HEADER CELL ADHESION 18-SEP-09 3JXA
TITLE IMMUNOGLOBULIN DOMAINS 1-4 OF MOUSE CNTN4
CAVEAT 3JXA NAG A 2 HAS WRONG CHIRALITY AT ATOM C1 NAG A 4 HAS WRONG
CAVEAT 2 3JXA CHIRALITY AT ATOM C1 NAG B 5 HAS WRONG CHIRALITY AT ATOM C1
CAVEAT 3 3JXA NAG B 8 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONTACTIN 4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: IG 1-4 FRAGMENT (UNP RESIDUES 25-404);
COMPND 5 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: CNTN4;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSGHP1
KEYWDS IMMUNOGLOBULIN-LIKE DOMAINS, HORSESHOE-LIKE CONFORMATION, IMMUNE
KEYWDS 2 SYSTEM, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BOUYAIN
REVDAT 5 29-JUL-20 3JXA 1 CAVEAT COMPND REMARK SEQADV
REVDAT 5 2 1 HET HETNAM FORMUL LINK
REVDAT 5 3 1 SITE ATOM
REVDAT 4 01-NOV-17 3JXA 1 REMARK
REVDAT 3 13-JUL-11 3JXA 1 VERSN
REVDAT 2 16-FEB-10 3JXA 1 JRNL
REVDAT 1 22-DEC-09 3JXA 0
JRNL AUTH S.BOUYAIN,D.J.WATKINS
JRNL TITL THE PROTEIN TYROSINE PHOSPHATASES PTPRZ AND PTPRG BIND TO
JRNL TITL 2 DISTINCT MEMBERS OF THE CONTACTIN FAMILY OF NEURAL
JRNL TITL 3 RECOGNITION MOLECULES.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 2443 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 20133774
JRNL DOI 10.1073/PNAS.0911235107
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.070
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 3 NUMBER OF REFLECTIONS : 37921
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 1886
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 37.1766 - 5.6441 0.99 3185 167 0.1743 0.2146
REMARK 3 2 5.6441 - 4.4823 1.00 3072 161 0.1453 0.1891
REMARK 3 3 4.4823 - 3.9164 1.00 3070 162 0.1572 0.2340
REMARK 3 4 3.9164 - 3.5586 1.00 3016 158 0.1938 0.2375
REMARK 3 5 3.5586 - 3.3038 0.98 2991 157 0.2095 0.2588
REMARK 3 6 3.3038 - 3.1091 0.97 2927 153 0.2181 0.2832
REMARK 3 7 3.1091 - 2.9534 0.96 2903 154 0.2261 0.2839
REMARK 3 8 2.9534 - 2.8249 0.94 2842 148 0.2306 0.3194
REMARK 3 9 2.8249 - 2.7162 0.92 2711 142 0.2315 0.2803
REMARK 3 10 2.7162 - 2.6225 0.87 2655 135 0.2483 0.3488
REMARK 3 11 2.6225 - 2.5405 0.83 2475 126 0.2514 0.3356
REMARK 3 12 2.5405 - 2.4679 0.75 2274 120 0.2543 0.3047
REMARK 3 13 2.4679 - 2.4030 0.65 1914 103 0.2558 0.3097
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 : 0.29
REMARK 3 B_SOL : 50.89
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.860
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 78.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.45700
REMARK 3 B22 (A**2) : 11.96500
REMARK 3 B33 (A**2) : -11.50800
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.68800
REMARK 3 B23 (A**2) : 0.00000
