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HEADER TRANSFERASE 22-OCT-18 6MTW
TITLE LYSOSOMAL PHOSPHOLIPASE A2 IN COMPLEX WITH ZINC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GROUP XV PHOSPHOLIPASE A2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 1-O-ACYLCERAMIDE SYNTHASE,ACS,LCAT-LIKE LYSOPHOSPHOLIPASE,
COMPND 5 LLPL,LYSOPHOSPHOLIPASE 3,LYSOSOMAL PHOSPHOLIPASE A2,LPLA2;
COMPND 6 EC: 2.3.1.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PLA2G15, LYPLA3, UNQ341/PRO540;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293F
KEYWDS LIPASE, ESTERASE, HYDROLASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.BOULEY,J.J.T.TESMER
REVDAT 1 20-MAR-19 6MTW 0
JRNL AUTH R.BOULEY,V.HINKOVSKA-GALCHEVA,J.A.SHAYMAN,J.TESMER
JRNL TITL STRUCTURAL BASIS OF LYSOSOMAL PHOSPHOLIPASE A2 INHIBITION BY
JRNL TITL 2 ZN2.
JRNL REF BIOCHEMISTRY 2019
JRNL REFN ISSN 1520-4995
JRNL PMID 30830753
JRNL DOI 10.1021/ACS.BIOCHEM.8B01124
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.34
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 57821
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.249
REMARK 3 R VALUE (WORKING SET) : 0.248
REMARK 3 FREE R VALUE : 0.285
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.450
REMARK 3 FREE R VALUE TEST SET COUNT : 3953
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 39.3442 - 6.0624 0.99 3975 134 0.2342 0.2613
REMARK 3 2 6.0624 - 4.8147 0.98 3988 141 0.2144 0.2574
REMARK 3 3 4.8147 - 4.2068 1.00 3961 127 0.1944 0.2257
REMARK 3 4 4.2068 - 3.8226 1.00 3995 150 0.1996 0.2109
REMARK 3 5 3.8226 - 3.5488 1.00 4003 144 0.2241 0.2638
REMARK 3 6 3.5488 - 3.3397 1.00 4028 140 0.2320 0.2593
REMARK 3 7 3.3397 - 3.1725 1.00 4000 152 0.2440 0.2844
REMARK 3 8 3.1725 - 3.0344 1.00 3987 142 0.2713 0.3032
REMARK 3 9 3.0344 - 2.9177 1.00 3978 144 0.2675 0.3258
REMARK 3 10 2.9177 - 2.8170 0.96 3810 141 0.2596 0.2781
REMARK 3 11 2.8170 - 2.7289 0.99 3967 140 0.2652 0.3748
REMARK 3 12 2.7289 - 2.6510 0.99 4004 140 0.2585 0.3218
REMARK 3 13 2.6510 - 2.5812 0.99 3984 144 0.2559 0.2866
REMARK 3 14 2.5812 - 2.5182 0.99 3970 143 0.2469 0.2914
REMARK 3 15 2.5182 - 2.4610 0.99 4007 144 0.2643 0.3024
REMARK 3 16 2.4610 - 2.4086 1.00 3934 134 0.2630 0.3213
REMARK 3 17 2.4086 - 2.3604 1.00 3991 142 0.2760 0.3126
REMARK 3 18 2.3604 - 2.3159 1.00 4065 146 0.2731 0.3089
REMARK 3 19 2.3159 - 2.2745 1.00 3976 142 0.2800 0.2800
REMARK 3 20 2.2745 - 2.2360 1.00 4009 148 0.3438 0.3702
REMARK 3 21 2.2360 - 2.1999 1.00 4034 146 0.3083 0.3643
REMARK 3 22 2.1999 - 2.1661 1.00 3913 140 0.2966 0.3820
REMARK 3 23 2.1661 - 2.1342 1.00 4041 140 0.2900 0.3225
REMARK 3 24 2.1342 - 2.1042 1.00 3923 145 0.2933 0.3755
REMARK 3 25 2.1042 - 2.0757 1.00 4075 154 0.3092 0.3286
REMARK 3 26 2.0757 - 2.0488 0.98 3944 139 0.3148 0.2824
REMARK 3 27 2.0488 - 2.0232 0.95 3711 128 0.3110 0.3385
REMARK 3 28 2.0232 - 1.9990 0.87 3491 123 0.3372 0.3940
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) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.030
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 : 0.003 6280
REMARK 3 ANGLE : 0.637 8568
REMARK 3 CHIRALITY : 0.045 926
REMARK 3 PLANARITY : 0.005 1100
REMARK 3 DIHEDRAL : 15.016 3672
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN B AND ( RESID 4:379 OR RESID 401:407 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 91.8953 171.9136 -45.0195
REMARK 3 T TENSOR
REMARK 3 T11: 0.2289 T22: 0.1953
REMARK 3 T33: 0.2788 T12: -0.0177
REMARK 3 T13: -0.0141 T23: 0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 1.3957 L22: 1.3588
