HEADER HYDROLASE 22-DEC-15 5FIB
TITLE OPEN FORM OF MURINE ACID SPHINGOMYELINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SPHINGOMYELIN PHOSPHODIESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 84-611;
COMPND 5 SYNONYM: ACID SPHINGOMYELINASE,ASMASE;
COMPND 6 EC: 3.1.4.12;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: SMPD1, ASM;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS SMPD1, ASM, ASMASE, SAPOSIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.GORELIK,K.ILLES,L.X.HEINZ,G.SUPERTI-FURGA,B.NAGAR
REVDAT 5 27-SEP-23 5FIB 1 HETSYN LINK
REVDAT 4 29-JUL-20 5FIB 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 20-JUN-18 5FIB 1 KEYWDS REMARK
REVDAT 2 03-AUG-16 5FIB 1 JRNL
REVDAT 1 06-JUL-16 5FIB 0
JRNL AUTH A.GORELIK,K.ILLES,L.X.HEINZ,G.SUPERTI-FURGA,B.NAGAR
JRNL TITL CRYSTAL STRUCTURE OF MAMMALIAN ACID SPHINGOMYELINASE.
JRNL REF NAT COMMUN V. 7 12196 2016
JRNL REFN ESSN 2041-1723
JRNL PMID 27435900
JRNL DOI 10.1038/NCOMMS12196
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 73.2
REMARK 3 NUMBER OF REFLECTIONS : 63065
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930
REMARK 3 FREE R VALUE TEST SET COUNT : 3109
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 45.7037 - 7.8332 1.00 3717 193 0.1687 0.2112
REMARK 3 2 7.8332 - 6.2224 1.00 3713 196 0.1828 0.2306
REMARK 3 3 6.2224 - 5.4373 1.00 3717 200 0.1782 0.2075
REMARK 3 4 5.4373 - 4.9408 1.00 3712 200 0.1499 0.1844
REMARK 3 5 4.9408 - 4.5870 1.00 3714 196 0.1364 0.1741
REMARK 3 6 4.5870 - 4.3168 1.00 3706 196 0.1432 0.1909
REMARK 3 7 4.3168 - 4.1008 1.00 3734 194 0.1572 0.2420
REMARK 3 8 4.1008 - 3.9223 1.00 3700 192 0.1693 0.2078
REMARK 3 9 3.9223 - 3.7714 0.99 3676 186 0.1843 0.2547
REMARK 3 10 3.7714 - 3.6413 0.89 3325 174 0.1963 0.2580
REMARK 3 11 3.6413 - 3.5275 0.80 2963 149 0.2086 0.2483
REMARK 3 12 3.5275 - 3.4267 0.73 2712 135 0.2247 0.3370
REMARK 3 13 3.4267 - 3.3365 0.69 2551 135 0.2494 0.2810
REMARK 3 14 3.3365 - 3.2552 0.66 2454 130 0.2696 0.2729
REMARK 3 15 3.2552 - 3.1812 0.63 2325 121 0.2758 0.2969
REMARK 3 16 3.1812 - 3.1135 0.59 2213 114 0.2778 0.3794
REMARK 3 17 3.1135 - 3.0512 0.51 1875 105 0.2858 0.2701
REMARK 3 18 3.0512 - 2.9937 0.42 1596 68 0.2892 0.3780
REMARK 3 19 2.9937 - 2.9402 0.37 1371 69 0.2881 0.3390
REMARK 3 20 2.9402 - 2.8904 0.32 1202 51 0.2972 0.3566
REMARK 3 21 2.8904 - 2.8438 0.29 1056 59 0.2940 0.3706
REMARK 3 22 2.8438 - 2.8000 0.25 924 46 0.3102 0.2844
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.940
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 : 0.005 9346
REMARK 3 ANGLE : 0.756 12838
REMARK 3 CHIRALITY : 0.041 1440
REMARK 3 PLANARITY : 0.004 1585
REMARK 3 DIHEDRAL : 12.766 5458
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 5FIB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216634.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63590