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 6253
REMARK 3 ANGLE : 0.932 8478
REMARK 3 CHIRALITY : 0.060 941
REMARK 3 PLANARITY : 0.005 1099
REMARK 3 DIHEDRAL : 17.303 2330
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESID 22:64
REMARK 3 ORIGIN FOR THE GROUP (A): 47.1969 2.1194 -10.7233
REMARK 3 T TENSOR
REMARK 3 T11: 0.6307 T22: 1.3646
REMARK 3 T33: 0.3589 T12: 0.3963
REMARK 3 T13: 0.1182 T23: 0.2754
REMARK 3 L TENSOR
REMARK 3 L11: -0.1593 L22: 0.6632
REMARK 3 L33: 2.2275 L12: -0.5756
REMARK 3 L13: -0.8413 L23: 0.6458
REMARK 3 S TENSOR
REMARK 3 S11: 0.3667 S12: 0.0509 S13: 0.4521
REMARK 3 S21: -0.0562 S22: 0.3197 S23: -0.2397
REMARK 3 S31: -0.2384 S32: -1.4982 S33: -0.4248
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 65:118)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.2451 -0.2946 -7.3657
REMARK 3 T TENSOR
REMARK 3 T11: 0.6456 T22: 1.8868
REMARK 3 T33: 0.5064 T12: 0.3537
REMARK 3 T13: 0.1315 T23: 0.3885
REMARK 3 L TENSOR
REMARK 3 L11: 1.1354 L22: 0.5947
REMARK 3 L33: 0.4485 L12: 0.1731
REMARK 3 L13: -1.5201 L23: 0.8509
REMARK 3 S TENSOR
REMARK 3 S11: 0.1474 S12: 0.2683 S13: 0.5702
REMARK 3 S21: 0.2858 S22: 0.2150 S23: 0.5662
REMARK 3 S31: -0.4806 S32: -1.8589 S33: -0.2655
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 119:314)
REMARK 3 ORIGIN FOR THE GROUP (A): 59.4472 -12.6188 26.7324
REMARK 3 T TENSOR
REMARK 3 T11: 0.1987 T22: -0.0099
REMARK 3 T33: 0.1429 T12: 0.0001
REMARK 3 T13: 0.0274 T23: 0.0603
REMARK 3 L TENSOR
REMARK 3 L11: 1.4345 L22: 1.6463
REMARK 3 L33: 2.1373 L12: -0.6093
REMARK 3 L13: -0.9717 L23: 0.1510
REMARK 3 S TENSOR
REMARK 3 S11: 0.1064 S12: 0.3135 S13: 0.1584
REMARK 3 S21: -0.1675 S22: -0.0148 S23: -0.0697
REMARK 3 S31: -0.2483 S32: -0.2325 S33: -0.1153
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 315:403)
REMARK 3 ORIGIN FOR THE GROUP (A): 55.7086 -14.9748 -22.1132
REMARK 3 T TENSOR
REMARK 3 T11: 0.8721 T22: 0.6415
REMARK 3 T33: 0.2359 T12: -0.3236
REMARK 3 T13: -0.1385 T23: 0.1250
REMARK 3 L TENSOR
REMARK 3 L11: 1.2738 L22: 1.5680
REMARK 3 L33: -0.5920 L12: -0.5429
REMARK 3 L13: -0.7034 L23: 0.9829
REMARK 3 S TENSOR
REMARK 3 S11: 0.2014 S12: 0.3992 S13: -0.3212
REMARK 3 S21: -0.8872 S22: 0.1648 S23: 0.2375
REMARK 3 S31: 1.1174 S32: -0.9565 S33: -0.2410
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN B AND RESID 22:119)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.2634 -24.1654 13.9504
REMARK 3 T TENSOR
REMARK 3 T11: 0.4352 T22: 0.6154
REMARK 3 T33: 0.7586 T12: -0.0160
REMARK 3 T13: -0.3405 T23: -0.1091
REMARK 3 L TENSOR
REMARK 3 L11: -0.3483 L22: 0.3557
REMARK 3 L33: 1.6680 L12: 0.0363
REMARK 3 L13: -0.3700 L23: -0.1305