REMARK 3 L33: 1.0540 L12: -0.1855
REMARK 3 L13: -0.4414 L23: -0.2212
REMARK 3 S TENSOR
REMARK 3 S11: 0.0091 S12: 0.0472 S13: -0.0541
REMARK 3 S21: -0.0544 S22: -0.0089 S23: -0.1656
REMARK 3 S31: 0.0677 S32: 0.0741 S33: -0.0041
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND ( RESID 4:379 OR RESID 401:407 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 68.0148 164.5460 5.2575
REMARK 3 T TENSOR
REMARK 3 T11: 0.1868 T22: 0.2317
REMARK 3 T33: 0.2913 T12: 0.0078
REMARK 3 T13: -0.0008 T23: 0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 0.9525 L22: 1.2279
REMARK 3 L33: 1.1374 L12: -0.0795
REMARK 3 L13: 0.3168 L23: 0.3205
REMARK 3 S TENSOR
REMARK 3 S11: -0.0102 S12: -0.0497 S13: 0.1918
REMARK 3 S21: 0.0669 S22: -0.0009 S23: 0.0260
REMARK 3 S31: -0.0755 S32: -0.0216 S33: 0.0131
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 501:674 ) OR ( CHAIN B AND RESID
REMARK 3 501:668 )
REMARK 3 ORIGIN FOR THE GROUP (A): 80.1536 168.0364 -19.9279
REMARK 3 T TENSOR
REMARK 3 T11: 0.2149 T22: 0.2339
REMARK 3 T33: 0.3072 T12: 0.0172
REMARK 3 T13: -0.0227 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.2720 L22: 0.0915
REMARK 3 L33: 0.7727 L12: 0.0048
REMARK 3 L13: -0.4565 L23: -0.0093
REMARK 3 S TENSOR
REMARK 3 S11: -0.0025 S12: -0.0293 S13: 0.0225
REMARK 3 S21: -0.0097 S22: -0.0058 S23: -0.0399
REMARK 3 S31: -0.0612 S32: 0.0737 S33: -0.0064
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 6MTW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1000235920.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-OCT-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : DIAMOND (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 0.5.546
REMARK 200 DATA SCALING SOFTWARE : XIA2 0.5.546
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57874
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.999
REMARK 200 RESOLUTION RANGE LOW (A) : 39.340
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.14800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.9400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.52500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.460
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: 4X90
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CACODYLATE PH 5.6, 6%
REMARK 280 ISOPROPANOL, 250 MM ZINC ACETATE, 2 MM 1-HYDROXY-2-AZELAOYL-SN-
REMARK 280 GLYCERO-3-PHOSPHOCHOLINE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 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 42.28350
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.41239
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 107.24800
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 42.28350
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 24.41239
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 107.24800
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 42.28350
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 24.41239
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 107.24800
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 48.82478
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 214.49600
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 48.82478
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 214.49600
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 48.82478
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 214.49600
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 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 618 LIES ON A SPECIAL POSITION.
