REMARK 465 ASP B 59
REMARK 465 TYR B 60
REMARK 465 LEU B 61
REMARK 465 ASP B 62
REMARK 465 LEU B 63
REMARK 465 GLU B 64
REMARK 465 LYS B 65
REMARK 465 ILE B 66
REMARK 465 PHE B 67
REMARK 465 SER B 68
REMARK 465 GLU B 69
REMARK 465 ASP B 70
REMARK 465 ASP B 71
REMARK 465 ASP B 72
REMARK 465 TYR B 73
REMARK 465 ILE B 74
REMARK 465 ASP B 75
REMARK 465 ILE B 76
REMARK 465 VAL B 77
REMARK 465 ASP B 78
REMARK 465 SER B 79
REMARK 465 LEU B 80
REMARK 465 SER B 81
REMARK 465 VAL B 82
REMARK 465 SER B 83
REMARK 465 PRO B 84
REMARK 465 THR B 85
REMARK 465 ASP B 86
REMARK 465 SER B 87
REMARK 465 ASP B 88
REMARK 465 VAL B 89
REMARK 465 SER B 90
REMARK 465 ALA B 91
REMARK 465 GLY B 92
REMARK 465 ASN B 93
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 173 CD CE NZ
REMARK 480 GLU A 175 CD OE1 OE2
REMARK 480 ARG A 189 NE CZ NH1 NH2
REMARK 480 ASP A 216 OD2
REMARK 480 GLU A 300 OE1
REMARK 480 GLN A 411 OE1 NE2
REMARK 480 ARG A 412 CG CD NE CZ NH1 NH2
REMARK 480 LYS B 165 CD CE NZ
REMARK 480 ARG B 193 CD NE CZ NH1 NH2
REMARK 480 ARG B 222 CD NE CZ NH1 NH2
REMARK 480 LYS B 364 CE
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 GLN A 96 -63.27 108.80
REMARK 500 ASP A 166 -35.08 -37.61
REMARK 500 GLU A 175 170.52 176.83
REMARK 500 PHE A 226 15.38 57.51
REMARK 500 ASP A 233 85.01 -150.61
REMARK 500 GLU A 300 127.43 174.82
REMARK 500 ASP A 322 70.98 44.51
REMARK 500 PHE A 441 -2.01 -158.28
REMARK 500 PRO A 477 -7.18 -58.99
REMARK 500 LEU B 95 62.39 -113.18
REMARK 500 ASP B 233 86.57 -156.91
REMARK 500 PHE B 234 5.73 -69.68
REMARK 500 PHE B 441 -10.10 -154.40
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 CA A 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 290 NE2
REMARK 620 2 HIS A 292 ND1 94.2
REMARK 620 3 HOH A 502 O 88.3 164.2
REMARK 620 4 HOH A 551 O 139.2 97.8 70.6
REMARK 620 5 HOH A 631 O 94.1 99.4 96.0 121.8
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JMO RELATED DB: PDB
DBREF 1JMJ A 1 480 UNP P05546 HEP2_HUMAN 20 499
DBREF 1JMJ B 1 480 UNP P05546 HEP2_HUMAN 20 499
SEQRES 1 A 480 GLY SER LYS GLY PRO LEU ASP GLN LEU GLU LYS GLY GLY
SEQRES 2 A 480 GLU THR ALA GLN SER ALA ASP PRO GLN TRP GLU GLN LEU
SEQRES 3 A 480 ASN ASN LYS ASN LEU SER MET PRO LEU LEU PRO ALA ASP
SEQRES 4 A 480 PHE HIS LYS GLU ASN THR VAL THR ASN ASP TRP ILE PRO