REMARK 3 S TENSOR
REMARK 3 S11: -0.1016 S12: 0.6191 S13: -0.4756
REMARK 3 S21: -0.4652 S22: 0.0842 S23: 0.2931
REMARK 3 S31: 0.1107 S32: -0.1056 S33: -0.0659
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN B AND RESID 120:129)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1196 -11.3519 4.5840
REMARK 3 T TENSOR
REMARK 3 T11: 0.7297 T22: 1.2545
REMARK 3 T33: 1.1477 T12: 0.1044
REMARK 3 T13: -0.2843 T23: 0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 0.1240 L22: 0.2538
REMARK 3 L33: 0.1990 L12: 0.1233
REMARK 3 L13: -0.1562 L23: -0.0598
REMARK 3 S TENSOR
REMARK 3 S11: -0.1132 S12: 0.2970 S13: -0.4660
REMARK 3 S21: -0.1686 S22: 0.5317 S23: 0.3463
REMARK 3 S31: 0.0810 S32: -0.9602 S33: -0.5370
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN B AND RESID 130:312)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4254 5.3463 20.3651
REMARK 3 T TENSOR
REMARK 3 T11: 0.1901 T22: 1.0721
REMARK 3 T33: 0.7544 T12: 0.2424
REMARK 3 T13: -0.1675 T23: -0.1113
REMARK 3 L TENSOR
REMARK 3 L11: 0.4781 L22: 0.6272
REMARK 3 L33: 0.7974 L12: 0.3952
REMARK 3 L13: -0.4552 L23: 0.2301
REMARK 3 S TENSOR
REMARK 3 S11: -0.0370 S12: -0.3749 S13: 0.2784
REMARK 3 S21: 0.0540 S22: 0.1242 S23: 0.2105
REMARK 3 S31: -0.1284 S32: -0.2641 S33: -0.1492
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 313:404)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.2781 -20.8050 36.5824
REMARK 3 T TENSOR
REMARK 3 T11: 0.2261 T22: 0.5158
REMARK 3 T33: 0.4745 T12: -0.0872
REMARK 3 T13: 0.0042 T23: 0.0321
REMARK 3 L TENSOR
REMARK 3 L11: -1.1091 L22: 1.4990
REMARK 3 L33: 3.2432 L12: 0.7178
REMARK 3 L13: 0.7419 L23: 1.0696
REMARK 3 S TENSOR
REMARK 3 S11: 0.2310 S12: -0.2605 S13: -0.2366
REMARK 3 S21: -0.0608 S22: -0.2228 S23: 0.5057
REMARK 3 S31: 0.2971 S32: -1.0281 S33: -0.0130
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 3JXA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-SEP-09.
REMARK 100 THE DEPOSITION ID IS D_1000055275.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAR-09; 11-APR-09
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; APS
REMARK 200 BEAMLINE : 22-ID; 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00; 1.00
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK MONOCHROMATOR;
REMARK 200 ROSENBAUM-ROCK MONOCHROMATOR
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD; MARMOSAIC
REMARK 200 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, DPS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40236
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 9.200
REMARK 200 R MERGE (I) : 0.13600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.54800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM NA/K PHOSPHATE PH 5.8, 10% PEG