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 0
REMARK 465 ALA A 1
REMARK 465 GLY A 2
REMARK 465 ARG A 3
REMARK 465 GLY B 0
REMARK 465 ALA B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
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 A 308 O HOH A 501 2.11
REMARK 500 OG SER B 308 O HOH B 501 2.13
REMARK 500 OD2 ASP A 23 O HOH A 502 2.19
REMARK 500 O HOH B 636 O HOH B 658 2.19
REMARK 500 OH TYR A 39 OD2 ASP A 79 2.19
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 ASP A 23 57.09 -150.71
REMARK 500 SER A 38 -159.59 -145.13
REMARK 500 LYS A 87 -167.86 -114.14
REMARK 500 TYR A 104 -85.74 -125.57
REMARK 500 GLU A 121 -96.11 -109.76
REMARK 500 SER A 165 -130.93 52.61
REMARK 500 PHE A 271 73.91 -150.53
REMARK 500 THR A 329 -50.06 -131.99
REMARK 500 ASP B 23 56.48 -149.55
REMARK 500 LYS B 87 -168.11 -113.98
REMARK 500 TYR B 104 -85.98 -124.97
REMARK 500 GLU B 121 -95.63 -109.69
REMARK 500 SER B 165 -131.03 53.12
REMARK 500 PHE B 271 74.83 -150.13
REMARK 500 THR B 329 -50.46 -131.38
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 404 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 165 OG
REMARK 620 2 HIS A 359 NE2 116.3
REMARK 620 3 HOH A 647 O 99.1 106.8
REMARK 620 4 HOH A 594 O 109.5 104.7 121.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 406 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 307 OD1
REMARK 620 2 CYS A 322 SG 110.8
REMARK 620 3 HOH A 501 O 99.1 81.9
REMARK 620 4 GLU A 110 OE2 46.4 83.7 132.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 405 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 322 SG
REMARK 620 2 HOH A 671 O 112.4
REMARK 620 3 HOH A 659 O 92.8 150.6
REMARK 620 4 HOH A 664 O 116.0 94.6 59.5
REMARK 620 5 HIS A 106 NE2 8.2 120.6 84.8 112.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 404 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 165 OG
REMARK 620 2 HIS B 359 NE2 115.4
REMARK 620 3 HOH B 605 O 113.3 107.0
REMARK 620 4 HOH B 641 O 102.5 104.8 113.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 406 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 307 OD1
REMARK 620 2 CYS B 322 SG 111.3
REMARK 620 3 HOH B 501 O 91.4 90.1
REMARK 620 4 GLU B 110 OE2 47.1 84.7 131.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 405 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 322 SG
REMARK 620 2 HOH B 658 O 114.2