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 45.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.720
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.3900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: 5HNQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 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 -Y+1/2,X+1/2,Z
REMARK 290 4555 Y+1/2,-X+1/2,Z
REMARK 290 5555 -X+1/2,Y+1/2,-Z
REMARK 290 6555 X+1/2,-Y+1/2,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 90.58650
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 90.58650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 90.58650
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 90.58650
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 90.58650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 90.58650
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 90.58650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 90.58650
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, E, F, G
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H, I, J
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 74
REMARK 465 ARG A 75
REMARK 465 PRO A 610
REMARK 465 ASN A 611
REMARK 465 ASP B 74
REMARK 465 ARG B 75
REMARK 465 PRO B 610
REMARK 465 ASN B 611
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER B 152 O4 MAN J 4 1.94
REMARK 500 O3 NAG I 2 O2 BMA I 3 2.02
REMARK 500 O5 NAG D 1 O2 FUC D 3 2.10
REMARK 500 OE1 GLU B 407 O HOH B 801 2.16
REMARK 500
REMARK 500 REMARK: NULL
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 ASN A 122 O3 FUC J 5 7553 2.07
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 ASN A 84 20.40 -78.21
REMARK 500 ALA A 124 -176.82 -50.73
REMARK 500 SER A 147 -75.42 -115.84
REMARK 500 PHE A 169 29.66 48.78
REMARK 500 HIS A 206 70.27 56.82
REMARK 500 CYS A 224 -159.74 -119.21
REMARK 500 SER A 246 -164.66 -175.14
REMARK 500 THR A 274 39.59 -94.13
REMARK 500 PRO A 327 175.76 -56.06
REMARK 500 ASN A 333 -37.45 -33.36
REMARK 500 ASP A 396 61.52 29.16
REMARK 500 HIS A 423 -67.07 -102.01
REMARK 500 TYR A 444 43.79 -108.60
REMARK 500 HIS A 455 -51.79 75.96
REMARK 500 ASN A 518 101.90 -59.89
REMARK 500 ASN B 84 37.03 -86.84
REMARK 500 ASN B 122 78.96 52.90
REMARK 500 ALA B 124 -166.18 -51.57
REMARK 500 SER B 147 -69.42 -120.92
REMARK 500 SER B 161 2.27 -69.55
REMARK 500 TYR B 218 51.38 -117.84
REMARK 500 CYS B 224 -164.06 -122.29
REMARK 500 SER B 246 -167.94 -174.43
REMARK 500 ASP B 249 -168.83 -106.13
REMARK 500 THR B 274 33.14 -91.79
REMARK 500 ASP B 276 72.06 60.60
REMARK 500 GLN B 284 53.26 -140.09
REMARK 500 ASN B 323 -15.64 76.11
REMARK 500 ASN B 393 97.16 -165.01
REMARK 500 ASP B 396 62.86 27.35
REMARK 500 HIS B 423 -70.71 -93.75
