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HEADER CELL ADHESION 21-JUL-17 5OJK
TITLE CRYSTAL STRUCTURE OF THE HUMAN NEUROLIGIN 1 CHOLINESTERASE DOMAIN
TITLE 2 CONTAINING SPLICED SEQUENCE B (SSB) (NL1(-A+B))
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROLIGIN-1,NEUROLIGIN-1;
COMPND 3 CHAIN: A, B;
COMPND 4 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: NLGN1, KIAA1070;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-/-;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHLSEC
KEYWDS NEUROLIGIN-NEUREXIN, SYNAPTIC ORGANIZER PROTEIN, SPLICED SEQUENCE B,
KEYWDS 2 CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.E.ELEGHEERT,A.R.ARICESCU
REVDAT 1 23-AUG-17 5OJK 0
JRNL AUTH J.ELEGHEERT,V.CVETKOVSKA,A.J.CLAYTON,C.HEROVEN,
JRNL AUTH 2 K.M.VENNEKENS,S.N.SMUKOWSKI,M.C.REGAN,W.JIA,A.C.SMITH,
JRNL AUTH 3 H.FURUKAWA,J.N.SAVAS,J.DE WIT,J.BEGBIE,A.M.CRAIG,
JRNL AUTH 4 A.R.ARICESCU
JRNL TITL STRUCTURAL MECHANISM FOR MODULATION OF SYNAPTIC
JRNL TITL 2 NEUROLIGIN-NEUREXIN SIGNALING BY MDGA PROTEINS
JRNL REF NEURON V. 95 896 2017
JRNL REFN ISSN 0896-6273
JRNL DOI 10.1016/J.NEURON.2017.07.040
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_2044)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 40739
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.238
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920
REMARK 3 FREE R VALUE TEST SET COUNT : 2005
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 51.7126 - 6.1428 0.92 2826 158 0.2366 0.2718
REMARK 3 2 6.1428 - 4.8769 0.95 2788 144 0.2128 0.2473
REMARK 3 3 4.8769 - 4.2608 0.95 2767 140 0.1921 0.2152
REMARK 3 4 4.2608 - 3.8713 0.96 2745 135 0.2057 0.2605
REMARK 3 5 3.8713 - 3.5939 0.97 2779 136 0.2183 0.2856
REMARK 3 6 3.5939 - 3.3821 0.97 2746 152 0.2425 0.2592
REMARK 3 7 3.3821 - 3.2127 0.97 2765 135 0.2437 0.2943
REMARK 3 8 3.2127 - 3.0729 0.97 2749 141 0.2548 0.3151
REMARK 3 9 3.0729 - 2.9546 0.98 2767 146 0.2555 0.2965
REMARK 3 10 2.9546 - 2.8527 0.97 2773 139 0.2573 0.3356
REMARK 3 11 2.8527 - 2.7635 0.98 2735 148 0.2794 0.3133
REMARK 3 12 2.7635 - 2.6845 0.98 2762 144 0.2939 0.3436
REMARK 3 13 2.6845 - 2.6138 0.98 2712 147 0.3209 0.3438
REMARK 3 14 2.6138 - 2.5501 0.98 2820 140 0.3331 0.3658
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 0.90
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.460
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 8714
REMARK 3 ANGLE : 0.782 11891
REMARK 3 CHIRALITY : 0.036 1296
REMARK 3 PLANARITY : 0.003 1549
REMARK 3 DIHEDRAL : 10.509 5109
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 5OJK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1200005899.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JAN-13
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96860
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40826