REMARK 280 3400, 1.2 M 1,6-HEXANEDIOL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 140.86400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.21550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 140.86400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.21550
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 OH TYR B 162 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 SER A 41
REMARK 465 GLU A 42
REMARK 465 GLU A 43
REMARK 465 LYS A 44
REMARK 465 GLU A 404
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 ND2 ASN B 90 C2 NAG B 6 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 CZ TYR B 162 OH TYR B 162 2555 1.38
REMARK 500 CZ TYR B 162 CZ TYR B 162 2555 2.11
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 LEU A 39 52.81 -102.68
REMARK 500 CYS A 50 111.98 -174.91
REMARK 500 ASN A 65 -3.19 57.82
REMARK 500 MET A 73 112.91 -174.19
REMARK 500 PHE A 75 -150.52 -172.60
REMARK 500 ALA A 95 43.25 -92.34
REMARK 500 ASN A 104 -159.21 -135.34
REMARK 500 GLU A 161 -6.11 79.11
REMARK 500 ASP A 167 -167.02 -170.08
REMARK 500 ARG A 359 -132.83 -141.94
REMARK 500 ARG A 361 33.40 -91.59
REMARK 500 GLN A 366 -115.81 61.91
REMARK 500 ALA A 379 130.21 -39.10
REMARK 500 LYS A 389 -7.87 -59.38
REMARK 500 ASP B 40 59.03 -101.17
REMARK 500 CYS B 50 95.32 -162.01
REMARK 500 ASP B 74 132.05 -171.78
REMARK 500 PHE B 75 -151.10 -158.18
REMARK 500 ASN B 88 65.18 66.72
REMARK 500 LEU B 121 111.37 -160.82
REMARK 500 LYS B 125 -71.49 -61.19
REMARK 500 PRO B 232 158.60 -45.20
REMARK 500 THR B 241 -179.17 -68.76
REMARK 500 CYS B 247 118.13 -160.97
REMARK 500 ALA B 262 5.45 -62.02
REMARK 500 ARG B 269 -31.41 81.70
REMARK 500 ASN B 284 72.67 49.03
REMARK 500 ASN B 299 -140.96 -142.68
REMARK 500 ASN B 304 128.71 -170.70
REMARK 500 GLU B 330 -0.86 79.52
REMARK 500 ARG B 359 -158.14 -162.38
REMARK 500 ARG B 361 -26.46 77.31
REMARK 500 GLN B 366 -123.41 63.26
REMARK 500 ALA B 403 170.34 -49.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3JXF RELATED DB: PDB
REMARK 900 RELATED ID: 3JXG RELATED DB: PDB
REMARK 900 RELATED ID: 3JXH RELATED DB: PDB
DBREF 3JXA A 25 404 UNP Q14BL8 Q14BL8_MOUSE 25 404
DBREF 3JXA B 25 404 UNP Q14BL8 Q14BL8_MOUSE 25 404
SEQADV 3JXA PRO A 22 UNP Q14BL8 EXPRESSION TAG
SEQADV 3JXA GLY A 23 UNP Q14BL8 EXPRESSION TAG
SEQADV 3JXA SER A 24 UNP Q14BL8 EXPRESSION TAG
SEQADV 3JXA PRO B 22 UNP Q14BL8 EXPRESSION TAG
SEQADV 3JXA GLY B 23 UNP Q14BL8 EXPRESSION TAG
SEQADV 3JXA SER B 24 UNP Q14BL8 EXPRESSION TAG
SEQRES 1 A 383 PRO GLY SER GLY PRO VAL PHE VAL GLN GLU PRO SER HIS