REMARK 500 HIS B 455 -44.89 75.52
REMARK 500 ASN B 518 99.75 -66.44
REMARK 500 SER B 596 71.49 -106.45
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 ZN A 703 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 78 NE2
REMARK 620 2 HIS A 80 NE2 96.0
REMARK 620 3 HIS B 573 NE2 19.0 114.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 701 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 204 OD1
REMARK 620 2 HIS A 206 NE2 134.8
REMARK 620 3 ASP A 276 OD1 96.3 91.8
REMARK 620 4 HIS A 457 NE2 85.1 98.7 163.8
REMARK 620 5 HOH A 802 O 93.5 131.0 71.2 92.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 702 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 276 OD1
REMARK 620 2 ASN A 316 OD1 92.6
REMARK 620 3 HIS A 423 NE2 85.7 97.3
REMARK 620 4 HIS A 455 ND1 156.0 107.2 104.6
REMARK 620 5 HOH A 802 O 67.5 129.2 125.3 89.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 703 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 573 NE2
REMARK 620 2 HIS B 78 NE2 108.2
REMARK 620 3 HIS B 80 NE2 107.8 0.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 701 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 204 OD1
REMARK 620 2 HIS B 206 NE2 124.7
REMARK 620 3 ASP B 276 OD1 81.7 90.6
REMARK 620 4 HIS B 457 NE2 92.8 100.1 169.3
REMARK 620 5 HOH B 806 O 110.8 118.4 71.7 102.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 702 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 276 OD1
REMARK 620 2 ASN B 316 OD1 103.5
REMARK 620 3 HIS B 423 NE2 79.6 95.1
REMARK 620 4 HIS B 455 ND1 162.5 94.0 100.5
REMARK 620 5 HOH B 806 O 71.8 122.0 137.1 97.8
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FI9 RELATED DB: PDB
REMARK 900 RELATED ID: 5FIC RELATED DB: PDB
REMARK 900 RELATED ID: 5HQN RELATED DB: PDB
DBREF 5FIB A 84 611 UNP Q04519 ASM_MOUSE 84 611
DBREF 5FIB B 84 611 UNP Q04519 ASM_MOUSE 84 611
SEQADV 5FIB ASP A 74 UNP Q04519 EXPRESSION TAG
SEQADV 5FIB ARG A 75 UNP Q04519 EXPRESSION TAG
SEQADV 5FIB HIS A 76 UNP Q04519 EXPRESSION TAG
SEQADV 5FIB HIS A 77 UNP Q04519 EXPRESSION TAG
SEQADV 5FIB HIS A 78 UNP Q04519 EXPRESSION TAG
SEQADV 5FIB HIS A 79 UNP Q04519 EXPRESSION TAG
SEQADV 5FIB HIS A 80 UNP Q04519 EXPRESSION TAG
SEQADV 5FIB HIS A 81 UNP Q04519 EXPRESSION TAG
SEQADV 5FIB LYS A 82 UNP Q04519 EXPRESSION TAG
SEQADV 5FIB LEU A 83 UNP Q04519 EXPRESSION TAG
SEQADV 5FIB ASP B 74 UNP Q04519 EXPRESSION TAG
SEQADV 5FIB ARG B 75 UNP Q04519 EXPRESSION TAG
SEQADV 5FIB HIS B 76 UNP Q04519 EXPRESSION TAG
SEQADV 5FIB HIS B 77 UNP Q04519 EXPRESSION TAG
SEQADV 5FIB HIS B 78 UNP Q04519 EXPRESSION TAG
SEQADV 5FIB HIS B 79 UNP Q04519 EXPRESSION TAG
SEQADV 5FIB HIS B 80 UNP Q04519 EXPRESSION TAG
SEQADV 5FIB HIS B 81 UNP Q04519 EXPRESSION TAG
SEQADV 5FIB LYS B 82 UNP Q04519 EXPRESSION TAG
SEQADV 5FIB LEU B 83 UNP Q04519 EXPRESSION TAG