REMARK 620 3 HOH B 667 O 110.8 105.6
REMARK 620 4 HIS B 106 NE2 7.5 109.8 118.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 407 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 671 O
REMARK 620 2 HOH A 652 O 107.7
REMARK 620 3 HOH A 661 O 140.9 95.0
REMARK 620 4 HOH A 501 O 86.1 126.0 106.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 407 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 501 O
REMARK 620 2 HOH B 667 O 93.9
REMARK 620 3 HOH B 652 O 106.1 146.5
REMARK 620 4 HOH B 653 O 115.4 95.8 99.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 401 bound
REMARK 800 to ASN A 66
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 402 bound
REMARK 800 to ASN A 365
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 401 bound
REMARK 800 to ASN B 66
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 402 bound
REMARK 800 to ASN B 365
DBREF 6MTW A 1 379 UNP Q8NCC3 PAG15_HUMAN 34 412
DBREF 6MTW B 1 379 UNP Q8NCC3 PAG15_HUMAN 34 412
SEQADV 6MTW GLY A 0 UNP Q8NCC3 EXPRESSION TAG
SEQADV 6MTW GLY B 0 UNP Q8NCC3 EXPRESSION TAG
SEQRES 1 A 380 GLY ALA GLY ARG HIS PRO PRO VAL VAL LEU VAL PRO GLY
SEQRES 2 A 380 ASP LEU GLY ASN GLN LEU GLU ALA LYS LEU ASP LYS PRO
SEQRES 3 A 380 THR VAL VAL HIS TYR LEU CYS SER LYS LYS THR GLU SER
SEQRES 4 A 380 TYR PHE THR ILE TRP LEU ASN LEU GLU LEU LEU LEU PRO
SEQRES 5 A 380 VAL ILE ILE ASP CYS TRP ILE ASP ASN ILE ARG LEU VAL
SEQRES 6 A 380 TYR ASN LYS THR SER ARG ALA THR GLN PHE PRO ASP GLY
SEQRES 7 A 380 VAL ASP VAL ARG VAL PRO GLY PHE GLY LYS THR PHE SER
SEQRES 8 A 380 LEU GLU PHE LEU ASP PRO SER LYS SER SER VAL GLY SER
SEQRES 9 A 380 TYR PHE HIS THR MET VAL GLU SER LEU VAL GLY TRP GLY
SEQRES 10 A 380 TYR THR ARG GLY GLU ASP VAL ARG GLY ALA PRO TYR ASP
SEQRES 11 A 380 TRP ARG ARG ALA PRO ASN GLU ASN GLY PRO TYR PHE LEU
SEQRES 12 A 380 ALA LEU ARG GLU MET ILE GLU GLU MET TYR GLN LEU TYR
SEQRES 13 A 380 GLY GLY PRO VAL VAL LEU VAL ALA HIS SER MET GLY ASN
SEQRES 14 A 380 MET TYR THR LEU TYR PHE LEU GLN ARG GLN PRO GLN ALA
SEQRES 15 A 380 TRP LYS ASP LYS TYR ILE ARG ALA PHE VAL SER LEU GLY
SEQRES 16 A 380 ALA PRO TRP GLY GLY VAL ALA LYS THR LEU ARG VAL LEU
SEQRES 17 A 380 ALA SER GLY ASP ASN ASN ARG ILE PRO VAL ILE GLY PRO
SEQRES 18 A 380 LEU LYS ILE ARG GLU GLN GLN ARG SER ALA VAL SER THR
SEQRES 19 A 380 SER TRP LEU LEU PRO TYR ASN TYR THR TRP SER PRO GLU