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 51.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: PHASER
REMARK 200 STARTING MODEL: 3BIX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M KSCN, 0.1M BIS-TRIS PROPANE PH
REMARK 280 8.5, 20% W/V PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 X,-Y,-Z
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.02500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 107.17000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.02500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 107.17000
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 TOTAL BURIED SURFACE AREA: 3300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 13.0 KCAL/MOL
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 852 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 GLU A 43
REMARK 465 THR A 44
REMARK 465 GLY A 45
REMARK 465 GLN A 46
REMARK 465 LYS A 47
REMARK 465 LEU A 48
REMARK 465 ASP A 49
REMARK 465 ASP A 50
REMARK 465 VAL A 51
REMARK 465 GLY A 124
REMARK 465 GLU A 180
REMARK 465 ASP A 181
REMARK 465 ASP A 182
REMARK 465 ILE A 183
REMARK 465 ARG A 184
REMARK 465 ASP A 185
REMARK 465 SER A 186
REMARK 465 GLU A 444
REMARK 465 VAL A 573
REMARK 465 PRO A 574
REMARK 465 GLN A 575
REMARK 465 ASP A 576
REMARK 465 THR A 577
REMARK 465 LYS A 578
REMARK 465 PHE A 579
REMARK 465 ILE A 580
REMARK 465 HIS A 581
REMARK 465 THR A 582
REMARK 465 LYS A 583
REMARK 465 PRO A 584
REMARK 465 ASN A 585
REMARK 465 ARG A 586
REMARK 465 PHE A 587
REMARK 465 GLU A 588
REMARK 465 GLU A 589
REMARK 465 ASN A 632
REMARK 465 LEU A 633
REMARK 465 ASN A 634
REMARK 465 ASP A 635
REMARK 465 ARG A 636
REMARK 465 THR A 637
REMARK 465 LYS A 638
REMARK 465 HIS A 639
REMARK 465 HIS A 640
REMARK 465 HIS A 641
REMARK 465 HIS A 642
REMARK 465 HIS A 643
REMARK 465 HIS A 644
REMARK 465 GLU B 43
REMARK 465 THR B 44
REMARK 465 GLY B 45
REMARK 465 GLN B 46
REMARK 465 LYS B 47
REMARK 465 LEU B 48
REMARK 465 ASP B 49
REMARK 465 ASP B 50
REMARK 465 VAL B 51
REMARK 465 GLY B 124
REMARK 465 GLU B 180
REMARK 465 ASP B 181
REMARK 465 ASP B 182
REMARK 465 ILE B 183
REMARK 465 ARG B 184
REMARK 465 ASP B 185
REMARK 465 SER B 186
REMARK 465 GLY B 187
REMARK 465 GLU B 444
REMARK 465 GLN B 575
REMARK 465 ASP B 576
REMARK 465 THR B 577
REMARK 465 LYS B 578
REMARK 465 PHE B 579
REMARK 465 ILE B 580
REMARK 465 HIS B 581
REMARK 465 THR B 582
REMARK 465 LYS B 583
REMARK 465 PRO B 584
REMARK 465 ASN B 585
REMARK 465 ARG B 586
REMARK 465 PHE B 587
REMARK 465 GLU B 588
REMARK 465 GLU B 589
REMARK 465 HIS B 631
REMARK 465 ASN B 632
REMARK 465 LEU B 633
REMARK 465 ASN B 634
REMARK 465 ASP B 635
REMARK 465 ARG B 636
REMARK 465 THR B 637
REMARK 465 LYS B 638
REMARK 465 HIS B 639
REMARK 465 HIS B 640
REMARK 465 HIS B 641
REMARK 465 HIS B 642
REMARK 465 HIS B 643
REMARK 465 HIS B 644
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 125 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 126 CG CD1 CD2