SEQRES 1 A 538 ASP ARG HIS HIS HIS HIS HIS HIS LYS LEU ASN LEU THR
SEQRES 2 A 538 CYS PRO ALA CYS LYS VAL LEU PHE THR ALA LEU ASN HIS
SEQRES 3 A 538 GLY LEU LYS LYS GLU PRO ASN VAL ALA ARG VAL GLY SER
SEQRES 4 A 538 VAL ALA ILE LYS ILE CYS LYS MET LEU ASN ILE ALA PRO
SEQRES 5 A 538 LEU ASP VAL CYS GLN SER ALA VAL HIS LEU PHE GLU ASP
SEQRES 6 A 538 ASP VAL VAL GLU VAL TRP THR ARG SER VAL LEU SER PRO
SEQRES 7 A 538 SER GLU ALA CYS GLY LEU LEU LEU GLY SER SER CYS GLY
SEQRES 8 A 538 HIS TRP ASP ILE PHE SER THR TRP ASN ILE SER LEU PRO
SEQRES 9 A 538 SER VAL PRO LYS PRO PRO PRO LYS PRO PRO SER PRO PRO
SEQRES 10 A 538 ALA PRO GLY ALA PRO VAL SER ARG VAL LEU PHE LEU THR
SEQRES 11 A 538 ASP LEU HIS TRP ASP HIS GLU TYR LEU GLU GLY THR ASP
SEQRES 12 A 538 PRO TYR CYS ALA ASP PRO LEU CYS CYS ARG ARG GLY SER
SEQRES 13 A 538 GLY TRP PRO PRO ASN SER GLN LYS GLY ALA GLY PHE TRP
SEQRES 14 A 538 GLY GLU TYR SER LYS CYS ASP LEU PRO LEU ARG THR LEU
SEQRES 15 A 538 GLU SER LEU LEU LYS GLY LEU GLY PRO ALA GLY PRO PHE
SEQRES 16 A 538 GLU MET VAL TYR TRP THR GLY ASP ILE PRO ALA HIS ASP
SEQRES 17 A 538 VAL TRP GLN GLN SER ARG GLN ASP GLN LEU ARG ALA LEU
SEQRES 18 A 538 THR THR ILE THR ASP LEU VAL ARG LYS PHE LEU GLY PRO
SEQRES 19 A 538 VAL PRO VAL TYR PRO ALA VAL GLY ASN HIS GLU SER THR
SEQRES 20 A 538 PRO VAL ASN GLY PHE PRO PRO PRO PHE ILE LYS GLY ASN
SEQRES 21 A 538 GLN SER SER GLN TRP LEU TYR GLU ALA MET ALA LYS ALA
SEQRES 22 A 538 TRP GLU PRO TRP LEU PRO ALA ASP ALA LEU HIS THR LEU
SEQRES 23 A 538 ARG ILE GLY GLY PHE TYR ALA LEU THR PRO ARG PRO GLY
SEQRES 24 A 538 LEU ARG LEU ILE SER LEU ASN MET ASN PHE CYS SER ARG
SEQRES 25 A 538 GLU ASN PHE TRP LEU LEU ILE ASN SER THR ASP PRO ALA
SEQRES 26 A 538 GLY GLN LEU GLN TRP LEU VAL GLU GLU LEU GLN ALA ALA
SEQRES 27 A 538 GLU ASN ARG GLY ASP LYS VAL HIS ILE ILE GLY HIS ILE
SEQRES 28 A 538 PRO PRO GLY HIS CYS LEU LYS SER TRP SER TRP ASN TYR
SEQRES 29 A 538 TYR LYS ILE ILE ALA ARG TYR GLU ASN THR LEU ALA GLY
SEQRES 30 A 538 GLN PHE PHE GLY HIS THR HIS VAL ASP GLU PHE GLU ILE
SEQRES 31 A 538 PHE TYR ASP GLU GLU THR LEU SER ARG PRO LEU ALA VAL
SEQRES 32 A 538 ALA PHE LEU ALA PRO SER ALA THR THR PHE ILE ASN LEU
SEQRES 33 A 538 ASN PRO GLY TYR ARG VAL TYR GLN ILE ASP GLY ASN TYR
SEQRES 34 A 538 PRO GLY SER SER HIS VAL VAL LEU ASP HIS GLU THR TYR
SEQRES 35 A 538 ILE LEU ASN LEU THR GLN ALA ASN ALA ALA GLY GLY THR
SEQRES 36 A 538 PRO SER TRP LYS ARG LEU TYR ARG ALA ARG GLU THR TYR
SEQRES 37 A 538 GLY LEU PRO ASP ALA MET PRO ALA SER TRP HIS ASN LEU
SEQRES 38 A 538 VAL TYR ARG MET ARG ASP ASP GLU GLN LEU PHE GLN THR
SEQRES 39 A 538 PHE TRP PHE LEU TYR HIS LYS GLY HIS PRO PRO SER GLU
SEQRES 40 A 538 PRO CYS GLY THR PRO CYS ARG LEU ALA THR LEU CYS ALA
SEQRES 41 A 538 GLN LEU SER ALA ARG ALA ASP SER PRO ALA LEU CYS ARG