SEQRES 20 A 380 LYS VAL PHE VAL GLN THR PRO THR ILE ASN TYR THR LEU
SEQRES 21 A 380 ARG ASP TYR ARG LYS PHE PHE GLN ASP ILE GLY PHE GLU
SEQRES 22 A 380 ASP GLY TRP LEU MET ARG GLN ASP THR GLU GLY LEU VAL
SEQRES 23 A 380 GLU ALA THR MET PRO PRO GLY VAL GLN LEU HIS CYS LEU
SEQRES 24 A 380 TYR GLY THR GLY VAL PRO THR PRO ASP SER PHE TYR TYR
SEQRES 25 A 380 GLU SER PHE PRO ASP ARG ASP PRO LYS ILE CYS PHE GLY
SEQRES 26 A 380 ASP GLY ASP GLY THR VAL ASN LEU LYS SER ALA LEU GLN
SEQRES 27 A 380 CYS GLN ALA TRP GLN SER ARG GLN GLU HIS GLN VAL LEU
SEQRES 28 A 380 LEU GLN GLU LEU PRO GLY SER GLU HIS ILE GLU MET LEU
SEQRES 29 A 380 ALA ASN ALA THR THR LEU ALA TYR LEU LYS ARG VAL LEU
SEQRES 30 A 380 LEU GLY PRO
SEQRES 1 B 380 GLY ALA GLY ARG HIS PRO PRO VAL VAL LEU VAL PRO GLY
SEQRES 2 B 380 ASP LEU GLY ASN GLN LEU GLU ALA LYS LEU ASP LYS PRO
SEQRES 3 B 380 THR VAL VAL HIS TYR LEU CYS SER LYS LYS THR GLU SER
SEQRES 4 B 380 TYR PHE THR ILE TRP LEU ASN LEU GLU LEU LEU LEU PRO
SEQRES 5 B 380 VAL ILE ILE ASP CYS TRP ILE ASP ASN ILE ARG LEU VAL
SEQRES 6 B 380 TYR ASN LYS THR SER ARG ALA THR GLN PHE PRO ASP GLY
SEQRES 7 B 380 VAL ASP VAL ARG VAL PRO GLY PHE GLY LYS THR PHE SER
SEQRES 8 B 380 LEU GLU PHE LEU ASP PRO SER LYS SER SER VAL GLY SER
SEQRES 9 B 380 TYR PHE HIS THR MET VAL GLU SER LEU VAL GLY TRP GLY
SEQRES 10 B 380 TYR THR ARG GLY GLU ASP VAL ARG GLY ALA PRO TYR ASP
SEQRES 11 B 380 TRP ARG ARG ALA PRO ASN GLU ASN GLY PRO TYR PHE LEU
SEQRES 12 B 380 ALA LEU ARG GLU MET ILE GLU GLU MET TYR GLN LEU TYR
SEQRES 13 B 380 GLY GLY PRO VAL VAL LEU VAL ALA HIS SER MET GLY ASN
SEQRES 14 B 380 MET TYR THR LEU TYR PHE LEU GLN ARG GLN PRO GLN ALA
SEQRES 15 B 380 TRP LYS ASP LYS TYR ILE ARG ALA PHE VAL SER LEU GLY
SEQRES 16 B 380 ALA PRO TRP GLY GLY VAL ALA LYS THR LEU ARG VAL LEU
SEQRES 17 B 380 ALA SER GLY ASP ASN ASN ARG ILE PRO VAL ILE GLY PRO
SEQRES 18 B 380 LEU LYS ILE ARG GLU GLN GLN ARG SER ALA VAL SER THR
SEQRES 19 B 380 SER TRP LEU LEU PRO TYR ASN TYR THR TRP SER PRO GLU
SEQRES 20 B 380 LYS VAL PHE VAL GLN THR PRO THR ILE ASN TYR THR LEU
SEQRES 21 B 380 ARG ASP TYR ARG LYS PHE PHE GLN ASP ILE GLY PHE GLU
SEQRES 22 B 380 ASP GLY TRP LEU MET ARG GLN ASP THR GLU GLY LEU VAL
SEQRES 23 B 380 GLU ALA THR MET PRO PRO GLY VAL GLN LEU HIS CYS LEU
SEQRES 24 B 380 TYR GLY THR GLY VAL PRO THR PRO ASP SER PHE TYR TYR
SEQRES 25 B 380 GLU SER PHE PRO ASP ARG ASP PRO LYS ILE CYS PHE GLY