REMARK 470 TYR A 442 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 446 CG CD CE NZ
REMARK 470 ARG A 450 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 598 CG CD CE NZ
REMARK 470 LYS A 608 CG CD CE NZ
REMARK 470 ASP B 123 CG OD1 OD2
REMARK 470 ARG B 125 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 126 CG CD1 CD2
REMARK 470 TYR B 442 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 446 CG CD CE NZ
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 O ASN A 71 O HOH A 801 2.15
REMARK 500 NH1 ARG B 331 O VAL B 341 2.19
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 OD2 ASP A 152 NH2 ARG B 297 4655 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 ASP A 106 -150.18 -103.27
REMARK 500 ALA A 110 73.05 -112.86
REMARK 500 TYR A 201 -7.34 73.71
REMARK 500 ASP A 380 -79.90 -127.39
REMARK 500 TYR A 457 43.14 -107.07
REMARK 500 TRP A 482 -52.87 -121.36
REMARK 500 PRO A 499 104.01 -56.21
REMARK 500 ALA A 520 109.59 -57.18
REMARK 500 LYS A 612 -158.54 -111.71
REMARK 500 ASP B 106 -150.74 -101.25
REMARK 500 ALA B 110 73.87 -111.95
REMARK 500 PRO B 127 87.70 -69.06
REMARK 500 TYR B 201 -7.96 73.74
REMARK 500 ASP B 380 -78.53 -129.30
REMARK 500 TYR B 457 41.73 -107.36
REMARK 500 TRP B 482 -52.73 -121.11
REMARK 500 PRO B 499 103.75 -56.41
REMARK 500 ALA B 520 109.60 -56.71
REMARK 500 PHE B 541 79.84 -115.77
REMARK 500 PRO B 569 0.06 -66.66
REMARK 500 LYS B 612 -158.74 -111.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 854 DISTANCE = 5.90 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 701 bound
REMARK 800 to ASN A 109
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 701 bound
REMARK 800 to ASN B 109
DBREF 5OJK A 46 181 UNP Q8N2Q7 NLGN1_HUMAN 46 164
DBREF 5OJK A 182 635 UNP Q8N2Q7 NLGN1_HUMAN 182 635
DBREF 5OJK B 46 181 UNP Q8N2Q7 NLGN1_HUMAN 46 164
DBREF 5OJK B 182 635 UNP Q8N2Q7 NLGN1_HUMAN 182 635
SEQADV 5OJK GLU A 43 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK THR A 44 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK GLY A 45 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK ARG A 636 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK THR A 637 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK LYS A 638 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK HIS A 639 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK HIS A 640 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK HIS A 641 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK HIS A 642 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK HIS A 643 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK HIS A 644 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK GLU B 43 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK THR B 44 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK GLY B 45 