SEQRES 2 A 383 VAL MET PHE PRO LEU ASP SER GLU GLU LYS LYS VAL LYS
SEQRES 3 A 383 LEU SER CYS GLU VAL LYS GLY ASN PRO LYS PRO HIS ILE
SEQRES 4 A 383 ARG TRP LYS LEU ASN GLY THR ASP VAL ASP ILE GLY MET
SEQRES 5 A 383 ASP PHE ARG TYR SER VAL VAL ASP GLY SER LEU LEU ILE
SEQRES 6 A 383 ASN ASN PRO ASN LYS THR GLN ASP ALA GLY THR TYR GLN
SEQRES 7 A 383 CYS ILE ALA THR ASN SER PHE GLY THR ILE VAL SER ARG
SEQRES 8 A 383 GLU ALA LYS LEU GLN PHE ALA TYR LEU GLU ASN PHE LYS
SEQRES 9 A 383 THR ARG THR ARG SER THR VAL SER VAL ARG ARG GLY GLN
SEQRES 10 A 383 GLY MET VAL LEU LEU CYS GLY PRO PRO PRO HIS SER GLY
SEQRES 11 A 383 GLU LEU SER TYR ALA TRP ILE PHE ASN GLU TYR PRO SER
SEQRES 12 A 383 TYR GLN ASP ASN ARG ARG PHE VAL SER GLN GLU THR GLY
SEQRES 13 A 383 ASN LEU TYR ILE ALA LYS VAL GLU LYS SER ASP VAL GLY
SEQRES 14 A 383 ASN TYR THR CYS VAL VAL THR ASN THR VAL THR ASN HIS
SEQRES 15 A 383 LYS VAL LEU GLY PRO PRO THR PRO LEU ILE LEU ARG ASN
SEQRES 16 A 383 ASP GLY VAL MET GLY GLU TYR GLU PRO LYS ILE GLU VAL
SEQRES 17 A 383 GLN PHE PRO GLU THR VAL PRO ALA GLU LYS GLY THR THR
SEQRES 18 A 383 VAL LYS LEU GLU CYS PHE ALA LEU GLY ASN PRO VAL PRO
SEQRES 19 A 383 THR ILE LEU TRP ARG ARG ALA ASP GLY LYS PRO ILE ALA
SEQRES 20 A 383 ARG LYS ALA ARG ARG HIS LYS SER ASN GLY ILE LEU GLU
SEQRES 21 A 383 ILE PRO ASN PHE GLN GLN GLU ASP ALA GLY SER TYR GLU
SEQRES 22 A 383 CYS VAL ALA GLU ASN SER ARG GLY LYS ASN VAL ALA LYS
SEQRES 23 A 383 GLY GLN LEU THR PHE TYR ALA GLN PRO ASN TRP VAL GLN
SEQRES 24 A 383 ILE ILE ASN ASP ILE HIS VAL ALA MET GLU GLU SER VAL
SEQRES 25 A 383 PHE TRP GLU CYS LYS ALA ASN GLY ARG PRO LYS PRO THR
SEQRES 26 A 383 TYR ARG TRP LEU LYS ASN GLY ASP PRO LEU LEU THR ARG
SEQRES 27 A 383 ASP ARG ILE GLN ILE GLU GLN GLY THR LEU ASN ILE THR
SEQRES 28 A 383 ILE VAL ASN LEU SER ASP ALA GLY MET TYR GLN CYS VAL
SEQRES 29 A 383 ALA GLU ASN LYS HIS GLY VAL ILE PHE SER SER ALA GLU
SEQRES 30 A 383 LEU SER VAL ILE ALA GLU
SEQRES 1 B 383 PRO GLY SER GLY PRO VAL PHE VAL GLN GLU PRO SER HIS
SEQRES 2 B 383 VAL MET PHE PRO LEU ASP SER GLU GLU LYS LYS VAL LYS
SEQRES 3 B 383 LEU SER CYS GLU VAL LYS GLY ASN PRO LYS PRO HIS ILE
SEQRES 4 B 383 ARG TRP LYS LEU ASN GLY THR ASP VAL ASP ILE GLY MET
SEQRES 5 B 383 ASP PHE ARG TYR SER VAL VAL ASP GLY SER LEU LEU ILE
SEQRES 6 B 383 ASN ASN PRO ASN LYS THR GLN ASP ALA GLY THR TYR GLN
SEQRES 7 B 383 CYS ILE ALA THR ASN SER PHE GLY THR ILE VAL SER ARG
SEQRES 8 B 383 GLU ALA LYS LEU GLN PHE ALA TYR LEU GLU ASN PHE LYS
SEQRES 9 B 383 THR ARG THR ARG SER THR VAL SER VAL ARG ARG GLY GLN
SEQRES 10 B 383 GLY MET VAL LEU LEU CYS GLY PRO PRO PRO HIS SER GLY
SEQRES 11 B 383 GLU LEU SER TYR ALA TRP ILE PHE ASN GLU TYR PRO SER