SEQRES 26 B 380 ASP GLY ASP GLY THR VAL ASN LEU LYS SER ALA LEU GLN
SEQRES 27 B 380 CYS GLN ALA TRP GLN SER ARG GLN GLU HIS GLN VAL LEU
SEQRES 28 B 380 LEU GLN GLU LEU PRO GLY SER GLU HIS ILE GLU MET LEU
SEQRES 29 B 380 ALA ASN ALA THR THR LEU ALA TYR LEU LYS ARG VAL LEU
SEQRES 30 B 380 LEU GLY PRO
HET NAG A 401 14
HET NAG A 402 14
HET CL A 403 1
HET ZN A 404 1
HET ZN A 405 1
HET ZN A 406 1
HET ZN A 407 1
HET NAG B 401 14
HET NAG B 402 14
HET CL B 403 1
HET ZN B 404 1
HET ZN B 405 1
HET ZN B 406 1
HET ZN B 407 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM CL CHLORIDE ION
HETNAM ZN ZINC ION
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 5 CL 2(CL 1-)
FORMUL 6 ZN 8(ZN 2+)
FORMUL 17 HOH *342(H2 O)
HELIX 1 AA1 ASN A 45 LEU A 50 5 6
HELIX 2 AA2 ILE A 53 ARG A 62 1 10
HELIX 3 AA3 THR A 88 PHE A 93 1 6
HELIX 4 AA4 PHE A 105 TRP A 115 1 11
HELIX 5 AA5 ALA A 133 GLU A 136 5 4
HELIX 6 AA6 ASN A 137 GLY A 156 1 20
HELIX 7 AA7 MET A 166 GLN A 178 1 13
HELIX 8 AA8 PRO A 179 TYR A 186 1 8
HELIX 9 AA9 ALA A 201 GLY A 210 1 10
HELIX 10 AB1 GLY A 219 ALA A 230 1 12
HELIX 11 AB2 ALA A 230 LEU A 236 1 7
HELIX 12 AB3 THR A 258 ARG A 260 5 3
HELIX 13 AB4 ASP A 261 ILE A 269 1 9
HELIX 14 AB5 GLU A 272 GLU A 282 1 11
HELIX 15 AB6 ASN A 331 LYS A 333 5 3
HELIX 16 AB7 SER A 334 TRP A 341 1 8
HELIX 17 AB8 GLN A 342 GLN A 345 5 4
HELIX 18 AB9 ILE A 360 ALA A 364 5 5
HELIX 19 AC1 ASN A 365 GLY A 378 1 14
HELIX 20 AC2 ASN B 45 LEU B 50 5 6
HELIX 21 AC3 ILE B 53 ARG B 62 1 10
HELIX 22 AC4 THR B 88 PHE B 93 1 6
HELIX 23 AC5 PHE B 105 TRP B 115 1 11
HELIX 24 AC6 ALA B 133 GLU B 136 5 4
HELIX 25 AC7 ASN B 137 GLY B 156 1 20
HELIX 26 AC8 MET B 166 GLN B 178 1 13
HELIX 27 AC9 PRO B 179 TYR B 186 1 8
HELIX 28 AD1 ALA B 201 GLY B 210 1 10
HELIX 29 AD2 GLY B 219 ALA B 230 1 12
HELIX 30 AD3 ALA B 230 LEU B 236 1 7
HELIX 31 AD4 THR B 258 ARG B 260 5 3
HELIX 32 AD5 ASP B 261 ILE B 269 1 9
HELIX 33 AD6 GLU B 272 GLU B 282 1 11
HELIX 34 AD7 ASN B 331 LYS B 333 5 3
HELIX 35 AD8 SER B 334 TRP B 341 1 8
HELIX 36 AD9 ILE B 360 ALA B 364 5 5
HELIX 37 AE1 ASN B 365 GLY B 378 1 14
SHEET 1 AA1 6 VAL A 123 GLY A 125 0
SHEET 2 AA1 6 VAL A 7 VAL A 10 1 N LEU A 9 O ARG A 124
SHEET 3 AA1 6 VAL A 159 HIS A 164 1 O VAL A 162 N VAL A 8
SHEET 4 AA1 6 ILE A 187 LEU A 193 1 O VAL A 191 N LEU A 161
SHEET 5 AA1 6 LEU A 295 THR A 301 1 O HIS A 296 N SER A 192