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK ARG B 636 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK THR B 637 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK LYS B 638 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK HIS B 639 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK HIS B 640 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK HIS B 641 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK HIS B 642 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK HIS B 643 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJK HIS B 644 UNP Q8N2Q7 EXPRESSION TAG
SEQRES 1 A 585 GLU THR GLY GLN LYS LEU ASP ASP VAL ASP PRO LEU VAL
SEQRES 2 A 585 ALA THR ASN PHE GLY LYS ILE ARG GLY ILE LYS LYS GLU
SEQRES 3 A 585 LEU ASN ASN GLU ILE LEU GLY PRO VAL ILE GLN PHE LEU
SEQRES 4 A 585 GLY VAL PRO TYR ALA ALA PRO PRO THR GLY GLU ARG ARG
SEQRES 5 A 585 PHE GLN PRO PRO GLU PRO PRO SER PRO TRP SER ASP ILE
SEQRES 6 A 585 ARG ASN ALA THR GLN PHE ALA PRO VAL CYS PRO GLN ASN
SEQRES 7 A 585 ILE ILE ASP GLY ARG LEU PRO GLU VAL MET LEU PRO VAL
SEQRES 8 A 585 TRP PHE THR ASN ASN LEU ASP VAL VAL SER SER TYR VAL
SEQRES 9 A 585 GLN ASP GLN SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES 10 A 585 VAL PRO THR GLU ASP ASP ILE ARG ASP SER GLY GLY PRO
SEQRES 11 A 585 LYS PRO VAL MET VAL TYR ILE HIS GLY GLY SER TYR MET
SEQRES 12 A 585 GLU GLY THR GLY ASN LEU TYR ASP GLY SER VAL LEU ALA
SEQRES 13 A 585 SER TYR GLY ASN VAL ILE VAL ILE THR VAL ASN TYR ARG
SEQRES 14 A 585 LEU GLY VAL LEU GLY PHE LEU SER THR GLY ASP GLN ALA
SEQRES 15 A 585 ALA LYS GLY ASN TYR GLY LEU LEU ASP LEU ILE GLN ALA
SEQRES 16 A 585 LEU ARG TRP THR SER GLU ASN ILE GLY PHE PHE GLY GLY
SEQRES 17 A 585 ASP PRO LEU ARG ILE THR VAL PHE GLY SER GLY ALA GLY
SEQRES 18 A 585 GLY SER CYS VAL ASN LEU LEU THR LEU SER HIS TYR SER
SEQRES 19 A 585 GLU GLY ASN ARG TRP SER ASN SER THR LYS GLY LEU PHE
SEQRES 20 A 585 GLN ARG ALA ILE ALA GLN SER GLY THR ALA LEU SER SER
SEQRES 21 A 585 TRP ALA VAL SER PHE GLN PRO ALA LYS TYR ALA ARG MET
SEQRES 22 A 585 LEU ALA THR LYS VAL GLY CYS ASN VAL SER ASP THR VAL
SEQRES 23 A 585 GLU LEU VAL GLU CYS LEU GLN LYS LYS PRO TYR LYS GLU
SEQRES 24 A 585 LEU VAL ASP GLN ASP ILE GLN PRO ALA ARG TYR HIS ILE
SEQRES 25 A 585 ALA PHE GLY PRO VAL ILE ASP GLY ASP VAL ILE PRO ASP
SEQRES 26 A 585 ASP PRO GLN ILE LEU MET GLU GLN GLY GLU PHE LEU ASN
SEQRES 27 A 585 TYR ASP ILE MET LEU GLY VAL ASN GLN GLY GLU GLY LEU
SEQRES 28 A 585 LYS PHE VAL GLU ASN ILE VAL ASP SER ASP ASP GLY ILE
SEQRES 29 A 585 SER ALA SER ASP PHE ASP PHE ALA VAL SER ASN PHE VAL
SEQRES 30 A 585 ASP ASN LEU TYR GLY TYR PRO GLU GLY LYS ASP VAL LEU
SEQRES 31 A 585 ARG GLU THR ILE LYS PHE MET TYR THR ASP TRP ALA ASP
SEQRES 32 A 585 ARG HIS ASN PRO GLU THR ARG ARG LYS THR LEU LEU ALA
SEQRES 33 A 585 LEU PHE THR ASP HIS GLN TRP VAL ALA PRO ALA VAL ALA