SEQRES 42 A 538 HIS LEU MET PRO ASN
SEQRES 1 B 538 ASP ARG HIS HIS HIS HIS HIS HIS LYS LEU ASN LEU THR
SEQRES 2 B 538 CYS PRO ALA CYS LYS VAL LEU PHE THR ALA LEU ASN HIS
SEQRES 3 B 538 GLY LEU LYS LYS GLU PRO ASN VAL ALA ARG VAL GLY SER
SEQRES 4 B 538 VAL ALA ILE LYS ILE CYS LYS MET LEU ASN ILE ALA PRO
SEQRES 5 B 538 LEU ASP VAL CYS GLN SER ALA VAL HIS LEU PHE GLU ASP
SEQRES 6 B 538 ASP VAL VAL GLU VAL TRP THR ARG SER VAL LEU SER PRO
SEQRES 7 B 538 SER GLU ALA CYS GLY LEU LEU LEU GLY SER SER CYS GLY
SEQRES 8 B 538 HIS TRP ASP ILE PHE SER THR TRP ASN ILE SER LEU PRO
SEQRES 9 B 538 SER VAL PRO LYS PRO PRO PRO LYS PRO PRO SER PRO PRO
SEQRES 10 B 538 ALA PRO GLY ALA PRO VAL SER ARG VAL LEU PHE LEU THR
SEQRES 11 B 538 ASP LEU HIS TRP ASP HIS GLU TYR LEU GLU GLY THR ASP
SEQRES 12 B 538 PRO TYR CYS ALA ASP PRO LEU CYS CYS ARG ARG GLY SER
SEQRES 13 B 538 GLY TRP PRO PRO ASN SER GLN LYS GLY ALA GLY PHE TRP
SEQRES 14 B 538 GLY GLU TYR SER LYS CYS ASP LEU PRO LEU ARG THR LEU
SEQRES 15 B 538 GLU SER LEU LEU LYS GLY LEU GLY PRO ALA GLY PRO PHE
SEQRES 16 B 538 GLU MET VAL TYR TRP THR GLY ASP ILE PRO ALA HIS ASP
SEQRES 17 B 538 VAL TRP GLN GLN SER ARG GLN ASP GLN LEU ARG ALA LEU
SEQRES 18 B 538 THR THR ILE THR ASP LEU VAL ARG LYS PHE LEU GLY PRO
SEQRES 19 B 538 VAL PRO VAL TYR PRO ALA VAL GLY ASN HIS GLU SER THR
SEQRES 20 B 538 PRO VAL ASN GLY PHE PRO PRO PRO PHE ILE LYS GLY ASN
SEQRES 21 B 538 GLN SER SER GLN TRP LEU TYR GLU ALA MET ALA LYS ALA
SEQRES 22 B 538 TRP GLU PRO TRP LEU PRO ALA ASP ALA LEU HIS THR LEU
SEQRES 23 B 538 ARG ILE GLY GLY PHE TYR ALA LEU THR PRO ARG PRO GLY
SEQRES 24 B 538 LEU ARG LEU ILE SER LEU ASN MET ASN PHE CYS SER ARG
SEQRES 25 B 538 GLU ASN PHE TRP LEU LEU ILE ASN SER THR ASP PRO ALA
SEQRES 26 B 538 GLY GLN LEU GLN TRP LEU VAL GLU GLU LEU GLN ALA ALA
SEQRES 27 B 538 GLU ASN ARG GLY ASP LYS VAL HIS ILE ILE GLY HIS ILE
SEQRES 28 B 538 PRO PRO GLY HIS CYS LEU LYS SER TRP SER TRP ASN TYR
SEQRES 29 B 538 TYR LYS ILE ILE ALA ARG TYR GLU ASN THR LEU ALA GLY
SEQRES 30 B 538 GLN PHE PHE GLY HIS THR HIS VAL ASP GLU PHE GLU ILE
SEQRES 31 B 538 PHE TYR ASP GLU GLU THR LEU SER ARG PRO LEU ALA VAL
SEQRES 32 B 538 ALA PHE LEU ALA PRO SER ALA THR THR PHE ILE ASN LEU
SEQRES 33 B 538 ASN PRO GLY TYR ARG VAL TYR GLN ILE ASP GLY ASN TYR
SEQRES 34 B 538 PRO GLY SER SER HIS VAL VAL LEU ASP HIS GLU THR TYR
SEQRES 35 B 538 ILE LEU ASN LEU THR GLN ALA ASN ALA ALA GLY GLY THR
SEQRES 36 B 538 PRO SER TRP LYS ARG LEU TYR ARG ALA ARG GLU THR TYR
SEQRES 37 B 538 GLY LEU PRO ASP ALA MET PRO ALA SER TRP HIS ASN LEU
SEQRES 38 B 538 VAL TYR ARG MET ARG ASP ASP GLU GLN LEU PHE GLN THR
SEQRES 39 B 538 PHE TRP PHE LEU TYR HIS LYS GLY HIS PRO PRO SER GLU
SEQRES 40 B 538 PRO CYS GLY THR PRO CYS ARG LEU ALA THR LEU CYS ALA
SEQRES 41 B 538 GLN LEU SER ALA ARG ALA ASP SER PRO ALA LEU CYS ARG