SEQRES 5 A 480 GLU GLY GLU GLU ASP ASP ASP TYR LEU ASP LEU GLU LYS
SEQRES 6 A 480 ILE PHE SER GLU ASP ASP ASP TYR ILE ASP ILE VAL ASP
SEQRES 7 A 480 SER LEU SER VAL SER PRO THR ASP SER ASP VAL SER ALA
SEQRES 8 A 480 GLY ASN ILE LEU GLN LEU PHE HIS GLY LYS SER ARG ILE
SEQRES 9 A 480 GLN ARG LEU ASN ILE LEU ASN ALA LYS PHE ALA PHE ASN
SEQRES 10 A 480 LEU TYR ARG VAL LEU LYS ASP GLN VAL ASN THR PHE ASP
SEQRES 11 A 480 ASN ILE PHE ILE ALA PRO VAL GLY ILE SER THR ALA MET
SEQRES 12 A 480 GLY MET ILE SER LEU GLY LEU LYS GLY GLU THR HIS GLU
SEQRES 13 A 480 GLN VAL HIS SER ILE LEU HIS PHE LYS ASP PHE VAL ASN
SEQRES 14 A 480 ALA SER SER LYS TYR GLU ILE THR THR ILE HIS ASN LEU
SEQRES 15 A 480 PHE ARG LYS LEU THR HIS ARG LEU PHE ARG ARG ASN PHE
SEQRES 16 A 480 GLY TYR THR LEU ARG SER VAL ASN ASP LEU TYR ILE GLN
SEQRES 17 A 480 LYS GLN PHE PRO ILE LEU LEU ASP PHE LYS THR LYS VAL
SEQRES 18 A 480 ARG GLU TYR TYR PHE ALA GLU ALA GLN ILE ALA ASP PHE
SEQRES 19 A 480 SER ASP PRO ALA PHE ILE SER LYS THR ASN ASN HIS ILE
SEQRES 20 A 480 MET LYS LEU THR LYS GLY LEU ILE LYS ASP ALA LEU GLU
SEQRES 21 A 480 ASN ILE ASP PRO ALA THR GLN MET MET ILE LEU ASN CYS
SEQRES 22 A 480 ILE TYR PHE LYS GLY SER TRP VAL ASN LYS PHE PRO VAL
SEQRES 23 A 480 GLU MET THR HIS ASN HIS ASN PHE ARG LEU ASN GLU ARG
SEQRES 24 A 480 GLU VAL VAL LYS VAL SER MET MET GLN THR LYS GLY ASN
SEQRES 25 A 480 PHE LEU ALA ALA ASN ASP GLN GLU LEU ASP CYS ASP ILE
SEQRES 26 A 480 LEU GLN LEU GLU TYR VAL GLY GLY ILE SER MET LEU ILE
SEQRES 27 A 480 VAL VAL PRO HIS LYS MET SER GLY MET LYS THR LEU GLU
SEQRES 28 A 480 ALA GLN LEU THR PRO ARG VAL VAL GLU ARG TRP GLN LYS
SEQRES 29 A 480 SER MET THR ASN ARG THR ARG GLU VAL LEU LEU PRO LYS
SEQRES 30 A 480 PHE LYS LEU GLU LYS ASN TYR ASN LEU VAL GLU SER LEU
SEQRES 31 A 480 LYS LEU MET GLY ILE ARG MET LEU PHE ASP LYS ASN GLY
SEQRES 32 A 480 ASN MET ALA GLY ILE SER ASP GLN ARG ILE ALA ILE ASP
SEQRES 33 A 480 LEU PHE LYS HIS GLN GLY THR ILE THR VAL ASN GLU GLU
SEQRES 34 A 480 GLY THR GLN ALA THR THR VAL THR THR VAL GLY PHE MET
SEQRES 35 A 480 PRO LEU SER THR GLN VAL ARG PHE THR VAL ASP ARG PRO
SEQRES 36 A 480 PHE LEU PHE LEU ILE TYR GLU HIS ARG THR SER CYS LEU
SEQRES 37 A 480 LEU PHE MET GLY ARG VAL ALA ASN PRO SER ARG SER
SEQRES 1 B 480 GLY SER LYS GLY PRO LEU ASP GLN LEU GLU LYS GLY GLY