SEQRES 34 A 585 THR ALA ASP LEU HIS SER ASN PHE GLY SER PRO THR TYR
SEQRES 35 A 585 PHE TYR ALA PHE TYR HIS HIS CYS GLN THR ASP GLN VAL
SEQRES 36 A 585 PRO ALA TRP ALA ASP ALA ALA HIS GLY ASP GLU VAL PRO
SEQRES 37 A 585 TYR VAL LEU GLY ILE PRO MET ILE GLY PRO THR GLU LEU
SEQRES 38 A 585 PHE PRO CYS ASN PHE SER LYS ASN ASP VAL MET LEU SER
SEQRES 39 A 585 ALA VAL VAL MET THR TYR TRP THR ASN PHE ALA LYS THR
SEQRES 40 A 585 GLY ASP PRO ASN GLN PRO VAL PRO GLN ASP THR LYS PHE
SEQRES 41 A 585 ILE HIS THR LYS PRO ASN ARG PHE GLU GLU VAL ALA TRP
SEQRES 42 A 585 THR ARG TYR SER GLN LYS ASP GLN LEU TYR LEU HIS ILE
SEQRES 43 A 585 GLY LEU LYS PRO ARG VAL LYS GLU HIS TYR ARG ALA ASN
SEQRES 44 A 585 LYS VAL ASN LEU TRP LEU GLU LEU VAL PRO HIS LEU HIS
SEQRES 45 A 585 ASN LEU ASN ASP ARG THR LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 585 GLU THR GLY GLN LYS LEU ASP ASP VAL ASP PRO LEU VAL
SEQRES 2 B 585 ALA THR ASN PHE GLY LYS ILE ARG GLY ILE LYS LYS GLU
SEQRES 3 B 585 LEU ASN ASN GLU ILE LEU GLY PRO VAL ILE GLN PHE LEU
SEQRES 4 B 585 GLY VAL PRO TYR ALA ALA PRO PRO THR GLY GLU ARG ARG
SEQRES 5 B 585 PHE GLN PRO PRO GLU PRO PRO SER PRO TRP SER ASP ILE
SEQRES 6 B 585 ARG ASN ALA THR GLN PHE ALA PRO VAL CYS PRO GLN ASN
SEQRES 7 B 585 ILE ILE ASP GLY ARG LEU PRO GLU VAL MET LEU PRO VAL
SEQRES 8 B 585 TRP PHE THR ASN ASN LEU ASP VAL VAL SER SER TYR VAL
SEQRES 9 B 585 GLN ASP GLN SER GLU ASP CYS LEU TYR LEU ASN ILE TYR
SEQRES 10 B 585 VAL PRO THR GLU ASP ASP ILE ARG ASP SER GLY GLY PRO
SEQRES 11 B 585 LYS PRO VAL MET VAL TYR ILE HIS GLY GLY SER TYR MET
SEQRES 12 B 585 GLU GLY THR GLY ASN LEU TYR ASP GLY SER VAL LEU ALA
SEQRES 13 B 585 SER TYR GLY ASN VAL ILE VAL ILE THR VAL ASN TYR ARG
SEQRES 14 B 585 LEU GLY VAL LEU GLY PHE LEU SER THR GLY ASP GLN ALA
SEQRES 15 B 585 ALA LYS GLY ASN TYR GLY LEU LEU ASP LEU ILE GLN ALA
SEQRES 16 B 585 LEU ARG TRP THR SER GLU ASN ILE GLY PHE PHE GLY GLY
SEQRES 17 B 585 ASP PRO LEU ARG ILE THR VAL PHE GLY SER GLY ALA GLY
SEQRES 18 B 585 GLY SER CYS VAL ASN LEU LEU THR LEU SER HIS TYR SER
SEQRES 19 B 585 GLU GLY ASN ARG TRP SER ASN SER THR LYS GLY LEU PHE
SEQRES 20 B 585 GLN ARG ALA ILE ALA GLN SER GLY THR ALA LEU SER SER
SEQRES 21 B 585 TRP ALA VAL SER PHE GLN PRO ALA LYS TYR ALA ARG MET
SEQRES 22 B 585 LEU ALA THR LYS VAL GLY CYS ASN VAL SER ASP THR VAL
SEQRES 23 B 585 GLU LEU VAL GLU CYS LEU GLN LYS LYS PRO TYR LYS GLU
SEQRES 24 B 585 LEU VAL ASP GLN ASP ILE GLN PRO ALA ARG TYR HIS ILE
SEQRES 25 B 585 ALA PHE GLY PRO VAL ILE ASP GLY ASP VAL ILE PRO ASP
SEQRES 26 B 585 ASP PRO GLN ILE LEU MET GLU GLN GLY GLU PHE LEU ASN
SEQRES 27 B 585 TYR ASP ILE MET LEU GLY VAL ASN GLN GLY GLU GLY LEU
SEQRES 28 B 585 LYS PHE VAL GLU ASN ILE VAL ASP SER ASP ASP GLY ILE
SEQRES 29 B 585 SER ALA SER ASP PHE ASP PHE ALA VAL SER ASN PHE VAL
SEQRES 30 B 585 ASP ASN LEU TYR GLY TYR PRO GLU GLY LYS ASP VAL LEU