SEQRES 42 B 538 HIS LEU MET PRO ASN
HET NAG C 1 26
HET NAG C 2 28
HET FUC C 3 21
HET NAG D 1 26
HET NAG D 2 28
HET FUC D 3 21
HET NAG E 1 26
HET NAG E 2 27
HET BMA E 3 20
HET MAN E 4 22
HET MAN E 5 22
HET FUC E 6 21
HET NAG F 1 27
HET NAG F 2 28
HET NAG G 1 26
HET NAG G 2 27
HET BMA G 3 22
HET FUC G 4 21
HET NAG H 1 26
HET NAG H 2 27
HET BMA H 3 20
HET MAN H 4 22
HET MAN H 5 22
HET FUC H 6 21
HET NAG I 1 27
HET NAG I 2 27
HET BMA I 3 20
HET MAN I 4 22
HET MAN I 5 22
HET NAG J 1 26
HET NAG J 2 27
HET BMA J 3 21
HET MAN J 4 22
HET FUC J 5 21
HET ZN A 701 1
HET ZN A 702 1
HET ZN A 703 1
HET SO4 A 722 5
HET SO4 A 723 5
HET SO4 A 724 5
HET SO4 A 725 5
HET SO4 A 726 5
HET SO4 A 727 5
HET SO4 A 728 5
HET SO4 A 729 5
HET SO4 A 730 5
HET SO4 A 731 5
HET ZN B 701 1
HET ZN B 702 1
HET ZN B 703 1
HET NAG B 704 28
HET SO4 B 721 5
HET SO4 B 722 5
HET SO4 B 723 5
HET SO4 B 724 5
HET SO4 B 725 5
HET SO4 B 726 5
HET SO4 B 727 5
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE 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 FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 3 NAG 17(C8 H15 N O6)
FORMUL 3 FUC 6(C6 H12 O5)
FORMUL 5 BMA 5(C6 H12 O6)
FORMUL 5 MAN 7(C6 H12 O6)
FORMUL 11 ZN 6(ZN 2+)
FORMUL 14 SO4 17(O4 S 2-)
FORMUL 35 HOH *30(H2 O)
HELIX 1 AA1 LEU A 85 LYS A 103 1 19
HELIX 2 AA2 LYS A 103 LEU A 121 1 19
HELIX 3 AA3 PRO A 125 SER A 147 1 23
HELIX 4 AA4 SER A 150 GLY A 160 1 11
HELIX 5 AA5 PRO A 251 GLY A 261 1 11
HELIX 6 AA6 GLY A 261 GLY A 266 1 6
HELIX 7 AA7 ASP A 281 GLN A 285 5 5
HELIX 8 AA8 SER A 286 GLY A 306 1 21
HELIX 9 AA9 SER A 336 TRP A 347 1 12
HELIX 10 AB1 PRO A 352 GLY A 363 1 12
HELIX 11 AB2 ASN A 379 SER A 384 5 6
HELIX 12 AB3 ASN A 387 LEU A 391 5 5
HELIX 13 AB4 ASP A 396 ALA A 398 5 3
HELIX 14 AB5 GLY A 399 GLY A 415 1 17
HELIX 15 AB6 PRO A 425 CYS A 429 5 5
HELIX 16 AB7 LEU A 430 TYR A 444 1 15
HELIX 17 AB8 ASN A 518 ASN A 523 1 6
HELIX 18 AB9 ALA A 537 GLY A 542 1 6
HELIX 19 AC1 MET A 547 ASP A 561 1 15
HELIX 20 AC2 ASP A 561 HIS A 573 1 13
HELIX 21 AC3 GLY A 583 SER A 596 1 14
HELIX 22 AC4 SER A 601 ARG A 606 5 6
HELIX 23 AC5 LEU B 85 LYS B 103 1 19
HELIX 24 AC6 LYS B 103 LEU B 121 1 19
HELIX 25 AC7 PRO B 125 SER B 147 1 23
HELIX 26 AC8 SER B 150 GLY B 160 1 11
HELIX 27 AC9 SER B 161 CYS B 163 5 3
HELIX 28 AD1 PRO B 251 GLY B 261 1 11
HELIX 29 AD2 GLY B 261 GLY B 266 1 6
HELIX 30 AD3 ASP B 281 GLN B 285 5 5
HELIX 31 AD4 SER B 286 GLY B 306 1 21
HELIX 32 AD5 SER B 336 TRP B 347 1 12
HELIX 33 AD6 PRO B 352 GLY B 363 1 12
HELIX 34 AD7 ASN B 379 SER B 384 5 6
HELIX 35 AD8 ASN B 387 ILE B 392 5 6
HELIX 36 AD9 ASP B 396 ALA B 398 5 3
HELIX 37 AE1 GLY B 399 GLY B 415 1 17
HELIX 38 AE2 PRO B 425 CYS B 429 5 5
HELIX 39 AE3 LEU B 430 TYR B 444 1 15
HELIX 40 AE4 ASN B 518 ASN B 523 1 6