SEQRES 2 B 480 GLU THR ALA GLN SER ALA ASP PRO GLN TRP GLU GLN LEU
SEQRES 3 B 480 ASN ASN LYS ASN LEU SER MET PRO LEU LEU PRO ALA ASP
SEQRES 4 B 480 PHE HIS LYS GLU ASN THR VAL THR ASN ASP TRP ILE PRO
SEQRES 5 B 480 GLU GLY GLU GLU ASP ASP ASP TYR LEU ASP LEU GLU LYS
SEQRES 6 B 480 ILE PHE SER GLU ASP ASP ASP TYR ILE ASP ILE VAL ASP
SEQRES 7 B 480 SER LEU SER VAL SER PRO THR ASP SER ASP VAL SER ALA
SEQRES 8 B 480 GLY ASN ILE LEU GLN LEU PHE HIS GLY LYS SER ARG ILE
SEQRES 9 B 480 GLN ARG LEU ASN ILE LEU ASN ALA LYS PHE ALA PHE ASN
SEQRES 10 B 480 LEU TYR ARG VAL LEU LYS ASP GLN VAL ASN THR PHE ASP
SEQRES 11 B 480 ASN ILE PHE ILE ALA PRO VAL GLY ILE SER THR ALA MET
SEQRES 12 B 480 GLY MET ILE SER LEU GLY LEU LYS GLY GLU THR HIS GLU
SEQRES 13 B 480 GLN VAL HIS SER ILE LEU HIS PHE LYS ASP PHE VAL ASN
SEQRES 14 B 480 ALA SER SER LYS TYR GLU ILE THR THR ILE HIS ASN LEU
SEQRES 15 B 480 PHE ARG LYS LEU THR HIS ARG LEU PHE ARG ARG ASN PHE
SEQRES 16 B 480 GLY TYR THR LEU ARG SER VAL ASN ASP LEU TYR ILE GLN
SEQRES 17 B 480 LYS GLN PHE PRO ILE LEU LEU ASP PHE LYS THR LYS VAL
SEQRES 18 B 480 ARG GLU TYR TYR PHE ALA GLU ALA GLN ILE ALA ASP PHE
SEQRES 19 B 480 SER ASP PRO ALA PHE ILE SER LYS THR ASN ASN HIS ILE
SEQRES 20 B 480 MET LYS LEU THR LYS GLY LEU ILE LYS ASP ALA LEU GLU
SEQRES 21 B 480 ASN ILE ASP PRO ALA THR GLN MET MET ILE LEU ASN CYS
SEQRES 22 B 480 ILE TYR PHE LYS GLY SER TRP VAL ASN LYS PHE PRO VAL
SEQRES 23 B 480 GLU MET THR HIS ASN HIS ASN PHE ARG LEU ASN GLU ARG
SEQRES 24 B 480 GLU VAL VAL LYS VAL SER MET MET GLN THR LYS GLY ASN
SEQRES 25 B 480 PHE LEU ALA ALA ASN ASP GLN GLU LEU ASP CYS ASP ILE
SEQRES 26 B 480 LEU GLN LEU GLU TYR VAL GLY GLY ILE SER MET LEU ILE
SEQRES 27 B 480 VAL VAL PRO HIS LYS MET SER GLY MET LYS THR LEU GLU
SEQRES 28 B 480 ALA GLN LEU THR PRO ARG VAL VAL GLU ARG TRP GLN LYS
SEQRES 29 B 480 SER MET THR ASN ARG THR ARG GLU VAL LEU LEU PRO LYS
SEQRES 30 B 480 PHE LYS LEU GLU LYS ASN TYR ASN LEU VAL GLU SER LEU
SEQRES 31 B 480 LYS LEU MET GLY ILE ARG MET LEU PHE ASP LYS ASN GLY
SEQRES 32 B 480 ASN MET ALA GLY ILE SER ASP GLN ARG ILE ALA ILE ASP
SEQRES 33 B 480 LEU PHE LYS HIS GLN GLY THR ILE THR VAL ASN GLU GLU
SEQRES 34 B 480 GLY THR GLN ALA THR THR VAL THR THR VAL GLY PHE MET
SEQRES 35 B 480 PRO LEU SER THR GLN VAL ARG PHE THR VAL ASP ARG PRO