SEQRES 31 B 585 ARG GLU THR ILE LYS PHE MET TYR THR ASP TRP ALA ASP
SEQRES 32 B 585 ARG HIS ASN PRO GLU THR ARG ARG LYS THR LEU LEU ALA
SEQRES 33 B 585 LEU PHE THR ASP HIS GLN TRP VAL ALA PRO ALA VAL ALA
SEQRES 34 B 585 THR ALA ASP LEU HIS SER ASN PHE GLY SER PRO THR TYR
SEQRES 35 B 585 PHE TYR ALA PHE TYR HIS HIS CYS GLN THR ASP GLN VAL
SEQRES 36 B 585 PRO ALA TRP ALA ASP ALA ALA HIS GLY ASP GLU VAL PRO
SEQRES 37 B 585 TYR VAL LEU GLY ILE PRO MET ILE GLY PRO THR GLU LEU
SEQRES 38 B 585 PHE PRO CYS ASN PHE SER LYS ASN ASP VAL MET LEU SER
SEQRES 39 B 585 ALA VAL VAL MET THR TYR TRP THR ASN PHE ALA LYS THR
SEQRES 40 B 585 GLY ASP PRO ASN GLN PRO VAL PRO GLN ASP THR LYS PHE
SEQRES 41 B 585 ILE HIS THR LYS PRO ASN ARG PHE GLU GLU VAL ALA TRP
SEQRES 42 B 585 THR ARG TYR SER GLN LYS ASP GLN LEU TYR LEU HIS ILE
SEQRES 43 B 585 GLY LEU LYS PRO ARG VAL LYS GLU HIS TYR ARG ALA ASN
SEQRES 44 B 585 LYS VAL ASN LEU TRP LEU GLU LEU VAL PRO HIS LEU HIS
SEQRES 45 B 585 ASN LEU ASN ASP ARG THR LYS HIS HIS HIS HIS HIS HIS
HET NAG A 701 14
HET PGE A 702 10
HET PGE A 703 10
HET NAG B 701 14
HET PGE B 702 10
HET PGE B 703 10
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM PGE TRIETHYLENE GLYCOL
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 4 PGE 4(C6 H14 O4)
FORMUL 9 HOH *109(H2 O)
HELIX 1 AA1 THR A 90 ARG A 94 5 5
HELIX 2 AA2 PRO A 132 ASN A 138 1 7
HELIX 3 AA3 ASN A 138 TYR A 145 1 8
HELIX 4 AA4 THR A 205 TYR A 209 5 5
HELIX 5 AA5 GLY A 211 ASN A 219 1 9
HELIX 6 AA6 LEU A 229 LEU A 235 1 7
HELIX 7 AA7 ASN A 245 ILE A 262 1 18
HELIX 8 AA8 GLY A 263 PHE A 265 5 3
HELIX 9 AA9 GLY A 278 LEU A 289 1 12
HELIX 10 AB1 SER A 290 GLU A 294 5 5
HELIX 11 AB2 GLN A 325 VAL A 337 1 13
HELIX 12 AB3 ASP A 343 GLN A 352 1 10
HELIX 13 AB4 PRO A 355 ASP A 361 1 7
HELIX 14 AB5 ASP A 385 GLN A 392 1 8
HELIX 15 AB6 GLY A 409 GLU A 414 1 6
HELIX 16 AB7 SER A 424 TYR A 440 1 17
HELIX 17 AB8 LYS A 446 TYR A 457 1 12
HELIX 18 AB9 ASP A 459 ARG A 463 5 5
HELIX 19 AC1 ASN A 465 TRP A 482 1 18
HELIX 20 AC2 TRP A 482 PHE A 496 1 15
HELIX 21 AC3 GLU A 525 GLY A 531 1 7
HELIX 22 AC4 GLY A 531 GLY A 536 1 6
HELIX 23 AC5 SER A 546 GLY A 567 1 22
HELIX 24 AC6 ARG A 616 GLU A 625 1 10
HELIX 25 AC7 GLU A 625 LEU A 630 1 6
HELIX 26 AC8 THR B 90 ARG B 94 5 5
HELIX 27 AC9 PRO B 132 ASN B 138 1 7
HELIX 28 AD1 ASN B 138 TYR B 145 1 8
HELIX 29 AD2 THR B 205 TYR B 209 5 5
HELIX 30 AD3 GLY B 211 ASN B 219 1 9
HELIX 31 AD4 LEU B 229 LEU B 235 1 7
HELIX 32 AD5 ASN B 245 ILE B 262 1 18
HELIX 33 AD6 GLY B 263 PHE B 265 5 3
HELIX 34 AD7 GLY B 278 LEU B 289 1 12
HELIX 35 AD8 SER B 290 GLU B 294 5 5
HELIX 36 AD9 GLN B 325 VAL B 337 1 13
HELIX 37 AE1 ASP B 343 GLN B 352 1 10
HELIX 38 AE2 PRO B 355 ASP B 361 1 7
HELIX 39 AE3 ASP B 385 GLN B 392 1 8
HELIX 40 AE4 GLY B 409 GLU B 414 1 6
HELIX 41 AE5 SER B 424 TYR B 440 1 17
HELIX 42 AE6 LYS B 446 TYR B 457 1 12