SHEET 6 AA1 6 VAL A 349 PRO A 355 1 O LEU A 350 N LEU A 295
SHEET 1 AA2 3 PHE A 40 TRP A 43 0
SHEET 2 AA2 3 LEU A 18 LEU A 22 -1 N ALA A 20 O PHE A 40
SHEET 3 AA2 3 VAL A 78 ARG A 81 -1 O ASP A 79 N LYS A 21
SHEET 1 AA3 2 VAL A 64 ASN A 66 0
SHEET 2 AA3 2 ALA A 71 GLN A 73 -1 O GLN A 73 N VAL A 64
SHEET 1 AA4 4 ASN A 256 TYR A 257 0
SHEET 2 AA4 4 VAL A 250 GLN A 251 -1 N VAL A 250 O TYR A 257
SHEET 3 AA4 4 THR A 305 TYR A 310 1 O PHE A 309 N GLN A 251
SHEET 4 AA4 4 LYS A 320 GLY A 324 -1 O GLY A 324 N THR A 305
SHEET 1 AA5 6 VAL B 123 GLY B 125 0
SHEET 2 AA5 6 VAL B 7 VAL B 10 1 N LEU B 9 O ARG B 124
SHEET 3 AA5 6 VAL B 159 HIS B 164 1 O VAL B 162 N VAL B 10
SHEET 4 AA5 6 ILE B 187 LEU B 193 1 O VAL B 191 N LEU B 161
SHEET 5 AA5 6 LEU B 295 THR B 301 1 O HIS B 296 N SER B 192
SHEET 6 AA5 6 VAL B 349 PRO B 355 1 O LEU B 350 N CYS B 297
SHEET 1 AA6 3 PHE B 40 TRP B 43 0
SHEET 2 AA6 3 LEU B 18 LEU B 22 -1 N ALA B 20 O PHE B 40
SHEET 3 AA6 3 VAL B 78 ARG B 81 -1 O ASP B 79 N LYS B 21
SHEET 1 AA7 2 VAL B 64 ASN B 66 0
SHEET 2 AA7 2 ALA B 71 GLN B 73 -1 O GLN B 73 N VAL B 64
SHEET 1 AA8 4 ASN B 256 TYR B 257 0
SHEET 2 AA8 4 VAL B 250 GLN B 251 -1 N VAL B 250 O TYR B 257
SHEET 3 AA8 4 THR B 305 TYR B 310 1 O PHE B 309 N GLN B 251
SHEET 4 AA8 4 LYS B 320 GLY B 324 -1 O GLY B 324 N THR B 305
SSBOND 1 CYS A 32 CYS A 56 1555 1555 2.03
SSBOND 2 CYS A 297 CYS A 338 1555 1555 2.03
SSBOND 3 CYS B 32 CYS B 56 1555 1555 2.03
SSBOND 4 CYS B 297 CYS B 338 1555 1555 2.03
LINK ND2 ASN A 66 C1 NAG A 401 1555 1555 1.44
LINK OG SER A 165 ZN ZN A 404 1555 1555 1.96
LINK OD1 ASP A 307 ZN ZN A 406 1555 1555 2.06
LINK SG CYS A 322 ZN ZN A 406 1555 1555 2.27
LINK SG CYS A 322 ZN ZN A 405 1555 1555 2.32
LINK NE2 HIS A 359 ZN ZN A 404 1555 1555 2.07
LINK ND2 ASN A 365 C1 NAG A 402 1555 1555 1.43
LINK ND2 ASN B 66 C1 NAG B 401 1555 1555 1.44
LINK OG SER B 165 ZN ZN B 404 1555 1555 1.98
LINK OD1 ASP B 307 ZN ZN B 406 1555 1555 2.09
LINK SG CYS B 322 ZN ZN B 405 1555 1555 2.32
LINK SG CYS B 322 ZN ZN B 406 1555 1555 2.24
LINK NE2 HIS B 359 ZN ZN B 404 1555 1555 2.09
LINK ND2 ASN B 365 C1 NAG B 402 1555 1555 1.43
LINK ZN ZN A 404 O HOH A 647 1555 1555 2.32
LINK ZN ZN A 404 O HOH A 594 1555 1555 2.01
LINK ZN ZN A 405 O HOH A 671 1555 1555 1.92
LINK ZN ZN A 405 O HOH A 659 1555 1555 2.59
LINK ZN ZN A 405 O HOH A 664 1555 1555 1.93