SEQRES 36 B 480 PHE LEU PHE LEU ILE TYR GLU HIS ARG THR SER CYS LEU
SEQRES 37 B 480 LEU PHE MET GLY ARG VAL ALA ASN PRO SER ARG SER
MODRES 1JMJ ASN A 368 ASN GLYCOSYLATION SITE
MODRES 1JMJ ASN B 368 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET BMA C 3 11
HET CA A 501 1
HET NAG B 481 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM CA CALCIUM ION
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 BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 3 NAG 3(C8 H15 N O6)
FORMUL 3 BMA C6 H12 O6
FORMUL 4 CA CA 2+
FORMUL 6 HOH *297(H2 O)
HELIX 1 1 ASP A 62 SER A 68 1 7
HELIX 2 2 SER A 102 ASP A 124 1 23
HELIX 3 3 ALA A 135 SER A 147 1 13
HELIX 4 4 LEU A 148 LEU A 150 5 3
HELIX 5 5 LYS A 151 LEU A 162 1 12
HELIX 6 6 HIS A 163 SER A 171 1 9
HELIX 7 7 GLU A 175 ARG A 192 1 18
HELIX 8 8 LEU A 214 TYR A 225 1 12
HELIX 9 9 ASP A 236 THR A 251 1 16
HELIX 10 10 PRO A 285 THR A 289 5 5
HELIX 11 11 SER A 345 LEU A 354 1 10
HELIX 12 12 THR A 355 SER A 365 1 11
HELIX 13 13 LEU A 386 GLY A 394 1 9
HELIX 14 14 ARG A 396 ASP A 400 5 5
HELIX 15 15 SER B 102 ASP B 124 1 23
HELIX 16 16 ALA B 135 LEU B 148 1 14
HELIX 17 17 LYS B 151 LEU B 162 1 12
HELIX 18 18 HIS B 163 ASN B 169 1 7
HELIX 19 19 GLU B 175 ARG B 192 1 18
HELIX 20 20 LEU B 214 PHE B 226 1 13
HELIX 21 21 ASP B 236 THR B 251 1 16
HELIX 22 22 PRO B 285 THR B 289 5 5
HELIX 23 23 SER B 345 LEU B 354 1 10
HELIX 24 24 THR B 355 SER B 365 1 11
HELIX 25 25 LEU B 386 GLY B 394 1 9
HELIX 26 26 ARG B 396 ASP B 400 5 5
SHEET 1 A 4 ARG A 449 THR A 451 0
SHEET 2 A 4 THR A 367 PRO A 376 1 O GLU A 372 N PHE A 450
SHEET 3 A 4 VAL A 301 ASP A 318 -1 N MET A 307 O LEU A 375
SHEET 4 A 4 HIS A 290 ARG A 295 -1 O HIS A 290 N MET A 306
SHEET 1 B 8 ARG A 449 THR A 451 0
SHEET 2 B 8 THR A 367 PRO A 376 1 O GLU A 372 N PHE A 450
SHEET 3 B 8 VAL A 301 ASP A 318 -1 N MET A 307 O LEU A 375
SHEET 4 B 8 CYS A 323 TYR A 330 -1 O CYS A 323 N ASP A 318
SHEET 5 B 8 ILE A 334 PRO A 341 -1 O ILE A 334 N TYR A 330
SHEET 6 B 8 PHE A 456 GLU A 462 -1 O LEU A 457 N VAL A 339
SHEET 7 B 8 CYS A 467 VAL A 474 -1 O CYS A 467 N GLU A 462
SHEET 8 B 8 ILE A 132 ILE A 134 -1 N ILE A 132 O ARG A 473
SHEET 1 C 5 ALA A 229 ALA A 232 0
SHEET 2 C 5 THR A 198 GLN A 208 1 O LEU A 205 N GLN A 230
SHEET 3 C 5 MET A 268 LYS A 277 -1 O MET A 269 N TYR A 206