HELIX 41 AE5 ALA B 537 GLY B 542 1 6
HELIX 42 AE6 MET B 547 ASP B 561 1 15
HELIX 43 AE7 ASP B 561 HIS B 573 1 13
HELIX 44 AE8 GLY B 583 SER B 596 1 14
HELIX 45 AE9 SER B 601 ARG B 606 5 6
SHEET 1 AA1 6 VAL A 310 PRO A 312 0
SHEET 2 AA1 6 MET A 270 TRP A 273 1 N VAL A 271 O TYR A 311
SHEET 3 AA1 6 VAL A 196 LEU A 202 1 N LEU A 200 O TYR A 272
SHEET 4 AA1 6 GLY A 492 ASP A 499 -1 O TYR A 496 N VAL A 199
SHEET 5 AA1 6 VAL A 509 ILE A 516 -1 O LEU A 510 N GLN A 497
SHEET 6 AA1 6 LYS A 532 ARG A 536 -1 O LEU A 534 N THR A 514
SHEET 1 AA2 6 TYR A 365 ARG A 370 0
SHEET 2 AA2 6 LEU A 373 SER A 377 -1 O LEU A 375 N LEU A 367
SHEET 3 AA2 6 LYS A 417 ILE A 421 1 O HIS A 419 N ARG A 374
SHEET 4 AA2 6 LEU A 448 PHE A 453 1 O ALA A 449 N VAL A 418
SHEET 5 AA2 6 PRO A 473 LEU A 479 1 O PHE A 478 N GLN A 451
SHEET 6 AA2 6 GLU A 460 TYR A 465 -1 N PHE A 464 O ALA A 475
SHEET 1 AA3 6 VAL B 310 PRO B 312 0
SHEET 2 AA3 6 MET B 270 TRP B 273 1 N VAL B 271 O TYR B 311
SHEET 3 AA3 6 VAL B 196 LEU B 202 1 N LEU B 200 O TYR B 272
SHEET 4 AA3 6 GLY B 492 ASP B 499 -1 O ARG B 494 N PHE B 201
SHEET 5 AA3 6 VAL B 509 LEU B 517 -1 O LEU B 510 N GLN B 497
SHEET 6 AA3 6 TRP B 531 ARG B 536 -1 O LEU B 534 N THR B 514
SHEET 1 AA4 6 TYR B 365 ARG B 370 0
SHEET 2 AA4 6 LEU B 373 SER B 377 -1 O LEU B 375 N LEU B 367
SHEET 3 AA4 6 LYS B 417 ILE B 421 1 O HIS B 419 N ILE B 376
SHEET 4 AA4 6 LEU B 448 PHE B 453 1 O ALA B 449 N VAL B 418
SHEET 5 AA4 6 PRO B 473 LEU B 479 1 O PHE B 478 N GLN B 451
SHEET 6 AA4 6 GLU B 460 TYR B 465 -1 N PHE B 464 O ALA B 475
SSBOND 1 CYS A 87 CYS A 163 1555 1555 2.03
SSBOND 2 CYS A 90 CYS A 155 1555 1555 2.03
SSBOND 3 CYS A 118 CYS A 129 1555 1555 2.03
SSBOND 4 CYS A 219 CYS A 224 1555 1555 2.04
SSBOND 5 CYS A 225 CYS A 248 1555 1555 2.03
SSBOND 6 CYS A 383 CYS A 429 1555 1555 2.03
SSBOND 7 CYS A 582 CYS A 586 1555 1555 2.04
SSBOND 8 CYS A 592 CYS A 605 1555 1555 2.03
SSBOND 9 CYS B 87 CYS B 163 1555 1555 2.03
SSBOND 10 CYS B 90 CYS B 155 1555 1555 2.04
SSBOND 11 CYS B 118 CYS B 129 1555 1555 2.04
SSBOND 12 CYS B 219 CYS B 224 1555 1555 2.04
SSBOND 13 CYS B 225 CYS B 248 1555 1555 2.03
SSBOND 14 CYS B 383 CYS B 429 1555 1555 2.03
SSBOND 15 CYS B 582 CYS B 586 1555 1555 2.04
SSBOND 16 CYS B 592 CYS B 605 1555 1555 2.03
LINK ND2 ASN A 84 C1 NAG G 1 1555 1555 1.45
LINK ND2 ASN A 173 C1 NAG C 1 1555 1555 1.42
LINK ND2 ASN A 333 C1 NAG D 1 1555 1555 1.44
LINK ND2 ASN A 393 C1 NAG E 1 1555 1555 1.45
LINK ND2 ASN A 518 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN B 84 C1 NAG J 1 1555 1555 1.44
LINK ND2 ASN B 173 C1 NAG B 704 1555 1555 1.44
LINK ND2 ASN B 393 C1 NAG H 1 1555 1555 1.44
LINK ND2 ASN B 518 C1 NAG I 1 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O6 NAG C 1 C1 FUC C 3 1555 1555 1.45
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.46