SEQRES 12 B 383 TYR GLN ASP ASN ARG ARG PHE VAL SER GLN GLU THR GLY
SEQRES 13 B 383 ASN LEU TYR ILE ALA LYS VAL GLU LYS SER ASP VAL GLY
SEQRES 14 B 383 ASN TYR THR CYS VAL VAL THR ASN THR VAL THR ASN HIS
SEQRES 15 B 383 LYS VAL LEU GLY PRO PRO THR PRO LEU ILE LEU ARG ASN
SEQRES 16 B 383 ASP GLY VAL MET GLY GLU TYR GLU PRO LYS ILE GLU VAL
SEQRES 17 B 383 GLN PHE PRO GLU THR VAL PRO ALA GLU LYS GLY THR THR
SEQRES 18 B 383 VAL LYS LEU GLU CYS PHE ALA LEU GLY ASN PRO VAL PRO
SEQRES 19 B 383 THR ILE LEU TRP ARG ARG ALA ASP GLY LYS PRO ILE ALA
SEQRES 20 B 383 ARG LYS ALA ARG ARG HIS LYS SER ASN GLY ILE LEU GLU
SEQRES 21 B 383 ILE PRO ASN PHE GLN GLN GLU ASP ALA GLY SER TYR GLU
SEQRES 22 B 383 CYS VAL ALA GLU ASN SER ARG GLY LYS ASN VAL ALA LYS
SEQRES 23 B 383 GLY GLN LEU THR PHE TYR ALA GLN PRO ASN TRP VAL GLN
SEQRES 24 B 383 ILE ILE ASN ASP ILE HIS VAL ALA MET GLU GLU SER VAL
SEQRES 25 B 383 PHE TRP GLU CYS LYS ALA ASN GLY ARG PRO LYS PRO THR
SEQRES 26 B 383 TYR ARG TRP LEU LYS ASN GLY ASP PRO LEU LEU THR ARG
SEQRES 27 B 383 ASP ARG ILE GLN ILE GLU GLN GLY THR LEU ASN ILE THR
SEQRES 28 B 383 ILE VAL ASN LEU SER ASP ALA GLY MET TYR GLN CYS VAL
SEQRES 29 B 383 ALA GLU ASN LYS HIS GLY VAL ILE PHE SER SER ALA GLU
SEQRES 30 B 383 LEU SER VAL ILE ALA GLU
MODRES 3JXA ASN A 65 ASN GLYCOSYLATION SITE
MODRES 3JXA ASN A 191 ASN GLYCOSYLATION SITE
MODRES 3JXA ASN B 65 ASN GLYCOSYLATION SITE
MODRES 3JXA ASN B 90 ASN GLYCOSYLATION SITE
MODRES 3JXA ASN B 191 ASN GLYCOSYLATION SITE
MODRES 3JXA ASN A 370 ASN GLYCOSYLATION SITE
MODRES 3JXA ASN B 370 ASN GLYCOSYLATION SITE
MODRES 3JXA ASN A 90 ASN GLYCOSYLATION SITE
HET NAG A 1 14
HET NAG A 2 14
HET NAG A 3 14
HET NAG A 4 14
HET NAG B 5 14
HET NAG B 6 14
HET NAG B 7 14
HET NAG B 8 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
FORMUL 3 NAG 8(C8 H15 N O6)
FORMUL 11 HOH *187(H2 O)
HELIX 1 1 ASN A 90 ALA A 95 1 6
HELIX 2 2 GLU A 185 VAL A 189 5 5
HELIX 3 3 GLN A 286 ALA A 290 5 5
HELIX 4 4 ASN B 90 ALA B 95 1 6
HELIX 5 5 GLU B 185 VAL B 189 5 5
HELIX 6 6 GLN B 286 ALA B 290 5 5
HELIX 7 7 ASN B 375 ALA B 379 5 5
SHEET 1 A 2 SER A 24 GLN A 30 0
SHEET 2 A 2 GLU A 51 ASN A 55 -1 O ASN A 55 N SER A 24
SHEET 1 B 4 VAL A 35 PRO A 38 0
SHEET 2 B 4 ALA A 114 LEU A 121 1 O GLN A 117 N PHE A 37
SHEET 3 B 4 THR A 97 ASN A 104 -1 N TYR A 98 O ALA A 114
SHEET 4 B 4 GLY A 107 VAL A 110 -1 O ILE A 109 N ALA A 102
SHEET 1 C 5 THR A 67 ASP A 68 0
SHEET 2 C 5 HIS A 59 LEU A 64 -1 N LEU A 64 O THR A 67
SHEET 3 C 5 THR A 97 ASN A 104 -1 O ILE A 101 N ARG A 61
SHEET 4 C 5 ALA A 114 LEU A 121 -1 O ALA A 114 N TYR A 98
SHEET 5 C 5 HIS A 149 SER A 150 -1 O SER A 150 N TYR A 120