SHEET 4 C 5 ILE A 415 VAL A 426 1 N ASP A 416 O MET A 268
SHEET 5 C 5 PHE A 378 GLU A 381 -1 O PHE A 378 N VAL A 426
SHEET 1 D 5 ALA A 229 ALA A 232 0
SHEET 2 D 5 THR A 198 GLN A 208 1 O LEU A 205 N GLN A 230
SHEET 3 D 5 MET A 268 LYS A 277 -1 O MET A 269 N TYR A 206
SHEET 4 D 5 ILE A 415 VAL A 426 1 N ASP A 416 O MET A 268
SHEET 5 D 5 TYR A 384 ASN A 385 -1 N TYR A 384 O HIS A 420
SHEET 1 E 4 ARG B 449 THR B 451 0
SHEET 2 E 4 THR B 367 PRO B 376 1 O GLU B 372 N PHE B 450
SHEET 3 E 4 VAL B 301 ASP B 318 -1 N MET B 307 O LEU B 375
SHEET 4 E 4 HIS B 290 ARG B 295 -1 O HIS B 290 N MET B 306
SHEET 1 F 8 ARG B 449 THR B 451 0
SHEET 2 F 8 THR B 367 PRO B 376 1 O GLU B 372 N PHE B 450
SHEET 3 F 8 VAL B 301 ASP B 318 -1 N MET B 307 O LEU B 375
SHEET 4 F 8 CYS B 323 TYR B 330 -1 O CYS B 323 N ASP B 318
SHEET 5 F 8 ILE B 334 PRO B 341 -1 O ILE B 334 N TYR B 330
SHEET 6 F 8 PHE B 456 GLU B 462 -1 O LEU B 457 N VAL B 339
SHEET 7 F 8 CYS B 467 VAL B 474 -1 O CYS B 467 N GLU B 462
SHEET 8 F 8 ILE B 132 ILE B 134 -1 N ILE B 132 O ARG B 473
SHEET 1 G 5 ALA B 229 ALA B 232 0
SHEET 2 G 5 THR B 198 GLN B 208 1 O LEU B 205 N GLN B 230
SHEET 3 G 5 MET B 268 LYS B 277 -1 O MET B 269 N TYR B 206
SHEET 4 G 5 ILE B 415 VAL B 426 1 N ASP B 416 O MET B 268
SHEET 5 G 5 PHE B 378 GLU B 381 -1 O PHE B 378 N VAL B 426
SHEET 1 H 5 ALA B 229 ALA B 232 0
SHEET 2 H 5 THR B 198 GLN B 208 1 O LEU B 205 N GLN B 230
SHEET 3 H 5 MET B 268 LYS B 277 -1 O MET B 269 N TYR B 206
SHEET 4 H 5 ILE B 415 VAL B 426 1 N ASP B 416 O MET B 268
SHEET 5 H 5 TYR B 384 ASN B 385 -1 N TYR B 384 O HIS B 420
LINK ND2 ASN A 368 C1 NAG C 1 1555 1555 1.45
LINK ND2 ASN B 368 C1 NAG B 481 1555 1555 1.46
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.39
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.39
LINK NE2 HIS A 290 CA CA A 501 1555 1555 2.55
LINK ND1 HIS A 292 CA CA A 501 1555 1555 2.67
LINK CA CA A 501 O HOH A 502 1555 1555 3.10
LINK CA CA A 501 O HOH A 551 1555 1555 2.84
LINK CA CA A 501 O HOH A 631 1555 1555 2.65
CRYST1 74.730 80.000 92.240 90.00 102.04 90.00 P 1 21 1 4
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 0.013382 0.000000 0.002854 0.00000
SCALE2 0.000000 0.012500 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011085 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