LINK ZN ZN A 406 O HOH A 501 1555 1555 2.18
LINK ZN ZN A 407 O HOH A 671 1555 1555 1.98
LINK ZN ZN A 407 O HOH A 652 1555 1555 2.13
LINK ZN ZN A 407 O HOH A 661 1555 1555 2.01
LINK ZN ZN A 407 O HOH A 501 1555 1555 1.92
LINK ZN ZN B 404 O HOH B 605 1555 1555 1.94
LINK ZN ZN B 404 O HOH B 641 1555 1555 2.30
LINK ZN ZN B 405 O HOH B 658 1555 1555 1.94
LINK ZN ZN B 405 O HOH B 667 1555 1555 1.91
LINK ZN ZN B 406 O HOH B 501 1555 1555 2.00
LINK ZN ZN B 407 O HOH B 501 1555 1555 1.95
LINK ZN ZN B 407 O HOH B 667 1555 1555 2.00
LINK ZN ZN B 407 O HOH B 652 1555 1555 2.02
LINK ZN ZN B 407 O HOH B 653 1555 1555 2.05
LINK NE2 HIS A 106 ZN ZN A 405 1555 3695 2.07
LINK OE2 GLU A 110 ZN ZN A 406 1555 3695 2.02
LINK NE2 HIS B 106 ZN ZN B 405 1555 2975 2.10
LINK OE2 GLU B 110 ZN ZN B 406 1555 2975 2.08
CISPEP 1 TRP A 43 LEU A 44 0 -6.34
CISPEP 2 PHE A 314 PRO A 315 0 -4.13
CISPEP 3 TRP B 43 LEU B 44 0 -6.01
CISPEP 4 PHE B 314 PRO B 315 0 -3.86
SITE 1 AC1 3 GLN A 294 HIS A 347 GLN A 348
SITE 1 AC2 5 ASP A 13 SER A 165 HIS A 359 HOH A 594
SITE 2 AC2 5 HOH A 647
SITE 1 AC3 8 CYS A 322 ZN A 406 ZN A 407 HOH A 501
SITE 2 AC3 8 HOH A 659 HOH A 664 HOH A 671 HOH A 673
SITE 1 AC4 6 ASP A 307 SER A 308 CYS A 322 ZN A 405
SITE 2 AC4 6 ZN A 407 HOH A 501
SITE 1 AC5 7 SER A 308 ZN A 405 ZN A 406 HOH A 501
SITE 2 AC5 7 HOH A 652 HOH A 661 HOH A 671
SITE 1 AC6 3 GLN B 294 HIS B 347 GLN B 348
SITE 1 AC7 5 ASP B 13 SER B 165 HIS B 359 HOH B 605
SITE 2 AC7 5 HOH B 641
SITE 1 AC8 6 CYS B 322 ZN B 406 ZN B 407 HOH B 636
SITE 2 AC8 6 HOH B 658 HOH B 667
SITE 1 AC9 6 ASP B 307 SER B 308 CYS B 322 ZN B 405
SITE 2 AC9 6 ZN B 407 HOH B 501
SITE 1 AD1 7 SER B 308 ZN B 405 ZN B 406 HOH B 501
SITE 2 AD1 7 HOH B 652 HOH B 653 HOH B 667
SITE 1 AD2 4 ASN A 66 GLN A 73 HOH A 504 HOH A 628
SITE 1 AD3 8 LEU A 354 PRO A 355 SER A 357 ASN A 365
SITE 2 AD3 8 THR A 367 HOH A 574 HOH A 610 HOH A 626
SITE 1 AD4 4 ASN B 66 GLN B 73 HOH B 504 HOH B 579
SITE 1 AD5 5 LEU B 354 PRO B 355 ASN B 365 THR B 367
SITE 2 AD5 5 HOH B 545
CRYST1 84.567 84.567 321.744 90.00 90.00 120.00 H 3 18
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 0.011825 0.006827 0.000000 0.00000
SCALE2 0.000000 0.013654 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003108 0.00000
TER 3020 PRO A 379
TER 6040 PRO B 379
MASTER 491 0 14 37 30 0 24 6 6446 2 99 60
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