SHEET 1 D 2 LYS A 47 LEU A 48 0
SHEET 2 D 2 LEU A 84 LEU A 85 -1 O LEU A 84 N LEU A 48
SHEET 1 E 5 VAL A 132 VAL A 134 0
SHEET 2 E 5 THR A 210 LEU A 214 1 O PRO A 211 N VAL A 132
SHEET 3 E 5 GLY A 190 ASN A 198 -1 N GLY A 190 O LEU A 212
SHEET 4 E 5 LEU A 153 PHE A 159 -1 N SER A 154 O THR A 197
SHEET 5 E 5 TYR A 162 PRO A 163 -1 O TYR A 162 N PHE A 159
SHEET 1 F 4 VAL A 132 VAL A 134 0
SHEET 2 F 4 THR A 210 LEU A 214 1 O PRO A 211 N VAL A 132
SHEET 3 F 4 GLY A 190 ASN A 198 -1 N GLY A 190 O LEU A 212
SHEET 4 F 4 LYS A 204 LEU A 206 -1 O VAL A 205 N VAL A 196
SHEET 1 G 3 MET A 140 LEU A 142 0
SHEET 2 G 3 LEU A 179 ILE A 181 -1 O LEU A 179 N LEU A 142
SHEET 3 G 3 ARG A 170 VAL A 172 -1 N PHE A 171 O TYR A 180
SHEET 1 H 4 TYR A 223 GLN A 230 0
SHEET 2 H 4 VAL A 243 ASN A 252 -1 O LEU A 250 N LYS A 226
SHEET 3 H 4 ILE A 279 ILE A 282 -1 O ILE A 282 N VAL A 243
SHEET 4 H 4 ARG A 272 HIS A 274 -1 N ARG A 272 O GLU A 281
SHEET 1 I 4 THR A 234 GLU A 238 0
SHEET 2 I 4 GLY A 302 GLN A 320 1 O GLN A 309 N VAL A 235
SHEET 3 I 4 GLY A 291 ASN A 299 -1 N ALA A 297 O ASN A 304
SHEET 4 I 4 THR A 256 ARG A 261 -1 N ARG A 260 O GLU A 294
SHEET 1 J 3 THR A 234 GLU A 238 0
SHEET 2 J 3 GLY A 302 GLN A 320 1 O GLN A 309 N VAL A 235
SHEET 3 J 3 LYS A 338 ARG A 342 -1 O LYS A 338 N GLN A 320
SHEET 1 K 5 ILE A 325 ALA A 328 0
SHEET 2 K 5 GLY A 391 ILE A 402 1 O ILE A 402 N VAL A 327
SHEET 3 K 5 GLY A 380 ASN A 388 -1 N TYR A 382 O ALA A 397
SHEET 4 K 5 THR A 346 LYS A 351 -1 N ARG A 348 O VAL A 385
SHEET 5 K 5 ASP A 354 PRO A 355 -1 O ASP A 354 N LYS A 351
SHEET 1 L 3 VAL A 333 GLU A 336 0
SHEET 2 L 3 THR A 368 ILE A 371 -1 O LEU A 369 N TRP A 335
SHEET 3 L 3 ILE A 362 GLU A 365 -1 N GLN A 363 O ASN A 370
SHEET 1 M 2 SER B 24 GLN B 30 0
SHEET 2 M 2 GLU B 51 ASN B 55 -1 O GLU B 51 N VAL B 29
SHEET 1 N 5 VAL B 35 PRO B 38 0
SHEET 2 N 5 GLY B 107 LEU B 121 1 O GLN B 117 N PHE B 37
SHEET 3 N 5 GLY B 96 ASN B 104 -1 N TYR B 98 O ALA B 114
SHEET 4 N 5 HIS B 59 LEU B 64 -1 N ARG B 61 O ILE B 101
SHEET 5 N 5 THR B 67 ASP B 68 -1 O THR B 67 N LEU B 64
SHEET 1 O 3 VAL B 35 PRO B 38 0
SHEET 2 O 3 GLY B 107 LEU B 121 1 O GLN B 117 N PHE B 37
SHEET 3 O 3 HIS B 149 SER B 150 -1 O SER B 150 N TYR B 120
SHEET 1 P 3 LYS B 45 LEU B 48 0
SHEET 2 P 3 SER B 83 ASN B 87 -1 O LEU B 84 N LEU B 48
SHEET 3 P 3 SER B 78 VAL B 80 -1 N SER B 78 O LEU B 85
SHEET 1 Q 5 VAL B 132 VAL B 134 0
SHEET 2 Q 5 THR B 210 LEU B 214 1 O ILE B 213 N VAL B 134
SHEET 3 Q 5 GLY B 190 ASN B 198 -1 N TYR B 192 O THR B 210
SHEET 4 Q 5 LEU B 153 PHE B 159 -1 N ALA B 156 O VAL B 195
SHEET 5 Q 5 TYR B 162 PRO B 163 -1 O TYR B 162 N PHE B 159
SHEET 1 R 4 VAL B 132 VAL B 134 0