LINK O6 NAG D 1 C1 FUC D 3 1555 1555 1.47
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.47
LINK O6 NAG E 1 C1 FUC E 6 1555 1555 1.45
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.46
LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.46
LINK O6 BMA E 3 C1 MAN E 5 1555 1555 1.46
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.46
LINK O6 NAG G 1 C1 FUC G 4 1555 1555 1.45
LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.45
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44
LINK O6 NAG H 1 C1 FUC H 6 1555 1555 1.45
LINK O4 NAG H 2 C1 BMA H 3 1555 1555 1.44
LINK O3 BMA H 3 C1 MAN H 4 1555 1555 1.45
LINK O6 BMA H 3 C1 MAN H 5 1555 1555 1.45
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.45
LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.45
LINK O3 BMA I 3 C1 MAN I 4 1555 1555 1.46
LINK O6 BMA I 3 C1 MAN I 5 1555 1555 1.45
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.42
LINK O6 NAG J 1 C1 FUC J 5 1555 1555 1.45
LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.46
LINK O3 BMA J 3 C1 MAN J 4 1555 1555 1.46
LINK NE2 HIS A 78 ZN ZN A 703 1555 1555 2.02
LINK NE2 HIS A 80 ZN ZN A 703 1555 1555 2.02
LINK OD1 ASP A 204 ZN ZN A 701 1555 1555 2.04
LINK NE2 HIS A 206 ZN ZN A 701 1555 1555 2.02
LINK OD1 ASP A 276 ZN ZN A 701 1555 1555 2.24
LINK OD1 ASP A 276 ZN ZN A 702 1555 1555 2.14
LINK OD1 ASN A 316 ZN ZN A 702 1555 1555 2.11
LINK NE2 HIS A 423 ZN ZN A 702 1555 1555 2.07
LINK ND1 HIS A 455 ZN ZN A 702 1555 1555 2.11
LINK NE2 HIS A 457 ZN ZN A 701 1555 1555 2.07
LINK NE2 HIS A 573 ZN ZN B 703 1555 7553 2.04
LINK ZN ZN A 701 O HOH A 802 1555 1555 1.99
LINK ZN ZN A 702 O HOH A 802 1555 1555 2.30
LINK ZN ZN A 703 NE2 HIS B 573 7553 1555 2.04
LINK NE2 HIS B 78 ZN ZN B 703 1555 1555 2.02
LINK NE2 HIS B 80 ZN ZN B 703 1555 1555 2.03
LINK OD1 ASP B 204 ZN ZN B 701 1555 1555 2.04
LINK NE2 HIS B 206 ZN ZN B 701 1555 1555 2.05
LINK OD1 ASP B 276 ZN ZN B 701 1555 1555 2.26
LINK OD1 ASP B 276 ZN ZN B 702 1555 1555 2.14
LINK OD1 ASN B 316 ZN ZN B 702 1555 1555 2.10
LINK NE2 HIS B 423 ZN ZN B 702 1555 1555 2.03
LINK ND1 HIS B 455 ZN ZN B 702 1555 1555 2.09
LINK NE2 HIS B 457 ZN ZN B 701 1555 1555 2.05
LINK ZN ZN B 701 O HOH B 806 1555 1555 2.16
LINK ZN ZN B 702 O HOH B 806 1555 1555 2.27
CISPEP 1 GLY A 266 PRO A 267 0 -2.00
CISPEP 2 THR A 320 PRO A 321 0 1.62
CISPEP 3 PHE A 486 ILE A 487 0 0.82
CISPEP 4 GLY B 266 PRO B 267 0 0.59
CISPEP 5 THR B 320 PRO B 321 0 1.97
CISPEP 6 PHE B 486 ILE B 487 0 0.22
CRYST1 181.173 181.173 109.891 90.00 90.00 90.00 P 4 21 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 0.005520 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005520 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009100 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