HELIX 43 AE7 ASP B 459 ARG B 463 5 5
HELIX 44 AE8 ASN B 465 TRP B 482 1 18
HELIX 45 AE9 TRP B 482 PHE B 496 1 15
HELIX 46 AF1 GLU B 525 GLY B 531 1 7
HELIX 47 AF2 GLY B 531 GLY B 536 1 6
HELIX 48 AF3 SER B 546 GLY B 567 1 22
HELIX 49 AF4 ARG B 616 GLU B 625 1 10
HELIX 50 AF5 GLU B 625 LEU B 630 1 6
SHEET 1 AA1 3 LEU A 54 THR A 57 0
SHEET 2 AA1 3 GLY A 60 ARG A 63 -1 O ILE A 62 N VAL A 55
SHEET 3 AA1 3 ILE A 107 ASN A 109 1 O ARG A 108 N LYS A 61
SHEET 1 AA211 ILE A 65 LYS A 67 0
SHEET 2 AA211 VAL A 77 PRO A 84 -1 O GLN A 79 N ILE A 65
SHEET 3 AA211 TYR A 155 VAL A 160 -1 O VAL A 160 N ILE A 78
SHEET 4 AA211 ILE A 221 VAL A 225 -1 O THR A 224 N ASN A 157
SHEET 5 AA211 LYS A 190 TYR A 195 1 N TYR A 195 O ILE A 223
SHEET 6 AA211 GLY A 267 SER A 277 1 O THR A 273 N VAL A 192
SHEET 7 AA211 ARG A 308 GLN A 312 1 O GLN A 312 N GLY A 276
SHEET 8 AA211 ASP A 399 ASN A 405 1 O ASP A 399 N ALA A 309
SHEET 9 AA211 THR A 500 PHE A 505 1 O PHE A 505 N VAL A 404
SHEET 10 AA211 LEU A 601 ILE A 605 1 O LEU A 603 N PHE A 502
SHEET 11 AA211 ARG A 610 GLU A 613 -1 O ARG A 610 N HIS A 604
SHEET 1 AA3 3 LEU B 54 THR B 57 0
SHEET 2 AA3 3 GLY B 60 ARG B 63 -1 O ILE B 62 N VAL B 55
SHEET 3 AA3 3 ILE B 107 ASN B 109 1 O ARG B 108 N LYS B 61
SHEET 1 AA411 ILE B 65 LYS B 67 0
SHEET 2 AA411 VAL B 77 PRO B 84 -1 O GLN B 79 N ILE B 65
SHEET 3 AA411 TYR B 155 VAL B 160 -1 O VAL B 160 N ILE B 78
SHEET 4 AA411 ILE B 221 VAL B 225 -1 O THR B 224 N ASN B 157
SHEET 5 AA411 LYS B 190 TYR B 195 1 N TYR B 195 O ILE B 223
SHEET 6 AA411 GLY B 267 SER B 277 1 O THR B 273 N VAL B 192
SHEET 7 AA411 ARG B 308 GLN B 312 1 O GLN B 312 N GLY B 276
SHEET 8 AA411 ASP B 399 ASN B 405 1 O ASP B 399 N ALA B 309
SHEET 9 AA411 THR B 500 PHE B 505 1 O PHE B 505 N VAL B 404
SHEET 10 AA411 LEU B 601 ILE B 605 1 O LEU B 603 N PHE B 502
SHEET 11 AA411 ARG B 610 GLU B 613 -1 O ARG B 610 N HIS B 604
SSBOND 1 CYS A 117 CYS A 153 1555 1555 2.03
SSBOND 2 CYS A 339 CYS A 350 1555 1555 2.03
SSBOND 3 CYS A 509 CYS A 543 1555 1555 2.03
SSBOND 4 CYS B 117 CYS B 153 1555 1555 2.03
SSBOND 5 CYS B 339 CYS B 350 1555 1555 2.03
SSBOND 6 CYS B 509 CYS B 543 1555 1555 2.03
LINK ND2 ASN A 109 C1 NAG A 701 1555 1555 1.44
LINK ND2 ASN B 109 C1 NAG B 701 1555 1555 1.44
CISPEP 1 VAL B 573 PRO B 574 0 2.36
SITE 1 AC1 2 GLN A 352 LYS A 353
SITE 1 AC2 2 GLY A 238 ILE A 377
SITE 1 AC3 3 TRP A 298 GLN B 352 LYS B 353
SITE 1 AC4 5 SER B 236 GLY B 238 LYS B 243 ILE B 377
SITE 2 AC4 5 ASP B 378
SITE 1 AC5 3 ARG A 63 ASN A 109 GLN B 240
SITE 1 AC6 3 GLN A 240 ARG B 63 ASN B 109
CRYST1 49.570 118.050 214.340 90.00 90.00 90.00 P 2 21 21 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 0.020173 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008471 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004665 0.00000
TER 4200 HIS A 631
TER 8408 LEU B 630
MASTER 443 0 6 50 28 0 7 6 8564 2 82 90
END |