SHEET 2 R 4 THR B 210 LEU B 214 1 O ILE B 213 N VAL B 134
SHEET 3 R 4 GLY B 190 ASN B 198 -1 N TYR B 192 O THR B 210
SHEET 4 R 4 LYS B 204 LEU B 206 -1 O VAL B 205 N VAL B 196
SHEET 1 S 3 MET B 140 LEU B 142 0
SHEET 2 S 3 LEU B 179 ILE B 181 -1 O LEU B 179 N LEU B 142
SHEET 3 S 3 ARG B 170 VAL B 172 -1 N PHE B 171 O TYR B 180
SHEET 1 T 2 TYR B 223 VAL B 229 0
SHEET 2 T 2 PHE B 248 ASN B 252 -1 O PHE B 248 N GLU B 228
SHEET 1 U 4 THR B 234 GLU B 238 0
SHEET 2 U 4 LYS B 303 GLN B 320 1 O GLN B 309 N VAL B 235
SHEET 3 U 4 GLY B 291 GLU B 298 -1 N TYR B 293 O GLY B 308
SHEET 4 U 4 THR B 256 ARG B 261 -1 N LEU B 258 O VAL B 296
SHEET 1 V 3 THR B 234 GLU B 238 0
SHEET 2 V 3 LYS B 303 GLN B 320 1 O GLN B 309 N VAL B 235
SHEET 3 V 3 LYS B 338 ARG B 342 -1 O LYS B 338 N VAL B 319
SHEET 1 W 3 VAL B 243 GLU B 246 0
SHEET 2 W 3 ILE B 279 ILE B 282 -1 O LEU B 280 N LEU B 245
SHEET 3 W 3 ARG B 272 HIS B 274 -1 N ARG B 272 O GLU B 281
SHEET 1 X 5 ILE B 325 VAL B 327 0
SHEET 2 X 5 GLY B 391 VAL B 401 1 O SER B 400 N ILE B 325
SHEET 3 X 5 GLY B 380 ASN B 388 -1 N TYR B 382 O ALA B 397
SHEET 4 X 5 THR B 346 LYS B 351 -1 N ARG B 348 O VAL B 385
SHEET 5 X 5 ASP B 354 PRO B 355 -1 O ASP B 354 N LYS B 351
SHEET 1 Y 3 VAL B 333 GLU B 336 0
SHEET 2 Y 3 THR B 368 ILE B 371 -1 O ILE B 371 N VAL B 333
SHEET 3 Y 3 ILE B 362 GLU B 365 -1 N GLN B 363 O ASN B 370
SSBOND 1 CYS A 50 CYS A 100 1555 1555 2.04
SSBOND 2 CYS A 144 CYS A 194 1555 1555 2.06
SSBOND 3 CYS A 247 CYS A 295 1555 1555 2.04
SSBOND 4 CYS A 337 CYS A 384 1555 1555 2.04
SSBOND 5 CYS B 50 CYS B 100 1555 1555 2.03
SSBOND 6 CYS B 144 CYS B 194 1555 1555 2.04
SSBOND 7 CYS B 247 CYS B 295 1555 1555 2.03
SSBOND 8 CYS B 337 CYS B 384 1555 1555 2.03
LINK C1 NAG A 1 ND2 ASN A 65 1555 1555 1.45
LINK C1 NAG A 2 ND2 ASN A 90 1555 1555 1.44
LINK C1 NAG A 3 ND2 ASN A 191 1555 1555 1.45
LINK C1 NAG A 4 ND2 ASN A 370 1555 1555 1.44
LINK C1 NAG B 5 ND2 ASN B 65 1555 1555 1.45
LINK C1 NAG B 6 ND2 ASN B 90 1555 1555 1.44
LINK C1 NAG B 7 ND2 ASN B 191 1555 1555 1.44
LINK C1 NAG B 8 ND2 ASN B 370 1555 1555 1.44
CISPEP 1 ASN A 55 PRO A 56 0 3.29
CISPEP 2 MET A 73 ASP A 74 0 4.19
CISPEP 3 ASN A 252 PRO A 253 0 5.14
CISPEP 4 ARG A 342 PRO A 343 0 -2.09
CISPEP 5 ASP A 360 ARG A 361 0 2.26
CISPEP 6 ASN B 55 PRO B 56 0 3.70
CISPEP 7 MET B 73 ASP B 74 0 0.14
CISPEP 8 ASN B 252 PRO B 253 0 -0.20
CISPEP 9 ARG B 342 PRO B 343 0 5.99
CRYST1 281.728 40.431 95.076 90.00 103.32 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.003550 0.000000 0.000840 0.00000
SCALE2 0.000000 0.024733 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010809 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
